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P0AGA2

- SECY_ECOLI

UniProt

P0AGA2 - SECY_ECOLI

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Protein
Protein translocase subunit SecY
Gene
secY, prlA, b3300, JW3262
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently. SecY is required to insert newly synthesized SecY into the inner membrane. Overexpression of some hybrid proteins has been thought to jam the protein secretion apparatus resulting in cell death; while this may be true, overexpression also results in FtsH-mediated degradation of SecY.UniRule annotation

GO - Molecular functioni

  1. protein bindingInferred from physical interactioni PubMed 18761620PubMed 9111035 Source: IntAct
Complete GO annotation...

GO - Biological processi

  1. intracellular protein transmembrane transportInferred from mutant phenotypei PubMed 2254269 Source: EcoliWiki
  2. intracellular protein transportInferred from mutant phenotypei PubMed 2254269 Source: EcoliWiki
  3. protein targetingInferred from electronic annotationi Source: UniProtKB-HAMAP
  4. protein transport by the Sec complexInferred from direct assayi PubMed 2167176 Source: EcoCyc
Complete GO annotation...

Keywords - Biological processi

Protein transport, Translocation, Transport

Enzyme and pathway databases

BioCyciEcoCyc:SECY.
ECOL316407:JW3262-MONOMER.

Protein family/group databases

TCDBi3.A.5.1.1. the general secretory pathway (sec) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein translocase subunit SecY
Gene namesi
Name:secY
Synonyms:prlA
Ordered Locus Names:b3300, JW3262
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10766. secY.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2222Cytoplasmic Inferred
Add
BLAST
Transmembranei23 – 3513Helical; Name=1; Inferred
Add
BLAST
Topological domaini36 – 6025Periplasmic By similarity
Add
BLAST
Transmembranei61 – 9636Discontinuously helical; Name=2; By similarity
Add
BLAST
Intramembranei61 – 7010Helical; Name=Helix 2A; Inferred
Intramembranei71 – 766 Inferred
Intramembranei77 – 9620Helical; Name=Helix 2B; Inferred
Add
BLAST
Topological domaini97 – 11519Cytoplasmic Inferred
Add
BLAST
Transmembranei116 – 13116Helical; Name=3; Inferred
Add
BLAST
Topological domaini132 – 16433Periplasmic Inferred
Add
BLAST
Transmembranei165 – 17814Helical; Name=4; Inferred
Add
BLAST
Topological domaini179 – 1835Cytoplasmic Inferred
Transmembranei184 – 20017Helical; Name=5; Inferred
Add
BLAST
Topological domaini201 – 22323Periplasmic Inferred
Add
BLAST
Transmembranei224 – 23714Helical; Name=6; Inferred
Add
BLAST
Topological domaini238 – 27336Cytoplasmic Inferred
Add
BLAST
Transmembranei274 – 28714Helical; Name=7; Inferred
Add
BLAST
Topological domaini288 – 31326Periplasmic Inferred
Add
BLAST
Transmembranei314 – 32916Helical; Name=8; Inferred
Add
BLAST
Topological domaini330 – 38051Cytoplasmic Inferred
Add
BLAST
Transmembranei381 – 39515Helical; Name=9; Inferred
Add
BLAST
Topological domaini396 – 3961Periplasmic Inferred
Transmembranei397 – 41317Helical; Name=10; Inferred
Add
BLAST
Topological domaini414 – 44330Cytoplasmic Inferred
Add
BLAST

GO - Cellular componenti

  1. integral component of membraneInferred from direct assayi PubMed 3004955 Source: EcoliWiki
  2. integral component of plasma membraneInferred from direct assayi PubMed 2538820 Source: EcoCyc
  3. intracellularInferred from mutant phenotypei PubMed 2254269 Source: GOC
  4. plasma membraneInferred from direct assayi PubMed 3004955 Source: EcoliWiki
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi40 – 401P → S in secY100; temperature-sensitive.
Mutagenesisi60 – 7415Missing: Some loss of viability, supports protein translocation; strongly suppresses defective and missing signal sequences; transient transmembrane channels open. 2 Publications
Add
BLAST
Mutagenesisi65 – 706Missing: Grows almost as well as wild-type, supports protein translocation; strongly suppresses defective and missing signal sequences; transient transmembrane channels open. 2 Publications
Mutagenesisi67 – 671F → C in prlA3; altered signal sequence interaction, transient channel opening and closing in presence of oxidant; massive ion flux when cross-linked to SecE C-120 mutation. 1 Publication
Mutagenesisi167 – 1671G → E in secY100; temperature-sensitive.
Mutagenesisi240 – 2401G → D in secY24; temperature-sensitive at 42 degrees Celsius, impairs interaction with SecE even at 30 degrees in vitro. 1 Publication
Mutagenesisi282 – 2821S → R in prlA401; altered signal sequence interaction, transient transmembrane channels open.
Mutagenesisi286 – 2861F → Y in prlA4-1; altered signal sequence interaction.
Mutagenesisi287 – 2871P → L in secY161; altered signal sequence interaction.
Mutagenesisi290 – 2901I → T in secY121; altered signal sequence interaction.
Mutagenesisi357 – 3571R → H in secY39; cold-sensitive.
Mutagenesisi363 – 3631A → S in secY40; cold-sensitive.
Mutagenesisi408 – 4081I → N in prlA4-2; altered signal sequence interaction. 1 Publication
Mutagenesisi424 – 44320Missing: No longer complements secY24, a temperature-sensitive secY mutation. 1 Publication
Add
BLAST

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 443443Protein translocase subunit SecYUniRule annotation
PRO_0000131721Add
BLAST

Post-translational modificationi

SecY that is not part of the protein translocation apparatus is degraded by FtsH. Also degraded by FtsH when the SecYEG complex is jammed, or upon treatment with antibiotics that block translation elongation such as chloramphenicol.UniRule annotation

Proteomic databases

PaxDbiP0AGA2.
PRIDEiP0AGA2.

Expressioni

Gene expression databases

GenevestigatoriP0AGA2.

Interactioni

Subunit structurei

Component of the Sec protein translocase complex. Heterotrimer consisting of SecY, SecE and SecG subunits. The heterotrimers can form oligomers, although 1 heterotrimer is thought to be able to translocate proteins. Interacts with the ribosome. Interacts with SecDF-YajC and YidC; YidC interacts with nascent inner membrane proteins after SecY. SecY probably contacts the 23S rRNA and possibly also ribosomal protein L23 during ribosome docking. A single SecY molecule forms the translocating pore, although interaction with SecA may require oligomers.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
secAP104084EBI-761422,EBI-543213

Protein-protein interaction databases

DIPiDIP-59302N.
IntActiP0AGA2. 2 interactions.
STRINGi511145.b3300.

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AKHelectron microscopy14.90B/Y1-436[»]
2AKIelectron microscopy14.90B/Y1-436[»]
3J01electron microscopy-A8-442[»]
3J45electron microscopy9.50y6-440[»]
3J46electron microscopy10.10y6-440[»]
ProteinModelPortaliP0AGA2.
SMRiP0AGA2. Positions 8-442.

Miscellaneous databases

EvolutionaryTraceiP0AGA2.

Family & Domainsi

Sequence similaritiesi

Belongs to the SecY/SEC61-alpha family.

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0201.
HOGENOMiHOG000080585.
KOiK03076.
OMAiAWNVQFY.
OrthoDBiEOG651SWP.
PhylomeDBiP0AGA2.

Family and domain databases

Gene3Di1.10.3370.10. 1 hit.
HAMAPiMF_01465. SecY.
InterProiIPR026593. SecY.
IPR002208. SecY/SEC61-alpha.
IPR023201. SecY_su_dom.
[Graphical view]
PANTHERiPTHR10906. PTHR10906. 1 hit.
PfamiPF00344. SecY. 1 hit.
[Graphical view]
PIRSFiPIRSF004557. SecY. 1 hit.
SUPFAMiSSF103491. SSF103491. 1 hit.
TIGRFAMsiTIGR00967. 3a0501s007. 1 hit.
PROSITEiPS00755. SECY_1. 1 hit.
PS00756. SECY_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0AGA2-1 [UniParc]FASTA

« Hide

MAKQPGLDFQ SAKGGLGELK RRLLFVIGAL IVFRIGSFIP IPGIDAAVLA    50
KLLEQQRGTI IEMFNMFSGG ALSRASIFAL GIMPYISASI IIQLLTVVHP 100
TLAEIKKEGE SGRRKISQYT RYGTLVLAIF QSIGIATGLP NMPGMQGLVI 150
NPGFAFYFTA VVSLVTGTMF LMWLGEQITE RGIGNGISII IFAGIVAGLP 200
PAIAHTIEQA RQGDLHFLVL LLVAVLVFAV TFFVVFVERG QRRIVVNYAK 250
RQQGRRVYAA QSTHLPLKVN MAGVIPAIFA SSIILFPATI ASWFGGGTGW 300
NWLTTISLYL QPGQPLYVLL YASAIIFFCF FYTALVFNPR ETADNLKKSG 350
AFVPGIRPGE QTAKYIDKVM TRLTLVGALY ITFICLIPEF MRDAMKVPFY 400
FGGTSLLIVV VVIMDFMAQV QTLMMSSQYE SALKKANLKG YGR 443
Length:443
Mass (Da):48,512
Last modified:July 21, 1986 - v1
Checksum:i711CA63CD8809763
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X01563 Genomic DNA. Translation: CAA25725.1.
U18997 Genomic DNA. Translation: AAA58097.1.
U00096 Genomic DNA. Translation: AAC76325.1.
AP009048 Genomic DNA. Translation: BAE77991.1.
PIRiQQECSY. A04473.
RefSeqiNP_417759.1. NC_000913.3.
YP_492132.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76325; AAC76325; b3300.
BAE77991; BAE77991; BAE77991.
GeneIDi12934410.
947799.
KEGGiecj:Y75_p3876.
eco:b3300.
PATRICi32122032. VBIEscCol129921_3393.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X01563 Genomic DNA. Translation: CAA25725.1 .
U18997 Genomic DNA. Translation: AAA58097.1 .
U00096 Genomic DNA. Translation: AAC76325.1 .
AP009048 Genomic DNA. Translation: BAE77991.1 .
PIRi QQECSY. A04473.
RefSeqi NP_417759.1. NC_000913.3.
YP_492132.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2AKH electron microscopy 14.90 B/Y 1-436 [» ]
2AKI electron microscopy 14.90 B/Y 1-436 [» ]
3J01 electron microscopy - A 8-442 [» ]
3J45 electron microscopy 9.50 y 6-440 [» ]
3J46 electron microscopy 10.10 y 6-440 [» ]
ProteinModelPortali P0AGA2.
SMRi P0AGA2. Positions 8-442.
ModBasei Search...

Protein-protein interaction databases

DIPi DIP-59302N.
IntActi P0AGA2. 2 interactions.
STRINGi 511145.b3300.

Protein family/group databases

TCDBi 3.A.5.1.1. the general secretory pathway (sec) family.

Proteomic databases

PaxDbi P0AGA2.
PRIDEi P0AGA2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC76325 ; AAC76325 ; b3300 .
BAE77991 ; BAE77991 ; BAE77991 .
GeneIDi 12934410.
947799.
KEGGi ecj:Y75_p3876.
eco:b3300.
PATRICi 32122032. VBIEscCol129921_3393.

Organism-specific databases

EchoBASEi EB0759.
EcoGenei EG10766. secY.

Phylogenomic databases

eggNOGi COG0201.
HOGENOMi HOG000080585.
KOi K03076.
OMAi AWNVQFY.
OrthoDBi EOG651SWP.
PhylomeDBi P0AGA2.

Enzyme and pathway databases

BioCyci EcoCyc:SECY.
ECOL316407:JW3262-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0AGA2.
PROi P0AGA2.

Gene expression databases

Genevestigatori P0AGA2.

Family and domain databases

Gene3Di 1.10.3370.10. 1 hit.
HAMAPi MF_01465. SecY.
InterProi IPR026593. SecY.
IPR002208. SecY/SEC61-alpha.
IPR023201. SecY_su_dom.
[Graphical view ]
PANTHERi PTHR10906. PTHR10906. 1 hit.
Pfami PF00344. SecY. 1 hit.
[Graphical view ]
PIRSFi PIRSF004557. SecY. 1 hit.
SUPFAMi SSF103491. SSF103491. 1 hit.
TIGRFAMsi TIGR00967. 3a0501s007. 1 hit.
PROSITEi PS00755. SECY_1. 1 hit.
PS00756. SECY_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The spc ribosomal protein operon of Escherichia coli: sequence and cotranscription of the ribosomal protein genes and a protein export gene."
    Cerretti D.P., Dean D., Davis G.R., Bedwell D.M., Nomura M.
    Nucleic Acids Res. 11:2599-2616(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. "The complete genome sequence of Escherichia coli K-12."
    Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
    Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "Topology analysis of the SecY protein, an integral membrane protein involved in protein export in Escherichia coli."
    Akiyama Y., Ito K.
    EMBO J. 6:3465-3470(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY.
  5. "Temperature-sensitive sec mutants of Escherichia coli: inhibition of protein export at the permissive temperature."
    Ito K., Hirota Y., Akiyama Y.
    J. Bacteriol. 171:1742-1743(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTANT SECY100.
  6. "Export of Escherichia coli alkaline phosphatase attached to an integral membrane protein, SecY."
    Akiyama Y., Ito K.
    J. Biol. Chem. 264:437-442(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: REQUIRED FOR ITS OWN INSERTION INTO MEMBRANES.
    Strain: K12 / MC4100.
  7. "Characterization of cold-sensitive secY mutants of Escherichia coli."
    Baba T., Jacq A., Brickman E., Beckwith J., Taura T., Ueguchi C., Akiyama Y., Ito K.
    J. Bacteriol. 172:7005-7010(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTANTS SECY39 AND SECY40.
  8. "Novel prlA alleles defective in supporting staphylokinase processing in Escherichia coli."
    Sako T.
    J. Bacteriol. 173:2289-2296(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTANTS SECY121 AND SECY161.
  9. "Biochemical analysis of the biogenesis and function of the Escherichia coli export factor SecY."
    Swidersky U.E., Rienhoefer-Schweer A., Werner P.K., Ernst F., Benson S.A., Hoffschulte H.K., Mueller M.
    Eur. J. Biochem. 207:803-811(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  10. "PrlA suppressor mutations cluster in regions corresponding to three distinct topological domains."
    Osborne R.S., Silhavy T.J.
    EMBO J. 12:3391-3398(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTANTS.
  11. "A cytoplasmic domain is important for the formation of a SecY-SecE translocator complex."
    Baba T., Taura T., Shimoike T., Akiyama Y., Yoshihisa T., Ito K.
    Proc. Natl. Acad. Sci. U.S.A. 91:4539-4543(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF GLY-240.
    Strain: K12 / MC4100.
  12. "The allele-specific synthetic lethality of prlA-prlG double mutants predicts interactive domains of SecY and SecE."
    Flower A.M., Osborne R.S., Silhavy T.J.
    EMBO J. 14:884-893(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTANTS.
  13. "FtsH is required for proteolytic elimination of uncomplexed forms of SecY, an essential protein translocase subunit."
    Kihara A., Akiyama Y., Ito K.
    Proc. Natl. Acad. Sci. U.S.A. 92:4532-4536(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEGRADATION BY FTSH.
  14. "Sec-dependent membrane protein insertion: sequential interaction of nascent FtsQ with SecY and YidC."
    Urbanus M.L., Scotti P.A., Froderberg L., Saaf A., de Gier J.W., Brunner J., Samuelson J.C., Dalbey R.E., Oudega B., Luirink J.
    EMBO Rep. 2:524-529(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FTSQ BEFORE YIDC.
  15. "Global topology analysis of the Escherichia coli inner membrane proteome."
    Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.
    Science 308:1321-1323(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
    Strain: K12 / MG1655 / ATCC 47076.
  16. "Protein translocation is mediated by oligomers of the SecY complex with one SecY copy forming the channel."
    Osborne A.R., Rapoport T.A.
    Cell 129:97-110(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SECA, CHARACTERIZATION OF THE TRANSLOCATING PORE.
  17. "Effects of antibiotics and a proto-oncogene homolog on destruction of protein translocator SecY."
    van Stelten J., Silva F., Belin D., Silhavy T.J.
    Science 325:753-756(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: COMPLEX DEGRADATION.
    Strain: K12 / MC4100.
  18. "Determining the conductance of the SecY protein translocation channel for small molecules."
    Saparov S.M., Erlandson K., Cannon K., Schaletzky J., Schulman S., Rapoport T.A., Pohl P.
    Mol. Cell 26:501-509(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF CHANNEL OPENING, MUTAGENESIS OF 60-ILE--ARG-74; 65-ASN--GLY-70; PHE-67 AND ILE-408.
  19. "The plug domain of the SecY protein stabilizes the closed state of the translocation channel and maintains a membrane seal."
    Li W., Schulman S., Boyd D., Erlandson K., Beckwith J., Rapoport T.A.
    Mol. Cell 26:511-521(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF 60-ILE--ARG-74 AND 65-ASN--GLY-70.
  20. "Lateral opening of a translocon upon entry of protein suggests the mechanism of insertion into membranes."
    Egea P.F., Stroud R.M.
    Proc. Natl. Acad. Sci. U.S.A. 107:17182-17187(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF 424-MET--ARG-443.
    Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
  21. "Structure of the E. coli protein-conducting channel bound to a translating ribosome."
    Mitra K., Schaffitzel C., Shaikh T., Tama F., Jenni S., Brooks C.L. III, Ban N., Frank J.
    Nature 438:318-324(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (14.9 ANGSTROMS) OF 1-436 IN COMPLEX WITH THE RIBOSOME AND A NASCENT POLYPEPTIDE CHAIN.
    Strain: MRE-600.
  22. "Cryo-EM structure of the ribosome-SecYE complex in the membrane environment."
    Frauenfeld J., Gumbart J., Sluis E.O., Funes S., Gartmann M., Beatrix B., Mielke T., Berninghausen O., Becker T., Schulten K., Beckmann R.
    Nat. Struct. Mol. Biol. 18:614-621(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY CRYOELECTRON MICROSCOPY IN COMPLEX WITH THE RIBOSOME AND A NASCENT POLYPEPTIDE CHAIN.
  23. "Structure, function, and biogenesis of SecY, an integral membrane protein involved in protein export."
    Ito K.
    J. Bioenerg. Biomembr. 22:353-367(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  24. "Protein translocation across the bacterial cytoplasmic membrane."
    Driessen A.J., Nouwen N.
    Annu. Rev. Biochem. 77:643-667(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.

Entry nameiSECY_ECOLI
AccessioniPrimary (citable) accession number: P0AGA2
Secondary accession number(s): P03844, Q2M6W5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: June 11, 2014
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene

External Data

Dasty 3

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