SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P0A9A6

- FTSZ_ECOLI

UniProt

P0A9A6 - FTSZ_ECOLI

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here

Protein
Cell division protein FtsZ
Gene
ftsZ, sfiB, sulB, b0095, JW0093
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity. Polymerization and bundle formation is enhanced by CbeA.UniRule annotation

Enzyme regulationi

Formation of the FtsZ ring is inhibited by SulA, MinCD, DicB and toxins CbtA and CptA. Inhibition by toxin CbtA, SulA or DicB overexpression is neutralized by cytoskeleton bundling-enhancing protein CbeA, while inhibition by toxin CptA is neutralized by antitoxin CptB.4 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier
Nucleotide bindingi103 – 1119GTP Reviewed prediction

GO - Molecular functioni

  1. GTP bindingInferred from direct assayi PubMed 1528267PubMed 1528268 Source: EcoliWiki
  2. GTPase activityInferred from direct assayi PubMed 1528267PubMed 1528268 Source: EcoliWiki
  3. identical protein bindingInferred from physical interactioni PubMed 18394147PubMed 19415799PubMed 21216995PubMed 21216997PubMed 22064072PubMed 22515815 Source: IntAct
  4. protein bindingInferred from physical interactioni PubMed 10209756PubMed 10880432PubMed 15774864PubMed 17307852PubMed 17986188PubMed 18186792PubMed 18394147PubMed 19415799PubMed 21216995PubMed 21216997PubMed 22505682PubMed 22515815PubMed 24561554 Source: IntAct
Complete GO annotation...

GO - Biological processi

  1. barrier septum assemblyInferred from electronic annotationi Source: UniProtKB-KW
  2. cell divisionInferred from genetic interactioni PubMed 21317324 Source: CACAO
  3. cytokinesis by binary fissionInferred from electronic annotationi Source: UniProtKB-HAMAP
  4. protein polymerizationInferred from direct assayi PubMed 21321206PubMed 8917533 Source: EcoliWiki
  1. GTPase activityInferred from direct assayi PubMed 1528267PubMed 1528268 Source: EcoliWiki
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Septation

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10347-MONOMER.
ECOL316407:JW0093-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Cell division protein FtsZ
Gene namesi
Name:ftsZ
Synonyms:sfiB, sulB
Ordered Locus Names:b0095, JW0093
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10347. ftsZ.

Subcellular locationi

Cytoplasm
Note: Assembles at midcell at the inner surface of the cytoplasmic membrane.2 Publications

GO - Cellular componenti

  1. cell division siteInferred from direct assayi PubMed 9603865 Source: EcoliWiki
  2. cytoplasmInferred from direct assayi PubMed 1943703 Source: EcoliWiki
  3. protein complexInferred from electronic annotationi Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier
Mutagenesisi1 – 3232Missing: No interaction with MreB or YeeV.
Mutagenesisi33 – 4917Missing: No interaction with CtpA.
Mutagenesisi105 – 1051G → F in FtsZ-84; loss of GTPase-activity and conversion to an ATPase.
Mutagenesisi108 – 1081T → A in FtsZ-Z3; lethal; greatly reduced GTP binding.
Mutagenesisi317 – 38367Missing: No interaction with MreB or CbtA (YeeV).

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier
Chaini1 – 383383Cell division protein FtsZUniRule annotation
PRO_0000114349

Proteomic databases

PaxDbiP0A9A6.
PRIDEiP0A9A6.

2D gel databases

SWISS-2DPAGEiP0A9A6.

Expressioni

Gene expression databases

GenevestigatoriP0A9A6.

Interactioni

Subunit structurei

Homodimer. Polymerizes to form a dynamic ring structure in a strictly GTP-dependent manner. Polymers persist as long as GTP is present and disappear rapidly as soon as it is consumed. Interacts directly with several other division proteins, including FtsA and ZipA. Interacts with polymerization inhibitors SulA, CbtA and CptA. Interacts with MreB and polymerization bundling-enhancing factor CbeA.9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself7EBI-370963,EBI-370963
cbeAP763642EBI-370963,EBI-1126877
ftsAP0ABH06EBI-370963,EBI-550562
ftsEP0A9R72EBI-370963,EBI-550637
rlmNP369793EBI-370963,EBI-559071
zapCP758624EBI-370963,EBI-552519
zapDP366803EBI-370963,EBI-1113728
zipAP771734EBI-370963,EBI-1029213

Protein-protein interaction databases

DIPiDIP-31873N.
IntActiP0A9A6. 59 interactions.
MINTiMINT-8092601.
STRINGi511145.b0095.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier
Helixi374 – 3829

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1F47X-ray1.95A367-383[»]
ProteinModelPortaliP0A9A6.
SMRiP0A9A6. Positions 24-316.

Miscellaneous databases

EvolutionaryTraceiP0A9A6.

Family & Domainsi

Domaini

The central and C-terminal regions are required for dimerization.1 Publication

Sequence similaritiesi

Belongs to the FtsZ family.

Phylogenomic databases

eggNOGiCOG0206.
HOGENOMiHOG000049094.
KOiK03531.
OMAiQIGNGIT.
OrthoDBiEOG6S7XZG.
PhylomeDBiP0A9A6.

Family and domain databases

Gene3Di3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.
HAMAPiMF_00909. FtsZ.
InterProiIPR000158. Cell_div_FtsZ.
IPR020805. Cell_div_FtsZ_CS.
IPR024757. FtsZ_C.
IPR008280. Tub_FtsZ_C.
IPR018316. Tubulin/FtsZ_2-layer-sand-dom.
IPR003008. Tubulin_FtsZ_GTPase.
[Graphical view]
PfamiPF12327. FtsZ_C. 1 hit.
PF00091. Tubulin. 1 hit.
[Graphical view]
PRINTSiPR00423. CELLDVISFTSZ.
SMARTiSM00864. Tubulin. 1 hit.
SM00865. Tubulin_C. 1 hit.
[Graphical view]
SUPFAMiSSF52490. SSF52490. 1 hit.
SSF55307. SSF55307. 1 hit.
TIGRFAMsiTIGR00065. ftsZ. 1 hit.
PROSITEiPS01134. FTSZ_1. 1 hit.
PS01135. FTSZ_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0A9A6-1 [UniParc]FASTA

« Hide

MFEPMELTND AVIKVIGVGG GGGNAVEHMV RERIEGVEFF AVNTDAQALR    50
KTAVGQTIQI GSGITKGLGA GANPEVGRNA ADEDRDALRA ALEGADMVFI 100
AAGMGGGTGT GAAPVVAEVA KDLGILTVAV VTKPFNFEGK KRMAFAEQGI 150
TELSKHVDSL ITIPNDKLLK VLGRGISLLD AFGAANDVLK GAVQGIAELI 200
TRPGLMNVDF ADVRTVMSEM GYAMMGSGVA SGEDRAEEAA EMAISSPLLE 250
DIDLSGARGV LVNITAGFDL RLDEFETVGN TIRAFASDNA TVVIGTSLDP 300
DMNDELRVTV VATGIGMDKR PEITLVTNKQ VQQPVMDRYQ QHGMAPLTQE 350
QKPVAKVVND NAPQTAKEPD YLDIPAFLRK QAD 383
Length:383
Mass (Da):40,324
Last modified:July 19, 2005 - v1
Checksum:iB3A53340367DBBA0
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier
Sequence conflicti32 – 398ERIEGVEF → DALKVLNS in AAA23818. 1 Publication
Sequence conflicti158 – 1581D → N in CAA38872. 1 Publication
Sequence conflicti222 – 2221Y → H in CAA38872. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U00096 Genomic DNA. Translation: AAC73206.1.
AP009048 Genomic DNA. Translation: BAB96663.2.
X55034 Genomic DNA. Translation: CAA38872.1.
K02668 Genomic DNA. Translation: AAA23818.1.
M19211 Genomic DNA. Translation: AAA83848.1.
PIRiCEECZ. G64731.
RefSeqiNP_414637.1. NC_000913.3.
YP_488400.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC73206; AAC73206; b0095.
BAB96663; BAB96663; BAB96663.
GeneIDi12932893.
944786.
KEGGiecj:Y75_p0094.
eco:b0095.
PATRICi32115295. VBIEscCol129921_0099.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U00096 Genomic DNA. Translation: AAC73206.1 .
AP009048 Genomic DNA. Translation: BAB96663.2 .
X55034 Genomic DNA. Translation: CAA38872.1 .
K02668 Genomic DNA. Translation: AAA23818.1 .
M19211 Genomic DNA. Translation: AAA83848.1 .
PIRi CEECZ. G64731.
RefSeqi NP_414637.1. NC_000913.3.
YP_488400.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1F47 X-ray 1.95 A 367-383 [» ]
ProteinModelPortali P0A9A6.
SMRi P0A9A6. Positions 24-316.
ModBasei Search...

Protein-protein interaction databases

DIPi DIP-31873N.
IntActi P0A9A6. 59 interactions.
MINTi MINT-8092601.
STRINGi 511145.b0095.

Chemistry

BindingDBi P0A9A6.
ChEMBLi CHEMBL3999.

2D gel databases

SWISS-2DPAGEi P0A9A6.

Proteomic databases

PaxDbi P0A9A6.
PRIDEi P0A9A6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC73206 ; AAC73206 ; b0095 .
BAB96663 ; BAB96663 ; BAB96663 .
GeneIDi 12932893.
944786.
KEGGi ecj:Y75_p0094.
eco:b0095.
PATRICi 32115295. VBIEscCol129921_0099.

Organism-specific databases

EchoBASEi EB0343.
EcoGenei EG10347. ftsZ.

Phylogenomic databases

eggNOGi COG0206.
HOGENOMi HOG000049094.
KOi K03531.
OMAi QIGNGIT.
OrthoDBi EOG6S7XZG.
PhylomeDBi P0A9A6.

Enzyme and pathway databases

BioCyci EcoCyc:EG10347-MONOMER.
ECOL316407:JW0093-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0A9A6.
PROi P0A9A6.

Gene expression databases

Genevestigatori P0A9A6.

Family and domain databases

Gene3Di 3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.
HAMAPi MF_00909. FtsZ.
InterProi IPR000158. Cell_div_FtsZ.
IPR020805. Cell_div_FtsZ_CS.
IPR024757. FtsZ_C.
IPR008280. Tub_FtsZ_C.
IPR018316. Tubulin/FtsZ_2-layer-sand-dom.
IPR003008. Tubulin_FtsZ_GTPase.
[Graphical view ]
Pfami PF12327. FtsZ_C. 1 hit.
PF00091. Tubulin. 1 hit.
[Graphical view ]
PRINTSi PR00423. CELLDVISFTSZ.
SMARTi SM00864. Tubulin. 1 hit.
SM00865. Tubulin_C. 1 hit.
[Graphical view ]
SUPFAMi SSF52490. SSF52490. 1 hit.
SSF55307. SSF55307. 1 hit.
TIGRFAMsi TIGR00065. ftsZ. 1 hit.
PROSITEi PS01134. FTSZ_1. 1 hit.
PS01135. FTSZ_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publicationsDownload
  1. "The nucleotide sequence of the essential cell-division gene ftsZ of Escherichia coli."
    Yi Q.-M., Lutkenhaus J.
    Gene 36:241-247(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. "Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region."
    Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K., Mizobuchi K., Nakata A.
    Nucleic Acids Res. 20:3305-3308(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12.
  3. "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.
  4. "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], SEQUENCE REVISION TO 158 AND 222.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "DNA sequence and transcriptional organization of essential cell division genes ftsQ and ftsA of Escherichia coli: evidence for overlapping transcriptional units."
    Robinson A.C., Kenan D.J., Hatfull G.F., Sullivan N.F., Spiegelberg R., Donachie W.D.
    J. Bacteriol. 160:546-555(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-39.
  6. "Structure and expression of the cell division genes ftsQ, ftsA and ftsZ."
    Yi Q.-M., Rockenbach S., Ward J.E. Jr., Lutkenhaus J.
    J. Mol. Biol. 184:399-412(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-39.
    Strain: K12.
  7. Frutiger S., Hughes G.J., Pasquali C., Hochstrasser D.F.
    Submitted (FEB-1996) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 1-12.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  8. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
    Link A.J., Robison K., Church G.M.
    Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-12.
    Strain: K12 / EMG2.
  9. "Sequence analysis, transcriptional organization, and insertional mutagenesis of the envA gene of Escherichia coli."
    Beall B., Lutkenhaus J.
    J. Bacteriol. 169:5408-5415(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 377-383.
    Strain: K12.
  10. "FtsZ ring structure associated with division in Escherichia coli."
    Bi E., Lutkenhaus J.
    Nature 354:161-164(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, RING-LIKE STRUCTURE.
  11. "Escherichia coli cell-division gene ftsZ encodes a novel GTP-binding protein."
    Raychaudhuri D., Park J.T.
    Nature 359:251-254(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: GTPASE ACTIVITY.
  12. "The essential bacterial cell-division protein FtsZ is a GTPase."
    de Boer P., Crossley R., Rothfield L.
    Nature 359:254-256(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: GTPASE ACTIVITY.
  13. "Guanine nucleotide-dependent assembly of FtsZ into filaments."
    Mukherjee A., Lutkenhaus J.
    J. Bacteriol. 176:2754-2758(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: GTP-DEPENDENT FILAMENT FORMATION.
  14. "GTP-dependent polymerization of Escherichia coli FtsZ protein to form tubules."
    Bramhill D., Thompson C.M.
    Proc. Natl. Acad. Sci. U.S.A. 91:5813-5817(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: GTP-DEPENDENT FILAMENT FORMATION.
  15. "A point mutation converts Escherichia coli FtsZ septation GTPase to an ATPase."
    Raychaudhuri D., Park J.T.
    J. Biol. Chem. 269:22941-22944(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTANTS.
  16. "Interaction between FtsZ and inhibitors of cell division."
    Huang J., Cao C., Lutkenhaus J.
    J. Bacteriol. 178:5080-5085(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, INTERACTION WITH SULA.
  17. "Colocalization of cell division proteins FtsZ and FtsA to cytoskeletal structures in living Escherichia coli cells by using green fluorescent protein."
    Ma X., Ehrhardt D.W., Margolin W.
    Proc. Natl. Acad. Sci. U.S.A. 93:12998-13003(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH FTSA.
  18. "Dynamic assembly of FtsZ regulated by GTP hydrolysis."
    Mukherjee A., Lutkenhaus J.
    EMBO J. 17:462-469(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, GTPASE ACTIVITY.
  19. "FtsZ dimerization in vivo."
    Di Lallo G., Anderluzzi D., Ghelardini P., Paolozzi L.
    Mol. Microbiol. 32:265-274(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, DOMAIN.
    Strain: K12.
  20. "Rate-limiting guanosine 5'-triphosphate hydrolysis during nucleotide turnover by FtsZ, a prokaryotic tubulin homologue involved in bacterial cell division."
    Romberg L., Mitchison T.J.
    Biochemistry 43:282-288(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, GTPASE ACTIVITY.
  21. "Molecular evolution of FtsZ protein sequences encoded within the genomes of archaea, bacteria, and eukaryota."
    Vaughan S., Wickstead B., Gull K., Addinall S.G.
    J. Mol. Evol. 58:19-29(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHYLOGENETIC STUDY.
  22. "Bacterial cell division and the septal ring."
    Weiss D.S.
    Mol. Microbiol. 54:588-597(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  23. "Interaction between cell division proteins FtsE and FtsZ."
    Corbin B.D., Wang Y., Beuria T.K., Margolin W.
    J. Bacteriol. 189:3026-3035(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FTSE.
    Strain: K12 / MG1655 / ATCC 47076.
  24. "YeeV is an Escherichia coli toxin that inhibits cell division by targeting the cytoskeleton proteins, FtsZ and MreB."
    Tan Q., Awano N., Inouye M.
    Mol. Microbiol. 79:109-118(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, INTERACTION WITH MREB AND CBTA.
    Strain: K12 / BW25113.
  25. "A novel membrane-bound toxin for cell division, CptA (YgfX), inhibits polymerization of cytoskeleton proteins, FtsZ and MreB, in Escherichia coli."
    Masuda H., Tan Q., Awano N., Yamaguchi Y., Inouye M.
    FEMS Microbiol. Lett. 328:174-181(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, INTERACTION WITH CPTA.
    Strain: B / BL21-DE3 and K12 / BW25113.
  26. "YeeU enhances the bundling of cytoskeletal polymers of MreB and FtsZ, antagonizing the CbtA (YeeV) toxicity in Escherichia coli."
    Masuda H., Tan Q., Awano N., Wu K.P., Inouye M.
    Mol. Microbiol. 84:979-989(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, INTERACTION WITH CBEA.
    Strain: K12 / BW25113.
  27. "The bacterial cell-division protein ZipA and its interaction with an FtsZ fragment revealed by X-ray crystallography."
    Mosyak L., Zhang Y., Glasfeld E., Haney S., Stahl M., Seehra J., Somers W.S.
    EMBO J. 19:3179-3191(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 367-383 IN COMPLEX WITH ZIPA.

Entry nameiFTSZ_ECOLI
AccessioniPrimary (citable) accession number: P0A9A6
Secondary accession number(s): P06138, P77857, P78047
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: July 19, 2005
Last modified: June 11, 2014
This is version 87 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, Direct protein sequencing, 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

Similar proteinsi