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P0ABH9

- CLPA_ECOLI

UniProt

P0ABH9 - CLPA_ECOLI

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Protein
ATP-dependent Clp protease ATP-binding subunit ClpA
Gene
clpA, lopD, b0882, JW0866
Organism
Escherichia coli (strain K12)
Status
Reviewed - - Experimental evidence at protein leveli

Functioni

ATP-dependent specificity component of the ClpAP protease. It directs the protease to specific substrates. It has unfoldase activity. The primary function of the ClpA-ClpP complex appears to be the degradation of unfolded or abnormal proteins.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier
Nucleotide bindingi214 – 2218ATP Reviewed prediction
Nucleotide bindingi495 – 5028ATP Reviewed prediction

GO - Molecular functioni

  1. ATP bindingInferred from electronic annotationi Source: UniProtKB-KW
  2. ATP-dependent peptidase activityInferred from electronic annotationi Source: InterPro
  3. protein bindingInferred from physical interactioni PubMed 12235156PubMed 12426582PubMed 15037248PubMed 15690043PubMed 19317833PubMed 24561554PubMed 24627523 Source: IntAct
Complete GO annotation...

GO - Biological processi

  1. proteolysisInferred from direct assayi PubMed 3049606 Source: EcoCyc
  1. ATP-dependent peptidase activityInferred from electronic annotationi Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10156-MONOMER.
ECOL316407:JW0866-MONOMER.
MetaCyc:EG10156-MONOMER.
SABIO-RKiP0ABH9.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent Clp protease ATP-binding subunit ClpA
Gene namesi
Name:clpA
Synonyms:lopD
Ordered Locus Names:b0882, JW0866
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10156. clpA.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier
Chaini1 – 758758ATP-dependent Clp protease ATP-binding subunit ClpA
PRO_0000191079

Proteomic databases

PaxDbiP0ABH9.
PRIDEiP0ABH9.

Expressioni

Gene expression databases

GenevestigatoriP0ABH9.

Interactioni

Subunit structurei

Component of the ClpAP complex composed of six ClpA subunits assembled into a hexameric ring in the presence of ATP, and fourteen ClpP subunits arranged in two heptameric rings. Binds to ClpS.

Binary interactionsi

WithEntry#Exp.IntActNotes
clpSP0A8Q610EBI-546140,EBI-561456
fixXP686462EBI-546140,EBI-1113234

Protein-protein interaction databases

BioGridi850131. 1 interaction.
DIPiDIP-35409N.
IntActiP0ABH9. 75 interactions.
STRINGi511145.b0882.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier
Helixi4 – 2017
Beta strandi22 – 254
Helixi27 – 348
Helixi38 – 469
Helixi51 – 6515
Beta strandi72 – 743
Helixi82 – 9615
Beta strandi97 – 993
Beta strandi101 – 1033
Helixi105 – 1128
Helixi119 – 1268
Helixi131 – 1399
Beta strandi171 – 1733
Helixi176 – 1816
Helixi192 – 20211
Beta strandi204 – 2074
Beta strandi209 – 2135
Helixi220 – 23314
Helixi238 – 2403
Beta strandi244 – 2474
Beta strandi259 – 2613
Helixi263 – 27412
Beta strandi275 – 2784
Beta strandi280 – 2845
Turni285 – 2928
Beta strandi296 – 2983
Helixi300 – 3078
Beta strandi311 – 3133
Beta strandi317 – 3226
Helixi324 – 3285
Helixi329 – 3335
Helixi338 – 3403
Beta strandi341 – 3455
Helixi351 – 36919
Helixi375 – 38814
Helixi396 – 41116
Beta strandi412 – 4143
Helixi423 – 43311
Beta strandi441 – 4444
Helixi445 – 45612
Turni457 – 4593
Helixi464 – 47815
Beta strandi484 – 4863
Beta strandi488 – 4947
Helixi501 – 51212
Beta strandi515 – 5206
Helixi521 – 5233
Beta strandi525 – 5284
Beta strandi531 – 5333
Helixi541 – 5455
Helixi548 – 5558
Beta strandi557 – 5648
Helixi566 – 5683
Helixi571 – 58313
Beta strandi584 – 5885
Turni589 – 5913
Beta strandi592 – 5954
Beta strandi599 – 6057
Helixi629 – 6357
Helixi638 – 6414
Beta strandi645 – 6495
Helixi655 – 67521
Beta strandi678 – 6825
Helixi684 – 69411
Turni697 – 6993
Turni701 – 7033
Helixi704 – 7129
Helixi714 – 7163
Helixi717 – 7226
Turni724 – 7274
Beta strandi729 – 7368
Turni737 – 7404
Beta strandi741 – 7488
Beta strandi750 – 7523

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K6KX-ray1.80A1-143[»]
1KSFX-ray2.60X1-758[»]
1LZWX-ray2.50B1-146[»]
1MBUX-ray2.30A/B1-142[»]
1MBVX-ray3.30A1-142[»]
1MBXX-ray2.25A/B1-142[»]
1MG9X-ray2.30B1-146[»]
1R6BX-ray2.25X1-758[»]
1R6CX-ray2.15X1-143[»]
1R6OX-ray2.25A/B1-143[»]
1R6QX-ray2.35A/B1-143[»]
ProteinModelPortaliP0ABH9.
SMRiP0ABH9. Positions 1-755.

Miscellaneous databases

EvolutionaryTraceiP0ABH9.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier
Regioni169 – 417249I
Regioni421 – 609189II

Sequence similaritiesi

Belongs to the ClpA/ClpB family.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0542.
HOGENOMiHOG000218210.
KOiK03694.
OMAiATDICAD.
OrthoDBiEOG65F8SM.
PhylomeDBiP0ABH9.

Family and domain databases

Gene3Di1.10.1780.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR019489. Clp_ATPase_C.
IPR004176. Clp_N.
IPR013461. ClpA.
IPR001270. ClpA/B.
IPR018368. ClpA/B_CS1.
IPR028299. ClpA/B_CS2.
IPR023150. Dbl_Clp-N.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR11638:SF14. PTHR11638:SF14. 1 hit.
PfamiPF00004. AAA. 1 hit.
PF07724. AAA_2. 1 hit.
PF02861. Clp_N. 1 hit.
PF10431. ClpB_D2-small. 1 hit.
[Graphical view]
PRINTSiPR00300. CLPPROTEASEA.
SMARTiSM00382. AAA. 2 hits.
SM01086. ClpB_D2-small. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
TIGRFAMsiTIGR02639. ClpA. 1 hit.
PROSITEiPS00870. CLPAB_1. 1 hit.
PS00871. CLPAB_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0ABH9-1 [UniParc]FASTA

« Hide

MLNQELELSL NMAFARAREH RHEFMTVEHL LLALLSNPSA REALEACSVD    50
LVALRQELEA FIEQTTPVLP ASEEERDTQP TLSFQRVLQR AVFHVQSSGR 100
NEVTGANVLV AIFSEQESQA AYLLRKHEVS RLDVVNFISH GTRKDEPTQS 150
SDPGSQPNSE EQAGGEERME NFTTNLNQLA RVGGIDPLIG REKELERAIQ 200
VLCRRRKNNP LLVGESGVGK TAIAEGLAWR IVQGDVPEVM ADCTIYSLDI 250
GSLLAGTKYR GDFEKRFKAL LKQLEQDTNS ILFIDEIHTI IGAGAASGGQ 300
VDAANLIKPL LSSGKIRVIG STTYQEFSNI FEKDRALARR FQKIDITEPS 350
IEETVQIING LKPKYEAHHD VRYTAKAVRA AVELAVKYIN DRHLPDKAID 400
VIDEAGARAR LMPVSKRKKT VNVADIESVV ARIARIPEKS VSQSDRDTLK 450
NLGDRLKMLV FGQDKAIEAL TEAIKMARAG LGHEHKPVGS FLFAGPTGVG 500
KTEVTVQLSK ALGIELLRFD MSEYMERHTV SRLIGAPPGY VGFDQGGLLT 550
DAVIKHPHAV LLLDEIEKAH PDVFNILLQV MDNGTLTDNN GRKADFRNVV 600
LVMTTNAGVR ETERKSIGLI HQDNSTDAME EIKKIFTPEF RNRLDNIIWF 650
DHLSTDVIHQ VVDKFIVELQ VQLDQKGVSL EVSQEARNWL AEKGYDRAMG 700
ARPMARVIQD NLKKPLANEL LFGSLVDGGQ VTVALDKEKN ELTYGFQSAQ 750
KHKAEAAH 758
Length:758
Mass (Da):84,207
Last modified:October 25, 2005 - v1
Checksum:i0C96A2EB64A9F7DC
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier
Sequence conflicti367 – 3671A → G in AAA23583. 1 Publication
Sequence conflicti411 – 4111L → V in AAA23583. 1 Publication
Sequence conflicti533 – 5331L → V in AAA23583. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M31045 Genomic DNA. Translation: AAA23583.1.
U00096 Genomic DNA. Translation: AAC73969.1.
AP009048 Genomic DNA. Translation: BAA35601.1.
M23220 Genomic DNA. Translation: AAA23582.1.
PIRiSUECCA. B64827.
RefSeqiNP_415403.1. NC_000913.3.
YP_489155.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC73969; AAC73969; b0882.
BAA35601; BAA35601; BAA35601.
GeneIDi12932326.
945764.
KEGGiecj:Y75_p0855.
eco:b0882.
PATRICi32116973. VBIEscCol129921_0912.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M31045 Genomic DNA. Translation: AAA23583.1 .
U00096 Genomic DNA. Translation: AAC73969.1 .
AP009048 Genomic DNA. Translation: BAA35601.1 .
M23220 Genomic DNA. Translation: AAA23582.1 .
PIRi SUECCA. B64827.
RefSeqi NP_415403.1. NC_000913.3.
YP_489155.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1K6K X-ray 1.80 A 1-143 [» ]
1KSF X-ray 2.60 X 1-758 [» ]
1LZW X-ray 2.50 B 1-146 [» ]
1MBU X-ray 2.30 A/B 1-142 [» ]
1MBV X-ray 3.30 A 1-142 [» ]
1MBX X-ray 2.25 A/B 1-142 [» ]
1MG9 X-ray 2.30 B 1-146 [» ]
1R6B X-ray 2.25 X 1-758 [» ]
1R6C X-ray 2.15 X 1-143 [» ]
1R6O X-ray 2.25 A/B 1-143 [» ]
1R6Q X-ray 2.35 A/B 1-143 [» ]
ProteinModelPortali P0ABH9.
SMRi P0ABH9. Positions 1-755.
ModBasei Search...

Protein-protein interaction databases

BioGridi 850131. 1 interaction.
DIPi DIP-35409N.
IntActi P0ABH9. 75 interactions.
STRINGi 511145.b0882.

Proteomic databases

PaxDbi P0ABH9.
PRIDEi P0ABH9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC73969 ; AAC73969 ; b0882 .
BAA35601 ; BAA35601 ; BAA35601 .
GeneIDi 12932326.
945764.
KEGGi ecj:Y75_p0855.
eco:b0882.
PATRICi 32116973. VBIEscCol129921_0912.

Organism-specific databases

EchoBASEi EB0154.
EcoGenei EG10156. clpA.

Phylogenomic databases

eggNOGi COG0542.
HOGENOMi HOG000218210.
KOi K03694.
OMAi ATDICAD.
OrthoDBi EOG65F8SM.
PhylomeDBi P0ABH9.

Enzyme and pathway databases

BioCyci EcoCyc:EG10156-MONOMER.
ECOL316407:JW0866-MONOMER.
MetaCyc:EG10156-MONOMER.
SABIO-RKi P0ABH9.

Miscellaneous databases

EvolutionaryTracei P0ABH9.
PROi P0ABH9.

Gene expression databases

Genevestigatori P0ABH9.

Family and domain databases

Gene3Di 1.10.1780.10. 1 hit.
3.40.50.300. 2 hits.
InterProi IPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR019489. Clp_ATPase_C.
IPR004176. Clp_N.
IPR013461. ClpA.
IPR001270. ClpA/B.
IPR018368. ClpA/B_CS1.
IPR028299. ClpA/B_CS2.
IPR023150. Dbl_Clp-N.
IPR027417. P-loop_NTPase.
[Graphical view ]
PANTHERi PTHR11638:SF14. PTHR11638:SF14. 1 hit.
Pfami PF00004. AAA. 1 hit.
PF07724. AAA_2. 1 hit.
PF02861. Clp_N. 1 hit.
PF10431. ClpB_D2-small. 1 hit.
[Graphical view ]
PRINTSi PR00300. CLPPROTEASEA.
SMARTi SM00382. AAA. 2 hits.
SM01086. ClpB_D2-small. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 2 hits.
TIGRFAMsi TIGR02639. ClpA. 1 hit.
PROSITEi PS00870. CLPAB_1. 1 hit.
PS00871. CLPAB_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publicationsDownload
  1. "The ATP-dependent Clp protease of Escherichia coli. Sequence of clpA and identification of a Clp-specific substrate."
    Gottesman S., Clark W.P., Maurizi M.R.
    J. Biol. Chem. 265:7886-7893(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map."
    Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K.
    , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T.
    DNA Res. 3:137-155(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  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].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "The two-component, ATP-dependent Clp protease of Escherichia coli. Purification, cloning, and mutational analysis of the ATP-binding component."
    Katayama Y., Gottesman S., Pumphrey J., Rudikoff S., Clark W.P., Maurizi M.R.
    J. Biol. Chem. 263:15226-15236(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28, PARTIAL PROTEIN SEQUENCE.
    Strain: SG1110.
  6. "Structure and expression of the infA operon encoding translational initiation factor IF1. Transcriptional control by growth rate."
    Cummings H.S., Sands J.F., Foreman P.C., Fraser J., Hershey J.W.B.
    J. Biol. Chem. 266:16491-16498(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 511-758.
  7. "Conservation of the regulatory subunit for the Clp ATP-dependent protease in prokaryotes and eukaryotes."
    Gottesman S., Squires C., Pichersky E., Carrington M., Hobbs M., Mattick J.S., Dalrymple B., Kuramitsu H., Shiroza T., Foster T., Clark W.P., Ross B., Squires C.L., Maurizi M.R.
    Proc. Natl. Acad. Sci. U.S.A. 87:3513-3517(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: SIMILARITY TO OTHER CLPAB LIKE PROTEINS.
  8. "Crystal structure of ClpA, an Hsp100 chaperone and regulator of ClpAP protease."
    Guo F., Maurizi M.R., Esser L., Xia D.
    J. Biol. Chem. 277:46743-46752(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-143.
  9. "Structural analysis of the adaptor protein ClpS in complex with the N-terminal domain of ClpA."
    Zeth K., Ravelli R.B., Paal K., Cusack S., Bukau B., Dougan D.A.
    Nat. Struct. Biol. 9:906-911(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-146 IN COMPLEX WITH CLPS.
  10. "Crystal structure of the heterodimeric complex of the adaptor, ClpS, with the N-domain of the AAA+ chaperone, ClpA."
    Guo F., Esser L., Singh S.K., Maurizi M.R., Xia D.
    J. Biol. Chem. 277:46753-46762(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 1-143 IN COMPLEX WITH CLPS.

Entry nameiCLPA_ECOLI
AccessioniPrimary (citable) accession number: P0ABH9
Secondary accession number(s): P15716, P77686
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: October 25, 2005
Last modified: June 11, 2014
This is version 76 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

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