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Protein

ATP-dependent Clp protease ATP-binding subunit ClpA

Gene

clpA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-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 identifierActions
Nucleotide bindingi214 – 2218ATPSequence Analysis
Nucleotide bindingi495 – 5028ATPSequence Analysis

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • ATP-dependent peptidase activity Source: CACAO

GO - Biological processi

  • proteolysis Source: EcoCyc
  • response to oxidative stress Source: EcoCyc
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-RKP0ABH9.

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 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10156. clpA.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 758758ATP-dependent Clp protease ATP-binding subunit ClpAPRO_0000191079Add
BLAST

Proteomic databases

PaxDbiP0ABH9.
PRIDEiP0ABH9.

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.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
clpPP0A6G73EBI-546140,EBI-370625
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

1
758
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 2017Combined sources
Beta strandi22 – 254Combined sources
Helixi27 – 348Combined sources
Helixi38 – 469Combined sources
Helixi51 – 6515Combined sources
Beta strandi72 – 743Combined sources
Helixi82 – 9615Combined sources
Beta strandi97 – 993Combined sources
Beta strandi101 – 1033Combined sources
Helixi105 – 1128Combined sources
Helixi119 – 1268Combined sources
Helixi131 – 1399Combined sources
Beta strandi171 – 1733Combined sources
Helixi176 – 1816Combined sources
Helixi192 – 20211Combined sources
Beta strandi204 – 2074Combined sources
Beta strandi209 – 2135Combined sources
Helixi220 – 23314Combined sources
Helixi238 – 2403Combined sources
Beta strandi244 – 2474Combined sources
Beta strandi259 – 2613Combined sources
Helixi263 – 27412Combined sources
Beta strandi275 – 2784Combined sources
Beta strandi280 – 2845Combined sources
Turni285 – 2928Combined sources
Beta strandi296 – 2983Combined sources
Helixi300 – 3078Combined sources
Beta strandi311 – 3133Combined sources
Beta strandi317 – 3226Combined sources
Helixi324 – 3285Combined sources
Helixi329 – 3335Combined sources
Helixi338 – 3403Combined sources
Beta strandi341 – 3455Combined sources
Helixi351 – 36919Combined sources
Helixi375 – 38814Combined sources
Helixi396 – 41116Combined sources
Beta strandi412 – 4143Combined sources
Helixi423 – 43311Combined sources
Beta strandi441 – 4444Combined sources
Helixi445 – 45612Combined sources
Turni457 – 4593Combined sources
Helixi464 – 47815Combined sources
Beta strandi484 – 4863Combined sources
Beta strandi488 – 4947Combined sources
Helixi501 – 51212Combined sources
Beta strandi515 – 5206Combined sources
Helixi521 – 5233Combined sources
Beta strandi525 – 5284Combined sources
Beta strandi531 – 5333Combined sources
Helixi541 – 5455Combined sources
Helixi548 – 5558Combined sources
Beta strandi557 – 5648Combined sources
Helixi566 – 5683Combined sources
Helixi571 – 58313Combined sources
Beta strandi584 – 5885Combined sources
Turni589 – 5913Combined sources
Beta strandi592 – 5954Combined sources
Beta strandi599 – 6057Combined sources
Helixi629 – 6357Combined sources
Helixi638 – 6414Combined sources
Beta strandi645 – 6495Combined sources
Helixi655 – 67521Combined sources
Beta strandi678 – 6825Combined sources
Helixi684 – 69411Combined sources
Turni697 – 6993Combined sources
Turni701 – 7033Combined sources
Helixi704 – 7129Combined sources
Helixi714 – 7163Combined sources
Helixi717 – 7226Combined sources
Turni724 – 7274Combined sources
Beta strandi729 – 7368Combined sources
Turni737 – 7404Combined sources
Beta strandi741 – 7488Combined sources
Beta strandi750 – 7523Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0ABH9.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni169 – 417249IAdd
BLAST
Regioni421 – 609189IIAdd
BLAST

Sequence similaritiesi

Belongs to the ClpA/ClpB family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0542.
HOGENOMiHOG000218210.
InParanoidiP0ABH9.
KOiK03694.
OMAiFTHQDHS.
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]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLNQELELSL NMAFARAREH RHEFMTVEHL LLALLSNPSA REALEACSVD
60 70 80 90 100
LVALRQELEA FIEQTTPVLP ASEEERDTQP TLSFQRVLQR AVFHVQSSGR
110 120 130 140 150
NEVTGANVLV AIFSEQESQA AYLLRKHEVS RLDVVNFISH GTRKDEPTQS
160 170 180 190 200
SDPGSQPNSE EQAGGEERME NFTTNLNQLA RVGGIDPLIG REKELERAIQ
210 220 230 240 250
VLCRRRKNNP LLVGESGVGK TAIAEGLAWR IVQGDVPEVM ADCTIYSLDI
260 270 280 290 300
GSLLAGTKYR GDFEKRFKAL LKQLEQDTNS ILFIDEIHTI IGAGAASGGQ
310 320 330 340 350
VDAANLIKPL LSSGKIRVIG STTYQEFSNI FEKDRALARR FQKIDITEPS
360 370 380 390 400
IEETVQIING LKPKYEAHHD VRYTAKAVRA AVELAVKYIN DRHLPDKAID
410 420 430 440 450
VIDEAGARAR LMPVSKRKKT VNVADIESVV ARIARIPEKS VSQSDRDTLK
460 470 480 490 500
NLGDRLKMLV FGQDKAIEAL TEAIKMARAG LGHEHKPVGS FLFAGPTGVG
510 520 530 540 550
KTEVTVQLSK ALGIELLRFD MSEYMERHTV SRLIGAPPGY VGFDQGGLLT
560 570 580 590 600
DAVIKHPHAV LLLDEIEKAH PDVFNILLQV MDNGTLTDNN GRKADFRNVV
610 620 630 640 650
LVMTTNAGVR ETERKSIGLI HQDNSTDAME EIKKIFTPEF RNRLDNIIWF
660 670 680 690 700
DHLSTDVIHQ VVDKFIVELQ VQLDQKGVSL EVSQEARNWL AEKGYDRAMG
710 720 730 740 750
ARPMARVIQD NLKKPLANEL LFGSLVDGGQ VTVALDKEKN ELTYGFQSAQ

KHKAEAAH
Length:758
Mass (Da):84,207
Last modified:October 25, 2005 - v1
Checksum:i0C96A2EB64A9F7DC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti367 – 3671A → G in AAA23583 (PubMed:2186030).Curated
Sequence conflicti411 – 4111L → V in AAA23583 (PubMed:2186030).Curated
Sequence conflicti533 – 5331L → V in AAA23583 (PubMed:2186030).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
PIRiB64827. SUECCA.
RefSeqiNP_415403.1. NC_000913.3.

Genome annotation databases

EnsemblBacteriaiAAC73969; AAC73969; b0882.
BAA35601; BAA35601; BAA35601.
GeneIDi945764.
KEGGiecj:Y75_p0855.
eco:b0882.
PATRICi32116973. VBIEscCol129921_0912.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
PIRiB64827. SUECCA.
RefSeqiNP_415403.1. NC_000913.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Proteomic databases

PaxDbiP0ABH9.
PRIDEiP0ABH9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73969; AAC73969; b0882.
BAA35601; BAA35601; BAA35601.
GeneIDi945764.
KEGGiecj:Y75_p0855.
eco:b0882.
PATRICi32116973. VBIEscCol129921_0912.

Organism-specific databases

EchoBASEiEB0154.
EcoGeneiEG10156. clpA.

Phylogenomic databases

eggNOGiCOG0542.
HOGENOMiHOG000218210.
InParanoidiP0ABH9.
KOiK03694.
OMAiFTHQDHS.
OrthoDBiEOG65F8SM.
PhylomeDBiP0ABH9.

Enzyme and pathway databases

BioCyciEcoCyc:EG10156-MONOMER.
ECOL316407:JW0866-MONOMER.
MetaCyc:EG10156-MONOMER.
SABIO-RKP0ABH9.

Miscellaneous databases

EvolutionaryTraceiP0ABH9.
PROiP0ABH9.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. 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. 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 informationi

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 24, 2015
This is version 83 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. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.