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P0ABH9 (CLPA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ATP-dependent Clp protease ATP-binding subunit ClpA
Gene names
Name:clpA
Synonyms:lopD
Ordered Locus Names:b0882, JW0866
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length758 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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.

Sequence similarities

Belongs to the clpA/clpB family.

Ontologies

Keywords
   DomainRepeat
   LigandATP-binding
Nucleotide-binding
   Molecular functionChaperone
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processproteolysis

Inferred from direct assay Ref.5. Source: EcoCyc

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATP-dependent peptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

clpSP0A8Q68EBI-546140,EBI-561456

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 758758ATP-dependent Clp protease ATP-binding subunit ClpA
PRO_0000191079

Regions

Nucleotide binding214 – 2218ATP Potential
Nucleotide binding495 – 5028ATP Potential
Region169 – 417249I
Region421 – 609189II

Experimental info

Sequence conflict3671A → G in AAA23583. Ref.1
Sequence conflict4111L → V in AAA23583. Ref.1
Sequence conflict5331L → V in AAA23583. Ref.1

Secondary structure

1 ..................................................................................................................................... 758
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0ABH9 [UniParc].

Last modified October 25, 2005. Version 1.
Checksum: 0C96A2EB64A9F7DC

FASTA75884,207
        10         20         30         40         50         60 
MLNQELELSL NMAFARAREH RHEFMTVEHL LLALLSNPSA REALEACSVD LVALRQELEA 

        70         80         90        100        110        120 
FIEQTTPVLP ASEEERDTQP TLSFQRVLQR AVFHVQSSGR NEVTGANVLV AIFSEQESQA 

       130        140        150        160        170        180 
AYLLRKHEVS RLDVVNFISH GTRKDEPTQS SDPGSQPNSE EQAGGEERME NFTTNLNQLA 

       190        200        210        220        230        240 
RVGGIDPLIG REKELERAIQ VLCRRRKNNP LLVGESGVGK TAIAEGLAWR IVQGDVPEVM 

       250        260        270        280        290        300 
ADCTIYSLDI GSLLAGTKYR GDFEKRFKAL LKQLEQDTNS ILFIDEIHTI IGAGAASGGQ 

       310        320        330        340        350        360 
VDAANLIKPL LSSGKIRVIG STTYQEFSNI FEKDRALARR FQKIDITEPS IEETVQIING 

       370        380        390        400        410        420 
LKPKYEAHHD VRYTAKAVRA AVELAVKYIN DRHLPDKAID VIDEAGARAR LMPVSKRKKT 

       430        440        450        460        470        480 
VNVADIESVV ARIARIPEKS VSQSDRDTLK NLGDRLKMLV FGQDKAIEAL TEAIKMARAG 

       490        500        510        520        530        540 
LGHEHKPVGS FLFAGPTGVG KTEVTVQLSK ALGIELLRFD MSEYMERHTV SRLIGAPPGY 

       550        560        570        580        590        600 
VGFDQGGLLT DAVIKHPHAV LLLDEIEKAH PDVFNILLQV MDNGTLTDNN GRKADFRNVV 

       610        620        630        640        650        660 
LVMTTNAGVR ETERKSIGLI HQDNSTDAME EIKKIFTPEF RNRLDNIIWF DHLSTDVIHQ 

       670        680        690        700        710        720 
VVDKFIVELQ VQLDQKGVSL EVSQEARNWL AEKGYDRAMG ARPMARVIQD NLKKPLANEL 

       730        740        750 
LFGSLVDGGQ VTVALDKEKN ELTYGFQSAQ KHKAEAAH

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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 277:1453-1474(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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M31045 Genomic DNA. Translation: AAA23583.1.
U00096 Genomic DNA. Translation: AAC73969.1.
AP009048 Genomic DNA. Translation: BAA35601.1.
M23220 Genomic DNA. Translation: AAA23582.1.
PIRSUECCA. B64827.
RefSeqNP_415403.1. NC_000913.2.
YP_489155.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP0ABH9.
SMRP0ABH9. Positions 1-755.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-35409N.
IntActP0ABH9. 71 interactions.
STRING511145.b0882.

Proteomic databases

PaxDbP0ABH9.
PRIDEP0ABH9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73969; AAC73969; b0882.
BAA35601; BAA35601; BAA35601.
GeneID12932326.
945764.
KEGGecj:Y75_p0855.
eco:b0882.
PATRIC32116973. VBIEscCol129921_0912.

Organism-specific databases

EchoBASEEB0154.
EcoGeneEG10156. clpA.

Phylogenomic databases

eggNOGCOG0542.
HOGENOMHOG000218210.
KOK03694.
OMADRETQPT.
ProtClustDBPRK11034.

Enzyme and pathway databases

BioCycEcoCyc:EG10156-MONOMER.
ECOL316407:JW0866-MONOMER.
MetaCyc:EG10156-MONOMER.

Gene expression databases

GenevestigatorP0ABH9.

Family and domain databases

Gene3D1.10.1780.10. 1 hit.
InterProIPR003593. AAA+_ATPase.
IPR013093. ATPase_AAA-2.
IPR003959. ATPase_AAA_core.
IPR018368. Chaperonin_ClpA/B_CS.
IPR001270. Chaprnin_ClpA/B.
IPR019489. Clp_ATPase_C.
IPR004176. Clp_N.
IPR013461. ClpA.
IPR023150. Dbl_Clp-N.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERPTHR11638:SF14. PTHR11638:SF14. 1 hit.
PfamPF00004. AAA. 1 hit.
PF07724. AAA_2. 1 hit.
PF02861. Clp_N. 1 hit.
PF10431. ClpB_D2-small. 1 hit.
[Graphical view]
PRINTSPR00300. CLPPROTEASEA.
SMARTSM00382. AAA. 2 hits.
SM01086. ClpB_D2-small. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 2 hits.
TIGRFAMsTIGR02639. ClpA. 1 hit.
PROSITEPS00870. CLPAB_1. 1 hit.
PS00871. CLPAB_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0ABH9.

Entry information

Entry nameCLPA_ECOLI
AccessionPrimary (citable) accession number: P0ABH9
Secondary accession number(s): P15716, P77686
Entry history
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: October 25, 2005
Last modified: May 29, 2013
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents