ID   CLPA_ECOL6              Reviewed;         758 AA.
AC   P0ABI0; P15716; P77686;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA;
GN   Name=clpA; OrderedLocusNames=c1019;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: ATP-dependent specificity component of the ClpAP protease. It
CC       directs the protease to specific substrates. It has unfoldase activity.
CC       The primary function of the ClpA-ClpP complex appears to be the
CC       degradation of unfolded or abnormal proteins (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Component of the ClpAP complex composed of six ClpA subunits
CC       assembled into a hexameric ring in the presence of ATP, and fourteen
CC       ClpP subunits arranged in two heptameric rings. Binds to ClpS (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN79491.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE014075; AAN79491.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_000934041.1; NC_004431.1.
DR   AlphaFoldDB; P0ABI0; -.
DR   SMR; P0ABI0; -.
DR   STRING; 199310.c1019; -.
DR   EnsemblBacteria; AAN79491; AAN79491; c1019.
DR   GeneID; 66670844; -.
DR   KEGG; ecc:c1019; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_2_6; -.
DR   OMA; GRVIQEH; -.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0043335; P:protein unfolding; IEA:InterPro.
DR   Gene3D; 1.10.1780.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR036628; Clp_N_dom_sf.
DR   InterPro; IPR004176; Clp_R_dom.
DR   InterPro; IPR013461; ClpA.
DR   InterPro; IPR001270; ClpA/B.
DR   InterPro; IPR018368; ClpA/B_CS1.
DR   InterPro; IPR028299; ClpA/B_CS2.
DR   InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF07724; AAA_2; 1.
DR   Pfam; PF17871; AAA_lid_9; 1.
DR   Pfam; PF02861; Clp_N; 1.
DR   Pfam; PF10431; ClpB_D2-small; 1.
DR   PRINTS; PR00300; CLPPROTEASEA.
DR   SMART; SM00382; AAA; 2.
DR   SMART; SM01086; ClpB_D2-small; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   SUPFAM; SSF81923; SSF81923; 1.
DR   TIGRFAMs; TIGR02639; ClpA; 1.
DR   PROSITE; PS51903; CLP_R; 1.
DR   PROSITE; PS00870; CLPAB_1; 1.
DR   PROSITE; PS00871; CLPAB_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Nucleotide-binding; Repeat.
FT   CHAIN           1..758
FT                   /note="ATP-dependent Clp protease ATP-binding subunit ClpA"
FT                   /id="PRO_0000191081"
FT   DOMAIN          1..145
FT                   /note="Clp R"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          2..65
FT                   /note="Repeat 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          80..145
FT                   /note="Repeat 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          140..167
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          169..417
FT                   /note="I"
FT   REGION          421..609
FT                   /note="II"
FT   COMPBIAS        142..167
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         214..221
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         495..502
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   758 AA;  84207 MW;  0C96A2EB64A9F7DC CRC64;
     MLNQELELSL NMAFARAREH RHEFMTVEHL LLALLSNPSA REALEACSVD LVALRQELEA
     FIEQTTPVLP ASEEERDTQP TLSFQRVLQR AVFHVQSSGR NEVTGANVLV AIFSEQESQA
     AYLLRKHEVS RLDVVNFISH GTRKDEPTQS SDPGSQPNSE EQAGGEERME NFTTNLNQLA
     RVGGIDPLIG REKELERAIQ VLCRRRKNNP LLVGESGVGK TAIAEGLAWR IVQGDVPEVM
     ADCTIYSLDI GSLLAGTKYR GDFEKRFKAL LKQLEQDTNS ILFIDEIHTI IGAGAASGGQ
     VDAANLIKPL LSSGKIRVIG STTYQEFSNI FEKDRALARR FQKIDITEPS IEETVQIING
     LKPKYEAHHD VRYTAKAVRA AVELAVKYIN DRHLPDKAID VIDEAGARAR LMPVSKRKKT
     VNVADIESVV ARIARIPEKS VSQSDRDTLK NLGDRLKMLV FGQDKAIEAL TEAIKMARAG
     LGHEHKPVGS FLFAGPTGVG KTEVTVQLSK ALGIELLRFD MSEYMERHTV SRLIGAPPGY
     VGFDQGGLLT DAVIKHPHAV LLLDEIEKAH PDVFNILLQV MDNGTLTDNN GRKADFRNVV
     LVMTTNAGVR ETERKSIGLI HQDNSTDAME EIKKIFTPEF RNRLDNIIWF DHLSTDVIHQ
     VVDKFIVELQ VQLDQKGVSL EVSQEARNWL AEKGYDRAMG ARPMARVIQD NLKKPLANEL
     LFGSLVDGGQ VTVALDKEKN ELTYGFQSAQ KHKAEAAH