CLPA_ECO57
ID CLPA_ECO57 Reviewed; 758 AA.
AC P0ABI1; P15716; P77686;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA;
GN Name=clpA; OrderedLocusNames=Z1119, ECs0968;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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}.
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DR EMBL; AE005174; AAG55264.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB34391.1; -; Genomic_DNA.
DR PIR; D85600; D85600.
DR PIR; H90749; H90749.
DR RefSeq; NP_308995.1; NC_002695.1.
DR RefSeq; WP_000934041.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0ABI1; -.
DR SMR; P0ABI1; -.
DR STRING; 155864.EDL933_1016; -.
DR EnsemblBacteria; AAG55264; AAG55264; Z1119.
DR EnsemblBacteria; BAB34391; BAB34391; ECs_0968.
DR GeneID; 66670844; -.
DR GeneID; 917711; -.
DR KEGG; ece:Z1119; -.
DR KEGG; ecs:ECs_0968; -.
DR PATRIC; fig|386585.9.peg.1084; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_2_6; -.
DR OMA; GRVIQEH; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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; Reference proteome; Repeat.
FT CHAIN 1..758
FT /note="ATP-dependent Clp protease ATP-binding subunit ClpA"
FT /id="PRO_0000191080"
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
