ID O69936_STRCO Unreviewed; 842 AA.
AC O69936;
DT 01-AUG-1998, integrated into UniProtKB/TrEMBL.
DT 01-AUG-1998, sequence version 1.
DT 27-MAR-2024, entry version 141.
DE SubName: Full=Clp protease ATP binding subunit {ECO:0000313|EMBL:CAA19619.1};
GN Name=clpA {ECO:0000313|EMBL:CAA19619.1};
GN OrderedLocusNames=SCO6408 {ECO:0000313|EMBL:CAA19619.1};
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226 {ECO:0000313|EMBL:CAA19619.1, ECO:0000313|Proteomes:UP000001973};
RN [1] {ECO:0000313|EMBL:CAA19619.1, ECO:0000313|Proteomes:UP000001973}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145
RC {ECO:0000313|Proteomes:UP000001973};
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.H.,
RA Kieser T., Larke L., Murphy L., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
CC -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent.
CC {ECO:0000256|ARBA:ARBA00026057}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
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DR EMBL; AL939127; CAA19619.1; -; Genomic_DNA.
DR PIR; T34902; T34902.
DR RefSeq; NP_630495.1; NC_003888.3.
DR RefSeq; WP_011030897.1; NZ_VNID01000002.1.
DR AlphaFoldDB; O69936; -.
DR STRING; 100226.gene:17764065; -.
DR PaxDb; 100226-SCO6408; -.
DR PATRIC; fig|100226.15.peg.6508; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_1_11; -.
DR InParanoid; O69936; -.
DR OrthoDB; 9803641at2; -.
DR PhylomeDB; O69936; -.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0034605; P:cellular response to heat; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00009; AAA; 1.
DR CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR Gene3D; 1.10.8.60; -; 2.
DR Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 4.10.860.10; UVR domain; 1.
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; 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 InterPro; IPR001943; UVR_dom.
DR PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR PANTHER; PTHR11638:SF18; HEAT SHOCK PROTEIN 78, MITOCHONDRIAL; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF17871; AAA_lid_9; 1.
DR Pfam; PF02861; Clp_N; 2.
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; SSF81923; Double Clp-N motif; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51903; CLP_R; 1.
DR PROSITE; PS00870; CLPAB_1; 1.
DR PROSITE; PS00871; CLPAB_2; 1.
DR PROSITE; PS50151; UVR; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004432};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU004432};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000313|EMBL:CAA19619.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:CAA19619.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001973};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 31..177
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT DOMAIN 446..481
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 75..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 163..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 442..481
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 178..192
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 842 AA; 92111 MW; A8ADC12FDA90197F CRC64;
MTSGYMGPEG DPFAEFLARF FGGPRPRQID IGRLLSQPAR ELVRGAAQYA AEHGSRDLDT
EHLLRAALAT EPTRGLLSRA GADPDSLASQ IDERTGPVQH PPGEVPPPTS LSLTPAVKRA
LLDAHELARS TGTGYIGPEH VLSALAANPD SAAGHILNAA RFAPSNLPTE TPEAAKGRTE
SARTTNTPTL DKYGRDLTDL AQQGRIDPVI GREEEIEQTV EVLSRRGKNN PVLIGDAGVG
KTAIVEGLAQ RITDGDVPDV LIGRRVVALD LTGVVAGTRY RGDFEERMNN IVGEIRAHSD
ELIIFIDELH TVVGAGGGGE SGSMDAGNIL KPALARGELH IVGATTLEEY RRIEKDAALA
RRFQPILVPE PTTADAIEIL RGLRDRYEAH HQVRYTDEAL VAAVEMSDRY LTDRRLPDKA
IDLIDQAGAR VRLRARTKGT DVRALEREVD QLVRDKDQAV ADEQYEQATQ LRDRIVGLKQ
RITEATGDGQ ADEGLDLVVD TESIAEVVSR QTGIPVSSLT QEEKDRLLGL ESHLHERVVG
QDEAVRVVSD AVLRSRAGLS SADRPIGSFL FLGPTGVGKT ELARALAEAL FGSEDRMVRL
DMSEYQERHT VSRLVGAPPG YVGHEEAGQL TEVVRRHPYS LLLLDEVEKA HPDVFNILLQ
VLDDGRLTDS QGRTVDFSNT VVVMTSNLGS DVITRRGAGI GFGAGGAEAD EEARREQVLR
PLREHFRPEF LNRVDEIVVF RQLSGEQLRQ ITSLLLEQTR RMVHAQGVTV DFTDAAVDWL
AERGYQPEYG ARPLRRTIQR EVDNELSRLL LDGRVAEGGR VTVDVEDGRL AFRTPERPVP
EL
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