ID A0A515A3R7_9BACT Unreviewed; 874 AA.
AC A0A515A3R7;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 13-SEP-2023, entry version 15.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:QDK81464.1};
GN ORFNames=EXU85_23775 {ECO:0000313|EMBL:QDK81464.1};
OS Spirosoma sp. KCTC 42546.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae; Spirosoma.
OX NCBI_TaxID=2520506 {ECO:0000313|EMBL:QDK81464.1, ECO:0000313|Proteomes:UP000319550};
RN [1] {ECO:0000313|EMBL:QDK81464.1, ECO:0000313|Proteomes:UP000319550}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 42546 {ECO:0000313|EMBL:QDK81464.1,
RC ECO:0000313|Proteomes:UP000319550};
RA Kim S.-G., Kusolkumbot P., Suwannachart C.;
RT "Complet Genome Sequence of novel Spirosoma sp. KCTC 42546 isolated from an
RT artificial reservoir in Korea.";
RL Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Part of a stress-induced multi-chaperone system, it is
CC involved in the recovery of the cell from heat-induced damage, in
CC cooperation with DnaK, DnaJ and GrpE. {ECO:0000256|RuleBase:RU362034}.
CC -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent.
CC {ECO:0000256|ARBA:ARBA00026057}.
CC -!- SUBUNIT: Homohexamer; The oligomerization is ATP-dependent.
CC {ECO:0000256|RuleBase:RU362034}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU362034}.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
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DR EMBL; CP041360; QDK81464.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A515A3R7; -.
DR KEGG; spik:EXU85_23775; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000319550; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
DR GO; GO:0009408; P:response to heat; IEA:UniProtKB-UniRule.
DR CDD; cd00009; AAA; 1.
DR CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR017730; Chaperonin_ClpB.
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 NCBIfam; TIGR03346; chaperone_ClpB; 1.
DR PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR PANTHER; PTHR11638:SF18; HEAT SHOCK PROTEIN 104; 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; 1.
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.
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|RuleBase:RU362034};
KW Cytoplasm {ECO:0000256|RuleBase:RU362034};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Reference proteome {ECO:0000313|Proteomes:UP000319550};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..146
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 399..490
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 874 AA; 97319 MW; E75E59F09F5E88D1 CRC64;
MDFKNYTIKA QEVVQKASEI ALGNGQQGIE TGHLLQAILS EDENVVGFIA KKTGINLQNT
NAALQAILTT YPKVSGGNGS VYLSNDTAAA LAKASSYTKE FGDEFVSVEL MLLGLMGGKD
QIATLLKDAG FNEKQTKAAI NELRKGNSVK DQNAEAKYQS LERFSINLNE RARTGKIDPV
IGRDEEIRRV LQILSRRTKN NPILLGEPGV GKTAIVEGLA QRIVSGDVPE NLKTKTIVSL
DMGLLIAGAK YKGEFEERLK AVIKEVTDSD GQIILFIDEI HTLIGAGAGG EGAMDAANLL
KPALSRGELH TIGATTLKEY QKYIEKDKAL ERRFQAVMVD EPDMPDAISI LRGIKEKYEL
HHGVRIKDDA VIAAVELSTR YITDRFLPDK AIDLMDEAAA KLRLEMDSVP EELDELNRRI
MQLEIEREAI RRENDKEKET VLNKQIEDLS EQRNSLKAKW ETEKASVNEG RTLKEELDKL
KLEADQAERS GDYGKVAEIR YGRIPEIENK LNSLAKEGSD KDSSDRMMQE EVTADDIAEV
VAKWTGIPVS KMLQSDREKL LNLEKELGKR VAGQAEAIEV VADAVRRSRA GMQDPKRPIG
SFIFLGTTGV GKTEVARTLA EYLFNDENAL VRIDMSEYQE RHAVSRLIGA PPGYVGYDEG
GQLTEAVRRK PYSVVLLDEI EKAHPDVWNI LLQVLDEGRL TDNKGRVANF KNTIIIMTSN
IGSHLIQEKF AEDEGWNHSL VLEEAKSAVL ELLRQTIRPE FLNRIDEIVM FEPLTKANIR
KIVDIQFRGI KQRLAENGIQ LDATDEALTK IGEEGFDPQF GARPLKRVLQ RRVLNELSKS
ILSGEVKKDS VVLMELNNDG EIAFTNLDAH IENL
//