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Database: UniProt
Entry: A0A515A3R7_9BACT
LinkDB: A0A515A3R7_9BACT
Original site: A0A515A3R7_9BACT 
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
//
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