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Database: UniProt
Entry: A0A6B8JWF8_9GAMM
LinkDB: A0A6B8JWF8_9GAMM
Original site: A0A6B8JWF8_9GAMM 
ID   A0A6B8JWF8_9GAMM        Unreviewed;       868 AA.
AC   A0A6B8JWF8;
DT   17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 1.
DT   13-SEP-2023, entry version 11.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034,
GN   ECO:0000313|EMBL:QGM22494.1};
GN   ORFNames=GJ672_01965 {ECO:0000313|EMBL:QGM22494.1};
OS   Spiribacter sp. 2438.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Spiribacter.
OX   NCBI_TaxID=2666185 {ECO:0000313|EMBL:QGM22494.1, ECO:0000313|Proteomes:UP000363759};
RN   [1] {ECO:0000313|EMBL:QGM22494.1, ECO:0000313|Proteomes:UP000363759}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2438 {ECO:0000313|EMBL:QGM22494.1,
RC   ECO:0000313|Proteomes:UP000363759};
RA   Xue Q.;
RL   Submitted (NOV-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; CP046046; QGM22494.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A6B8JWF8; -.
DR   KEGG; spiz:GJ672_01965; -.
DR   Proteomes; UP000363759; 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:UP000363759};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          1..145
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          411..491
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   868 AA;  96517 MW;  9AA2A2C761899064 CRC64;
     MDKLTTKFQM ALADAQSLAL GRDHQMIEPE HLLLAMLDQE GGGVRHLLQQ AGVNGAYLRS
     QLGEAVDRLP TVAGAAGDVH VSNDLNRLLN QTDKLAQKRG DSYISSELFL LAAVQDGQSR
     VGQLLTGAGA NRQALEKAIE STRGGENVDD PNAEDQRQAL EKYTIDLTER AEQAKLDPVI
     GRDEEIRRTI QVLQRRTKNN PVLIGEPGVG KTAIVEGLAL RIVNQEVPEA LKHKRVLSLD
     MGAMVAGAKY RGEFEERMKA VLKDLARQEG EIILFIDEIH TIVGAGKAEG SMDAGNMLKP
     ALARGELHCI GATTLDEYRT NIEKDAALER RFQKVLVDEP SVEDTVAILR GLKERYEVHH
     GVEITDPAIV SAATLSQRYI TDRKLPDKAI DLVDEAASRI RIEIDSKPEA MDRLERRLIQ
     LKIEREALNK EEDEASRKRL ATLEDEIAEI EREYGEMESV WNAEKAAVEG ATGLKEALEQ
     ARQELETARR AGDLGRMSEL QYGRIPELEQ QLEAATQTED RPAMQLLRNA VTEEEVAEVV
     SKWTGIPVSK MLEGEREKLL KMESALGERV IGQHEAVEAV SNAIRRSRAG LSDPHRPNGS
     FLFLGPTGVG KTELCKALAG FLFDTEDAMV RVDMSEFMEK HSVARLIGAP PGYVGYEEGG
     YLTEAVRRKP YSVLLLDEVE KAHADVFNIL LQVLDDGRLT DSHGRTVDFR NTVIVMTSNL
     GSHLIQEHAG EAQYDEMKRQ VMGVVSQHFR PEFINRVDDV VVFHPLEREQ IRRITEIQVR
     DLSERLRERD MTLELSEAAL DVLGEAGFDP IYGARPLKRV LQQRMENALA QRILGGEFSP
     GDVIRVDAVG SGEASELRFE RLSEPVEA
//
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