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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//