ID A0A1E2VC47_9GAMM Unreviewed; 866 AA.
AC A0A1E2VC47;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=BFW38_14350 {ECO:0000313|EMBL:ODC04534.1};
OS Terasakiispira papahanaumokuakeensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Terasakiispira.
OX NCBI_TaxID=197479 {ECO:0000313|EMBL:ODC04534.1, ECO:0000313|Proteomes:UP000094291};
RN [1] {ECO:0000313|EMBL:ODC04534.1, ECO:0000313|Proteomes:UP000094291}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PH27A {ECO:0000313|EMBL:ODC04534.1,
RC ECO:0000313|Proteomes:UP000094291};
RA Seilhamer J.J.;
RL Submitted (AUG-2016) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ODC04534.1}.
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DR EMBL; MDTQ01000001; ODC04534.1; -; Genomic_DNA.
DR RefSeq; WP_068999518.1; NZ_MDTQ01000001.1.
DR AlphaFoldDB; A0A1E2VC47; -.
DR STRING; 197479.BFW38_14350; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000094291; Unassembled WGS sequence.
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:UP000094291};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..147
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 406..493
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 866 AA; 96710 MW; DF1D7AE01C495A31 CRC64;
MRIDRLTSKL QNAFADAQSM AVGRSHNELA PAHLLLALLE QEDSPLKPLI RQAGGDAGRL
RGSLDEVLNR LPTVSGQYDG NVQLSQALGR LLNLADRESQ KRGDQYIASE LVLLCALELK
DDTSKAIEQA GLTQPKLEKA IEQVRGGEKV DDPNAEDQRQ ALSKYTIDLT ERALSGKLDP
VIGRDDEIRR TIQVLQRRTK NNPVLIGEPG VGKTAIVEGL AQRIVNGEVP EGLKDKKVLS
LDMGSLIAGA KFRGEFEERL KAVLSDLSKE EGQVILFIDE LHTMVGAGKG EGSMDAGNML
KPALARGELH CVGATTLDEY RQYIEKDAAL ERRFQKVIVD EPSEEDTIAI LRGLKERYEV
HHGVEITDSA VIAAANLSSR YIPDRQLPDK AIDLMDEAAS RIRMEIDSKP EEMDKLERRM
IQLKIEREAL KKETDDGSKK RLDSLDELIA DYEHQYADLE EIWKSEKSNL QGAQQIKQQL
EQARIELEAA KRKGDLGRMS EIQYGVIPDL ERSLQMADQH EPVAHSHRLL RNRVTDEEIA
EVVSRWTGIP VNRMLESERD KLLRMEEALH ERVIGQDEAV TAVANAVRRS RAGLSDPFRP
NGSFLFLGPT GVGKTELCKS LAKFLFDTEE AMVRIDMSEF MEKHAVSRLI GAPPGYVGYE
EGGYLTEAVR RKPYSVILLD EVEKAHPDVF NILLQVLEDG RLTDGQGRTV DFRNTVIVMT
SNLGSDLIQT LTAESSYEAM KAQVMEVVGT HFRPELLNRI DEVVVFHPLQ KDQIRGIAEI
QLARLCQRLA ERELSLTLSG EFNDALVEQG YDPVFGARPL KRAIQQLLEN PLAQAILAGR
FSPGDTIQVR LQNGQPVFER AEHAMV
//