ID A0A4Z0LWG3_9GAMM Unreviewed; 860 AA.
AC A0A4Z0LWG3;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
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:TGD71574.1};
GN ORFNames=E4634_18190 {ECO:0000313|EMBL:TGD71574.1};
OS Haliea sp. SAOS-164.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales; Halieaceae;
OC Haliea.
OX NCBI_TaxID=2562682 {ECO:0000313|EMBL:TGD71574.1, ECO:0000313|Proteomes:UP000298050};
RN [1] {ECO:0000313|EMBL:TGD71574.1, ECO:0000313|Proteomes:UP000298050}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAOS-164 {ECO:0000313|EMBL:TGD71574.1,
RC ECO:0000313|Proteomes:UP000298050};
RA Verma A., Kumar P., Krishnamurthi S.;
RT "Taxonomy of novel Haliea sp. from mangrove soil of West Coast of India.";
RL Submitted (APR-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 -!- 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:TGD71574.1}.
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DR EMBL; SRLE01000013; TGD71574.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4Z0LWG3; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000298050; 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 78, MITOCHONDRIAL; 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:UP000298050};
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 412..492
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 860 AA; 95214 MW; 145B0F1FAFC8E522 CRC64;
MRMDKLTNQL QTALADAQSL ALGKDHNFIE PVHLLAALLE QSGGSARPLL QKAGGDIARL
RGEVQAAVEA LPRVSGTGGD VHISQDLMRV LNLTDKLAQQ GGDSYISSEL VLLAMLSAKG
RPADLMTACG VTEAALKTAI EQVRGGEKVD NPEAEESRQA LEKYTIDLTE RAEQGKLDPV
IGRDDEIRRT IQVLQRRTKN NPVLIGEPGV GKTAIVEGLA QRIVNGEVPE GLKDKRVLSL
DMGALLAGAK FRGDFEERLK AVLNELSKEE GRVILFIDEL HTMVGAGKAE GSMDAGNMLK
PALARGELHC VGATTLDEYR QYIEKDAALE RRFQKVLVDE PNEEDTIAIL RGLKERYEVH
HGVDITDSAI IAAAKLSQRY ITDRQLPDKA IDLVDEAASR IRMEIDSKPE SMDKLERRLI
QLKIEREAVK KDKDPAAKKQ LDHLDEEIDK AEREFADLEE VWKAEKASLQ GAAEIKSELE
QVKLELEAAR RAGDLTKMSE LQYGRIPQLE KQLEQAHEAE NTERSMTLLR NKVTDEEVAE
VVSRWTGIPI SKMLEGDREK LLRMEDALHS RVVGQDEAVV AVSNAVRRSR AGLSDPNRPN
GSFLFLGPTG VGKTELCKAL AEFLYDSEQA MVRVDMSEFM EKHSVARLIG APPGYVGYEE
GGYLTEAVRR RPYSLLLLDE VEKAHPDVFN ILLQVLEDGR LTDGQGRTVD FRNTVVVMTS
NLGSDLIQEM AGEENYAKMK AAVMGVVGTH FRPEFINRID ETVVFHPLQQ DQIRGIAGIQ
LQGLRKRLAE RELQLEISDS FMDHLVEAGF DPVYGARPLK RAIQQELENP LAQRILSGDF
APGTTVVVDQ EGENTVISGR
//
