ID A0A1J7CAV7_9GAMM Unreviewed; 857 AA.
AC A0A1J7CAV7;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 13-SEP-2023, entry version 28.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=BK025_00485 {ECO:0000313|EMBL:OIV47933.1};
OS Sodalis sp. TME1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Bruguierivoracaceae; Sodalis.
OX NCBI_TaxID=1912097 {ECO:0000313|EMBL:OIV47933.1, ECO:0000313|Proteomes:UP000181913};
RN [1] {ECO:0000313|EMBL:OIV47933.1, ECO:0000313|Proteomes:UP000181913}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TME1 {ECO:0000313|EMBL:OIV47933.1,
RC ECO:0000313|Proteomes:UP000181913};
RA Rosas-Perez T., Vera-Ponce De Leon A., Rosenblueth M., Ramirez-Puebla S.T.,
RA Rincon-Rosales R., Martinez-Romero J., Dunn M.F., Martinez-Romero E.;
RT "The Symbiome of Llaveia Cochineals (Hemiptera: Coccoidea: Monophlebidae)
RT Includes a Gammaproteobacterial Co-symbiont Sodalis TME1 and the Known
RT Candidatus Walczuchella monophlebidarum.";
RL Submitted (OCT-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:OIV47933.1}.
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DR EMBL; MNBX01000015; OIV47933.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J7CAV7; -.
DR Proteomes; UP000181913; 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:UP000181913};
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 405..492
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 857 AA; 95409 MW; 7A4301234D692988 CRC64;
MRLDRLTNKF QLALADAQSM ALGRDNQFIE PLHVMAALLK QEGGTVRPLL QSAGVNIVPF
ISAVEQACER LPQVEGTGGD VQPSQDLVRV LNLCDKLAQK CADSFISSEL FVLASLESRG
TLAELLKSAG ATTATITQAI EQMRGGEQVN DQGAEDQRQA LKKFTIDLTE RAEQGKLDPV
IGRDEEIRRT IQVLQRRTKN NPVLIGEPGV GKTAIVEGLA QRIVNGEVPE GLKNNRVLSL
DMGSLVAGAK YRGEFEERLK GVLSDLSKQE GNVILFIDEL HTMVGAGKAD GAMDAGNMLK
PALARGELHC VGATTLDEYR KFIEKDAALE RRFQKVFVAE PNVEDTIAIL RGLKERYELH
HHVQITDPAI VAAATLSHRY IADRQLPDKA IDLIDEAASS IRMQIDSKPE ELDRLERRII
QLKLEQQALK KESDDASLKR LAMLNDELAQ KERAYSELEE EWKAEKASLS GTQHLKAELE
QAKISIEQAR RVGDLARMSE LQYGKIPELE KQLAAASQSE GKGLRLLRNR VTDIEIAEVL
ARWTGIPVSR MLESERAKLL RMEQDLHQRV IGQNEAVEAV SNAIRRSRAG LADPNRPIGS
FMFLGPTGVG KTELCKALAT FLFDSDDAMV RIDMSEFMEK HSVSRLVGAP PGYVGYEEGG
CLTEAVRRRP YSVILLDEIE KAHPDVFNIL LQVLDDGRLT DGQGRTVDFR NTVVIMTSNL
GSDIIQERFG QMNYQEMKDV VLEVVSHHFR PEFLNRVDEV VVFHPLSREH ITEIAQIQLR
RLYQRLEERG YTATISDEAL ALLGKSGFDP VYGARPLKRA IQQEIENPLS QQILSGQLLP
GKPVKLEVRD DHIVASQ
//