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Database: UniProt
Entry: A0A1J7CAV7_9GAMM
LinkDB: A0A1J7CAV7_9GAMM
Original site: A0A1J7CAV7_9GAMM 
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
//
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