ID A0A495E8X1_9FLAO Unreviewed; 866 AA.
AC A0A495E8X1;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 13-SEP-2023, entry version 15.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=CLV91_2086 {ECO:0000313|EMBL:RKR13368.1};
OS Maribacter vaceletii.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Maribacter.
OX NCBI_TaxID=1206816 {ECO:0000313|EMBL:RKR13368.1, ECO:0000313|Proteomes:UP000269412};
RN [1] {ECO:0000313|EMBL:RKR13368.1, ECO:0000313|Proteomes:UP000269412}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25230 {ECO:0000313|EMBL:RKR13368.1,
RC ECO:0000313|Proteomes:UP000269412};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (OCT-2018) 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:RKR13368.1}.
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DR EMBL; RBIQ01000008; RKR13368.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A495E8X1; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000269412; 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:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 Hydrolase {ECO:0000313|EMBL:RKR13368.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:RKR13368.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000269412};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..144
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 410..528
FT /evidence="ECO:0000256|RuleBase:RU362034"
FT COILED 775..802
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 866 AA; 97505 MW; 3F9FD22113C4E069 CRC64;
MNFNNFTIKS QEAVQQAQIL AQSLGHQQIE NEHLYKGISE VDENVLPFLL KKLNVNNNLL
KQILDKELES FPKVSGGDIM ASREASKTLT EANVLAKKMN DEYVSLEHLL LAIFKSKSKV
AQILKDQGVT LKNLEAAINE LRKGGNVTSQ SAEETYNSLD KYAKNLNKLA DNGNLDPVIG
RDEEIRRILQ ILSRRTKNNP MLVGEPGVGK TAIAEGLAHR IVLGDVPENL KEKIIYSLDM
GALIAGAKYK GEFEERLKSV IKEVTESDGD IVLFIDEIHT LVGAGGGQGA MDAANILKPA
LARGELRAIG ATTLDEYQKY FEKDKALERR FQKVIVEEPD SESAISILRG IKEKYEAHHK
VRIKDEAVIA AVELSQRYIT NRFLPDKAID LMDEAASKLR MEINSKPEEL DVLDRKIMQL
EIEIEAIKRE NDTVKVKSLN IELANLKEDR IEIFAKWESE KTVVDNIQKT KQDIENYKLE
AERAERNGDY GKVAELRYGK IKEAQENLEK LQVELEQQQN VGTLIKEEVT NEDIADVVAK
WTGIPVTKML QSEREKLLQL EDVLHKRVVG QEEAIVAVSD AIRRSRAGLQ DTKKPIGSFL
FLGTTGVGKT ELAKTLASYL FDDENAMTRI DMSEYQERHS VSRLVGAPPG YVGYDEGGQL
TEAVRRRPYS VILLDEIEKA HPDTFNILLQ VLDEGRLTDN KGRVADFKNA IIIMTSNMGS
HIIQEKFENS KDTFSATESA RVEVLGLLRK TIRPEFLNRI DDIIMFTPLS KEDIKQIVEL
QIEQLKKMLN KQNIAIDATQ EAITYLANKG YEPQYGARPI KRVIQKEVLN NLSKELLKGS
IKAESIVLID SFNESLVFRN QNELAS
//