ID   A0A0X8J9I8_9FLAO        Unreviewed;       863 AA.
AC   A0A0X8J9I8;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=AXF12_04425 {ECO:0000313|EMBL:AMD84825.1};
OS   Capnocytophaga haemolytica.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Capnocytophaga.
OX   NCBI_TaxID=45243 {ECO:0000313|EMBL:AMD84825.1, ECO:0000313|Proteomes:UP000065822};
RN   [1] {ECO:0000313|Proteomes:UP000065822}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCUG 32990 {ECO:0000313|Proteomes:UP000065822};
RA   Holder M.E., Ajami N.J., Petrosino J.F.;
RL   Submitted (FEB-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}.
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DR   EMBL; CP014227; AMD84825.1; -; Genomic_DNA.
DR   RefSeq; WP_066428658.1; NZ_LT906449.1.
DR   AlphaFoldDB; A0A0X8J9I8; -.
DR   STRING; 45243.AXF12_04425; -.
DR   KEGG; chg:AXF12_04425; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000065822; Chromosome.
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   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..521
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   863 AA;  96983 MW;  AA2E339B28FA236A CRC64;
     MNFNNYTIKA QEAVASAQQL VQALGQQELQ NEHFFKAIEE VDENVLPFLF KKLNVNREAV
     DKQLGAALES YPKVSGGQIG ISRDAATMLN DAANIAKKWN DEYVSLEHLI LAIFKSKSKI
     AQILKDQGVR ESELEKAIKE LRRGERVTSA SAEDTYNSLN KYAKNLCNLA YHGKLDPVIG
     RDEEIRRVLQ ILSRRTKNNP MLIGEPGVGK TAIAEGLAHR IVQGDVPENL KDKVIYSLDM
     GALIAGAKYK GEFEERLKSV VKEVTSSEGS IILFIDEIHT LVGAGGGEGA MDAANILKPA
     LARGELRAIG ATTLDEYQKY FEKDKALERR FQKVMVEEPD TESAISILRG IKEKYETHHK
     VRIKDEAIIA AVELSERYIT NRFLPDKAID LMDEAAAKLR MEINSKPEEL DVLDRKIMQL
     EIEIEAIKRE KDEDKLVSLN VDLANLKEER NAIFAKWQSE KTVIDEVQAT KEAIENYKLE
     ADRAEREGDY GKVAELRYGK IKEAQDKLAE LQENLDKNAQ GNSLVKEEVT AEDIAEVVAK
     WTGIPVSKML QGEREKLLKL ESELHKRVVG QEEAIEAVSD AIRRSRAGLH DPKKPIGSFL
     FLGTTGVGKT ELAKALAEYL FDDENAMTRI DMSEYQERHA VSRLVGAPPG YVGYDEGGQL
     TEAVRRRPYS VILLDEIEKA HPDTFNILLQ VLDEGRLTDN KGRTADFKNT IIIMTSNMGS
     HIIQETFDKY PDDTERAIEQ SKTEVLQLLK ETVRPEFLNR IDDIIMFTPL SQANIRSIVR
     LQLDSVIKMV AKEGIIIDAT DDAVDYLARK GFDPQFGARP VKRIIQKEVL NKLSKEILSG
     SVHKDSVILI DAFDDQLVFR NNP
//