ID A0A5J5IHX4_9BACT Unreviewed; 873 AA.
AC A0A5J5IHX4;
DT 11-DEC-2019, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 1.
DT 13-SEP-2023, entry version 14.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:KAA9039168.1};
GN ORFNames=FW778_10055 {ECO:0000313|EMBL:KAA9039168.1};
OS Ginsengibacter hankyongi.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Ginsengibacter.
OX NCBI_TaxID=2607284 {ECO:0000313|EMBL:KAA9039168.1, ECO:0000313|Proteomes:UP000326903};
RN [1] {ECO:0000313|EMBL:KAA9039168.1, ECO:0000313|Proteomes:UP000326903}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BR5-29 {ECO:0000313|EMBL:KAA9039168.1,
RC ECO:0000313|Proteomes:UP000326903};
RA Im W.-T.;
RT "Draft genome sequence of Ginsengibacter sp. BR5-29.";
RL Submitted (SEP-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:KAA9039168.1}.
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DR EMBL; VYQF01000002; KAA9039168.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5J5IHX4; -.
DR Proteomes; UP000326903; 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:UP000326903};
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 398..523
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 873 AA; 98338 MW; E801E551D8346270 CRC64;
MNLNNLTIKS QEIFQKAQQL AFNEKNPNIE TEHLLKALLA DEDSPVEYLL KKNNINVNFV
EGKVDESLQK LPKMGEGEPA QVISRDLNNV LLRATATLKT FKDEFISVEH LLLAIVQGND
NAAKILKDAG LTEKSLIAAI KELKKGSTVS SQTSETQFNA LNKYAKNLNE LARSNKLDPV
IGRDEEIRRT LHILSRRTKN NPILVGEPGV GKTAIAEGLA HRIVNGDVPE NLRSKIIFAL
DMGLLIAGAK YKGEFEERLK SVIKEVGDSN GEIVLFIDEI HTLVGAGASE GAMDAANILK
PALARGELRA IGATTLNEYQ KFFEKDKALE RRFQKVMVDE PNVEDAISIL RGIKDKYETH
HHVRIKDEAI IAAVELSHRY ITDRFLPDKA IDLIDESAAK LRLEMNSMPE ELDKLERAIR
QLEIEREAIK REKDAAKLKE LNTEISNLSV QRDTFKAKWQ QEKEIVEKVQ NAKAEIENLK
MAAEKAEREG DYGKVAEIRY GKLQDQEKII NDFTVQLNEI SEKRLLKEEV DAEDIAESVA
KATGIPVSKM MQSEKDKLLN LEDELHKRVI GQDEAIEAVA DAIRRSSAGL HDPKKPLGSF
IFLGTTGVGK TELAKALAEY LFNDDSMMTR IDMSEYQEKH SVSRLVGAPP GYVGYDEGGQ
LTEAVRRKPY SVILLDEIEK AHPDVFNILL QVLDDGRLTD NKGRVVNFKN TIIIMTSNMG
SHIIQANFDN VTEENKVKVV DETRREVLEL LRQTIRPEFL NRIDEIIMFQ PLMKGEIKDI
IRIQLQDLKE QLQKNGVVLE FSEYALDYLA ENGFDPQFGA RPLKRLIQKQ IVNQLSKKLL
SGTIDKSHPV LVDVFDGVVV FRNDVNMHEK TVA
//