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Database: UniProt
Entry: A0A5J5IHX4_9BACT
LinkDB: A0A5J5IHX4_9BACT
Original site: A0A5J5IHX4_9BACT 
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
//
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