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Database: UniProt
Entry: A0A291QX57_9BACT
LinkDB: A0A291QX57_9BACT
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ID   A0A291QX57_9BACT        Unreviewed;       866 AA.
AC   A0A291QX57;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034,
GN   ECO:0000313|EMBL:ATL48525.1};
GN   ORFNames=COR50_15895 {ECO:0000313|EMBL:ATL48525.1};
OS   Chitinophaga caeni.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Chitinophaga.
OX   NCBI_TaxID=2029983 {ECO:0000313|EMBL:ATL48525.1, ECO:0000313|Proteomes:UP000220133};
RN   [1] {ECO:0000313|EMBL:ATL48525.1, ECO:0000313|Proteomes:UP000220133}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=13 {ECO:0000313|EMBL:ATL48525.1,
RC   ECO:0000313|Proteomes:UP000220133};
RA   Jin D., Kong X., Deng Y., Bai Z.;
RT   "Paenichitinophaga pekingensis gen. nov., sp. nov., isolated from activated
RT   sludge.";
RL   Submitted (OCT-2017) 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; CP023777; ATL48525.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A291QX57; -.
DR   KEGG; cbae:COR50_15895; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000220133; 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:0003723; F:RNA binding; 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   InterPro; IPR001313; Pumilio_RNA-bd_rpt.
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.
DR   PROSITE; PS50302; PUM; 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:UP000220133};
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..530
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   866 AA;  97212 MW;  A28299666CAE92DF CRC64;
     MNLNNFTIKS QETLQQAQQL AFNHQNASIE SGHLLKALLD DEDNSVEYLL KKNDVNTSFI
     QNKLNEQLQK YPVISNGEGG QTLSRDANNA LLRAGSSIKE FKDEFVSVEH LLLGLLGGSD
     DTAKLLKDAG LTEKGLKAAI TELRKGGTVN SQTADAQYNS LEKYAKNLNE LASAGKLDPV
     IGRDEEIRRT LHILSRRSKN NPILVGEPGV GKTAIAEGLA HRIVNGDVPD NLKSKIIFAL
     DMGSLMAGAK YRGEFEERLK AVVKEVSESN GEIILFIDEI HTLVGAGAME GAMDAANILK
     PALARGELRA IGATTLNEYQ KYFEKDKALE RRFQKVLIDE PTAEDAISIL RGIKEKYESH
     HHVRIKDEAI IAAVELSQRY ITDRFLPDKA IDLIDESAAK LRLEMNSMPE ELDELERRIR
     QLEIEREAIK RENDEAKLRE LAEEISRLSE ERNTFTAKWK QEKELVDQVQ NAKAAIENFK
     HEAETAERNG DYGRVAEIRY GKVKEQEELV TKLTGELEAL STNNKRLLKE EVDAEDIAEN
     VAKATGIPVA KMMQSEREKL LQLEEELHKR VVGQDEAIVA VADAIRRSRA GLQDPKRPIG
     SFIFLGTTGV GKTELAKALA DYLFDDDSMM TRIDMSEYQE KHAVSRLVGA PPGYVGYDEG
     GQLTEAVRRK PYSVVLLDEI EKAHPDVFNI LLQVLDDGRL TDNKGRVVNF KNTIIIMTSN
     MGSHIIQENF EKLSAENKEE VVENTKEQVM NLLKQTIRPE FLNRVDEVIM FQPLMRSEVK
     GIINIQLQHL KDLVAKNGMI LEFSEYALDY LSEQGYDPQF GARPLKRLIQ KEIVNLLSKK
     ILAGEIDKTK PVLIDVFDGV VVIRNK
//
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