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
//