ID A0A512RQZ9_9BACT Unreviewed; 866 AA.
AC A0A512RQZ9;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-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:GEP98127.1};
GN ORFNames=CCY01nite_43870 {ECO:0000313|EMBL:GEP98127.1};
OS Chitinophaga cymbidii.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Chitinophaga.
OX NCBI_TaxID=1096750 {ECO:0000313|EMBL:GEP98127.1, ECO:0000313|Proteomes:UP000321436};
RN [1] {ECO:0000313|EMBL:GEP98127.1, ECO:0000313|Proteomes:UP000321436}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 109752 {ECO:0000313|EMBL:GEP98127.1,
RC ECO:0000313|Proteomes:UP000321436};
RA Hosoyama A., Uohara A., Ohji S., Ichikawa N.;
RT "Whole genome shotgun sequence of Chitinophaga cymbidii NBRC 109752.";
RL Submitted (JUL-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:GEP98127.1}.
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DR EMBL; BKAU01000005; GEP98127.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A512RQZ9; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000321436; 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: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:UP000321436};
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 866 AA; 96993 MW; 7722F449AA3C4D1D CRC64;
MNLNNFTIKS QETLQHAQQL AFNDKNTAIE TGHLLKALLA DEDNSIEYLL KKNGVNTAFL
ESKVDEQIKK YTVIVNGEGG QTLSRDANNA LLRAGASIQE FKDEFVSVEH LLLGLLGGSD
DTAKLLKSAG LTEKGLKAAI TELRKGGTVN SQTAEAQYNS LEKYAKNLNE LARAGKLDPV
IGRDEEIRRT LHILSRRSKN NPILVGEPGV GKTAIAEGLA HRVVNGDVPE NLHNKIIYAL
DMGALMAGAK YRGEFEERLK AVVKEVSDSN GGIILFIDEI HTLIGAGAME GAMDAANILK
PALARGELRA IGATTLNEYQ KYFEKDKALE RRFQKVLIDE PSVEDAISIL RGLKERYENH
HHVLIKDEAI IAAVELSHRY ITDRFLPDKA IDLIDESAAK LRLEMNSMPE ELDELERRIR
QLEIEKEAIK RENDEDKLRE LSAEIARLSD ERNTFKSKWK EEKELVDKVQ NAKAAIEDLK
LAAEQAERNG DYGKVAEIRY GKIKEQEEQV LQLTVELNAI SAQHKRLLKE EVDAEDIAEN
VAKATGIPVS RMLQSERDKL LTLEDELHKR VVGQDEAITA VADAIRRSRA GLHDPKRPIG
SFIFLGTTGV GKTELAKALA DFLFDDESMM TRIDMSEYQE KHAVSRLVGA PPGYVGYDEG
GQLTEAVRRK PYSVVLLDEI EKAHPDVFNI LLQVLDDGRL TDNKGRVVNF KNTIIIMTSN
MGSHIIQENF EKINEGNRDE IVDGTKEEVM NLLRQTIRPE FLNRVDEVIM FQPLLRSEVR
GIINIQLQQL KELVAKNGMI LEFSDYALDY LAEQGYDPQF GARPLKRLIQ KEIVNLLSKK
ILAGDVDKSK PVLVDVFDGV VVIRNK
//