ID A0A3M9MWV7_9BACT Unreviewed; 872 AA.
AC A0A3M9MWV7;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:RNI29970.1};
GN ORFNames=EFA69_10610 {ECO:0000313|EMBL:RNI29970.1};
OS Rufibacter immobilis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Rufibacter.
OX NCBI_TaxID=1348778 {ECO:0000313|EMBL:RNI29970.1, ECO:0000313|Proteomes:UP000271010};
RN [1] {ECO:0000313|EMBL:RNI29970.1, ECO:0000313|Proteomes:UP000271010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCC P1 {ECO:0000313|EMBL:RNI29970.1,
RC ECO:0000313|Proteomes:UP000271010};
RA Yang Y.;
RT "Rufibacter latericius sp. nov., isolated from water in Baiyang Lake.";
RL Submitted (NOV-2018) 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:RNI29970.1}.
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DR EMBL; RJJE01000009; RNI29970.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M9MWV7; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000271010; 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 78, MITOCHONDRIAL; 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 Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..144
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 404..529
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 872 AA; 97841 MW; B04FF44E68830246 CRC64;
MNFNNYTIKS QEAVQKATEI AGGNQQQAIE TGHLLKGILQ TDENVTGFYL KKLGVNVNQF
NTRLDEIVNA YPKVSGGSPY LANEAAAALQ KANSYLKEFG DEYVAIEHLL LGLLAGRDKT
ATLLKDSGIS EKGLKAAIKE LRGDSKVTDQ NAEAKYNSLK RYAIDLNEQA RLGKIDPVIG
RDEEIRRVLQ ILSRRTKNNP ILLGEPGVGK TAIVEGLAQR IVSGDVPENL KSKTIMSLDM
GLLVAGAKYK GEFEERLKAV IKEVVDSEGE IVLFIDEIHT LIGAGAGGDS AMDAANLLKP
ALARGELHAI GATTLKEYQK YFEKDKAMER RFQSVTVDEP SIPDAISILR GIKEKYELHH
GVRIKDDAII AAVELSSRYI TDRFLPDKAI DLVDEAASKL RIEIDSLPVE LDEVQRKIMQ
LEIEREAIRR ENDKEKENLL SKEIADLSET RDALRAKWQS EKQVIEGIQK QKEAIEQYKL
EAEQAERAGD YGRVAELRYG KIQEAEAKLK ELQQQVQEQQ DGDHMLQEEV TSEDIAEVVA
KWTGVPVNKM LQSDREKLLH LEEELGRRVA GQEEAIAAIS DAVRRSRAGL QDPKRPIGSF
IFLGTTGVGK TELAKALADF LFNDENAMVR IDMSEYQERH AVSRLVGAPP GYVGYDEGGQ
LTEAVRRKPY SVILLDEIEK AHPDVFNILL QVLDDGRLTD NKGRVANFKN TIIIMTSNIG
AHIIQENFQH LDELNPEPTI DRTRDEVFEV LKKTLRPEFL NRIDELIMFR PLSSREIRKI
VDIQFRHIQE RLEESGIRLE ATDEVLDFLG QEGYDPQFGA RPLKRVLQRR VLNELSKAIL
AGDIRKDAVV EAVLEDGNIR FVNVDIDLPI DR
//
