ID A0A5D8YN71_9SPHI Unreviewed; 865 AA.
AC A0A5D8YN71;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 13-SEP-2023, entry version 13.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:TZF83830.1};
GN ORFNames=FW774_10220 {ECO:0000313|EMBL:TZF83830.1};
OS Pedobacter sp. BS3.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=2567937 {ECO:0000313|EMBL:TZF83830.1, ECO:0000313|Proteomes:UP000325329};
RN [1] {ECO:0000313|EMBL:TZF83830.1, ECO:0000313|Proteomes:UP000325329}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BS3 {ECO:0000313|EMBL:TZF83830.1,
RC ECO:0000313|Proteomes:UP000325329};
RA Im W.-T.;
RT "Draft genome sequence of Pedobacter sp.BS3.";
RL Submitted (AUG-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:TZF83830.1}.
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DR EMBL; VTRT01000003; TZF83830.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5D8YN71; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000325329; 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:UP000325329};
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 865 AA; 97499 MW; 14307B95D6DDC818 CRC64;
MNFNNFTIKA QEAIQKASEI AVGNQQQAIE TAHLLKGLLT VDENVVSYLL KKLNVNINRL
NSVLDAQIQS FPKVSGSEVY LSSGANSALQ KAQSYLKEFK DEFVSVEHIL LGLLNTGDKV
SGMLKDAGVT EKDLKKAITE LRGDSRVTDQ NAEATYNALN KYARNLNEYA ESGKLDPVIG
RDEEIRRVIQ ILSRRTKNNP ILIGEPGVGK TAIAEGIAFR IIKGDVPENL KSKTVYSLDM
GALIAGAKYK GEFEERLKAV VKEVTQSDGE IILFIDEIHT LVGAGGGGEG AMDAANILKP
ALARGELRAI GATTLNEYQK YLEKDKALER RFQKVMVDEP DTQDAISILR GLKERYETHH
KVRIKDEAII AAVELSQRYI SDRFLPDKAI DLMDEAASKL RLEMDSVPEE VDELDRRIMQ
LEIEREAIKR EKDEKKVADL SEEIANLSSQ RDSLKAKWQS EKDLVDKVNT QIEQIETYKL
EAEQAERAGD YGKVAELRYG KIKEAQDEVE RLKKELETQQ HNESRMLKEE VTAEDIAGVV
SRWTGIPVTK MVQSEREKLL HLEEELHKRV AGQQEAIEAI SDAIRRSRAG LHDKRKPIGS
FIFLGTTGVG KTELAKALAE FLFNDEHALV RIDMSEYQER HAVSRLIGAP PGYVGYDEGG
QLTEAVRRKP YSVILLDEIE KAHPDVFNIL LQVLDDGRLT DNKGRVVNFK NTIIIMTSNI
GSHLIQENFK DINEDNQEEI MAKTKNELFE LLKQTIRPEF LNRIDDLIMF TPLGRDEIRE
IVDLQFKGVQ QTLAEMGIQI EASPEALDWL AQLGYDPQFG ARPLKRVIQK RILNELSKDI
LAGKVDKDSK IKLDVFDNHF VFMNQ
//