ID A0A163VA12_9BACT Unreviewed; 866 AA.
AC A0A163VA12; A0A163VR11;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=AO394_00435 {ECO:0000313|EMBL:KZD17994.1};
OS Candidatus Fermentibacter daniensis.
OC Bacteria; Candidatus Fermentibacteria; Candidatus Fermentibacteria (class);
OC Candidatus Fermentibacterales; Candidatus Fermentibacteraceae;
OC Fermentibacter.
OX NCBI_TaxID=1729713 {ECO:0000313|EMBL:KZD17994.1, ECO:0000313|Proteomes:UP000076793};
RN [1] {ECO:0000313|EMBL:KZD17994.1, ECO:0000313|Proteomes:UP000076793}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Dam_1 {ECO:0000313|EMBL:KZD17994.1};
RX PubMed=27058503;
RA Kirkegaard R.H., Dueholm M.S., McIlroy S.J., Nierychlo M., Karst S.M.,
RA Albertsen M., Nielsen P.H.;
RT "Genomic insights into members of the candidate phylum Hyd24-12 common in
RT mesophilic anaerobic digesters.";
RL ISME J. 0:0-0(2016).
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:KZD17994.1}.
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DR EMBL; LKHB01000182; KZD17994.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A163VA12; -.
DR Proteomes; UP000076793; 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 410..459
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 866 AA; 95603 MW; AF1CAB0A73A7EF14 CRC64;
MNTDRYTIKA GEAIRDAIGF ASGNSEVTCL HLAAALLSDP ESTVSSVLSK LGADPGELRE
AISQALDRLP RVSGGSGPAM SAGLRKALSA AEGASARLKD DYTALEHLFM GLYESGDRQM
TALLSSAGFT LDDFLRALAE VRGASRAGSE NAEENYEALD KYTRDLTRLA LQQKLDPVIG
RDEEIRRVMQ VLGRRRKNNP VLLGEPGVGK TAVVEGLAGR IASGDTPEGL RDKRVLALDM
GALVAGTKFR GEFEERLKSV LNEITSSDGR IILFIDEMHT LVGAGAAEGS VDAANMLKPA
LARGELHCIG ATTLDEYRKY IEKDAALERR FQPVMVQPPD VSDTISILRG LRERYEVHHG
IRIQDSALIA AATLSDRYVS GRFLPDKAID LVDEAASRLR IEIDSMPVEV DEIRRRIMQL
EIEREGLQRE RDEASRARLE KVGAELAELG ERRTALEARW KSEKELIEQI REIARQTEEM
KTAESIAERE GDLGKVAEIR YGKLRDLDSR AADLRARLGG LQENGAMLAE EVTPEHIAEV
VSRWTGVPVT RMLEGERERL LRMEEALRER VVGQEEAVEA VSEAVRRARA GVQDPNRPLG
SFIFMGPTGV GKTELARALS EFLFDSEASM IRLDMSEFME KHSVSRMIGA PPGYIGYDEG
GHLTEAVRRR PYSVVLLDEI EKAHPDVFNI LLQVLDDGRL TDGQGRTVDF RNCLLIMTSN
VGSEWIAASA GSMPAPDMTA RARRDLEAQF RPEFLNRIDE VIVFRPLDVV DLRRIVSIQL
ARLNRLLEQS GISVEADEKA LDLLAERGFD PVYGARPLKR VIQKSVQNTL ATRMLSGELH
AGSSVSLTVE NGELSFHQKE KEPSPE
//
