ID W3AMJ1_9FIRM Unreviewed; 862 AA.
AC W3AMJ1;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=UYO_1816 {ECO:0000313|EMBL:ETP72215.1};
OS Lachnospiraceae bacterium JC7.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1165092 {ECO:0000313|EMBL:ETP72215.1, ECO:0000313|Proteomes:UP000018967};
RN [1] {ECO:0000313|EMBL:ETP72215.1, ECO:0000313|Proteomes:UP000018967}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JC7 {ECO:0000313|EMBL:ETP72215.1,
RC ECO:0000313|Proteomes:UP000018967};
RA Rosewarne C.P., Cheung J.L., Evans P.N., Tomkins N.W., Denman S.E.,
RA O Cuiv P., Morrison M.;
RT "Isolation and genomic characterisation of Lachnospiraceae sp. JC7, a newly
RT identified member of the bovine rumen core microbiota.";
RL Submitted (JUL-2012) 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:ETP72215.1}.
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DR EMBL; ALYD01000019; ETP72215.1; -; Genomic_DNA.
DR AlphaFoldDB; W3AMJ1; -.
DR PATRIC; fig|1165092.3.peg.1797; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000018967; 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..146
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 412..492
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 862 AA; 97807 MW; 5ACBAFD6B7D2C01A CRC64;
MNINKFTKKS IEAINKCQDI ITEYGNQYVE QIHLLYSLIT IDESLIAQLL KKMEVPVDEF
LERLEAEISK LPKVTGTGQM YMSQAANLAL TRAEDHSKSM GDEYVSVEHI FLSIMKEADP
TVKRLFNEYN ITKDGFLKAL SEVRGNQRVV SDNPEDVYDT LNKYGYEMVQ RARDQKMDPI
IGRDDEIRNI IRILSRKTKN NPVLIGEPGV GKTAVVEGLA QRIAKGEVPE SLKDKKVFAL
NMGSLVAGAK YRGEFEERLK AVLDEVKKSE GQILMFIDEL HTIVGAGRTD GAMDAGNILK
PMLARGELHC IGATTLDEYH KYIEKDAALE RRFQPVQIDQ PDVEDTIYIL RGIKESYEQY
HGVTITDNAL VAAATLSDRY ISDRFLPDKA IDLVDEACSM VKTQMESMPE DMAEIKSRLT
QLRMEQISLK KEDDKLSKER LQEIEKELAE LQSEFDAKMA QWDNEKNSAE NLQKLREQKD
RIRKDIEKSM QMADYDKASK LQYQDLPEIE RKLSEVENSV HGEDKSLLQE TVTEEEIGKI
VSRWTGIPVS KLNESERSKV LHLDLEIHKR LIGQDEAVEK VVEAIQRSKA GIKDPGRPIG
SFLFMGPTGV GKTELAKALA QNLFDDENAM VRIDMSEYME KYSVSRLIGA APGYVGYEEG
GQLTEAVRRK PYSVVLFDEI EKAHPDVFNI LLQVLDDGRI TDSQGKTVDF KNTIIILTSN
LGAQYLLEGI DGNGNITEAA RKNVHDELFK SFRPEFLNRL DEIIMFKPLS KDNIGNITDL
MISDINKRLS DRQLSIELTD AAKEYVADYG YEPQFGARPL RRFIQKNVET LVARCILEDK
VQEGDTIVID QRLGKLGIEI RH
//
