ID M6JGA4_9LEPT Unreviewed; 859 AA.
AC M6JGA4;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:EMN20701.1};
GN ORFNames=LEP1GSC063_3168 {ECO:0000313|EMBL:EMN20701.1};
OS Leptospira santarosai serovar Arenal str. MAVJ 401.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=1049976 {ECO:0000313|EMBL:EMN20701.1, ECO:0000313|Proteomes:UP000012106};
RN [1] {ECO:0000313|EMBL:EMN20701.1, ECO:0000313|Proteomes:UP000012106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAVJ 401 {ECO:0000313|EMBL:EMN20701.1,
RC ECO:0000313|Proteomes:UP000012106};
RA Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D.,
RA Sanka R., DePew J., Purushe J., Hartskeerl R.A., Ahmed A.,
RA van der Linden H., Goris M.G.A., Vinetz J.M., Sutton G.G., Nierman W.C.,
RA Fouts D.E.;
RL Submitted (JAN-2013) 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:EMN20701.1}.
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DR EMBL; AHMU02000065; EMN20701.1; -; Genomic_DNA.
DR RefSeq; WP_004465007.1; NZ_AHMU02000065.1.
DR AlphaFoldDB; M6JGA4; -.
DR Proteomes; UP000012106; 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..148
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 407..535
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 859 AA; 96159 MW; 9595EBF6C5353784 CRC64;
MKLDKLTAKL NEALHNAQSL AEKSGNPEIS EEHILREVLV QTDGLAPLLI SKLDLNPKSF
LAKTEDALGR LPKVGGTSSA DVGFSRSAVS LLKTADEIRK ELKDEYLSTD HILLGLMKGG
VGPLKEEFLK LGLEYSKLLK ITLENRKGKT IMDDSPEGKT DALAKYAKNL NELAKQGKLD
PVIGRDEEIR RTIQVLSRRT KNNPVLIGEP GVGKTAIVEG LANKIVQGEV PEGIRNKTLY
TLDLGSMIAG AKYRGEFEDR LKALLDEVKA SDGEVILFID EIHTLVGAGA TEGALDASNM
LKPMLARGEL RCIGATTLKE YQKYIEKDAA LERRFQPVYV KEPSVEETVT ILRGLKGRYE
LHHGIRILDS ALIAAATLSN RYIADRFLPD KAVDLIDEAS SKMRIEIDSM PEELDRASKR
IQSLKIEREA LKKERDSASK ERLKTLEKDL AEQEQNFQTL KARWDLEKSK IFRLKQIKEE
IEKYKNLEAD AERKGEINRV AEIRYGKLVD LQKEFEAANE ELKKQEGASR LLKEEVSEED
IANIVSRWTG IPVSKMLQGE RAKLLLMEDV LKARVIGQDH ALKLVSEAVQ RSRAGIADPN
RPIGTFLFLG PTGVGKTETA KALAEFLFDD ANAMHRIDMS EYMEAHSVAR LIGAPPGYVG
YDEGGQLTEA VRRRPYSLIL FDEVEKANPD VFNIFLQILD EGRLTDGKGR NVDFKNTVII
LTSNIGSDIL GSSEYSTEEK ERLVEERLKK QFKPEFLNRI DEVILFHSIT NSVIHKIAEI
QLEGLKQKAK ENGLDVRFTD ELKDYVSRAG FDAEYGARPL KRLIQREVGN ALSRYILNGK
FSDGQKVTAD YKQGRVIVV
//
