CLPB_LEPIN
ID CLPB_LEPIN Reviewed; 860 AA.
AC Q8F509;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Chaperone protein ClpB;
GN Name=clpB; OrderedLocusNames=LA_1879;
OS Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain
OS 56601).
OC Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX NCBI_TaxID=189518;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=56601;
RX PubMed=12712204; DOI=10.1038/nature01597;
RA Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H., Zhang Y.-X.,
RA Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F., Jiang J.-X.,
RA Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H., Yin H.-F., Zhang Y., Zhu G.-F.,
RA Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W., Yao Z.-J., Shen Y.,
RA Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A., Saint Girons I.,
RA Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z., Xu J.-G., Zhao G.-P.;
RT "Unique physiological and pathogenic features of Leptospira interrogans
RT revealed by whole-genome sequencing.";
RL Nature 422:888-893(2003).
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. Acts before DnaK, in the
CC processing of protein aggregates. Protein binding stimulates the ATPase
CC activity; ATP hydrolysis unfolds the denatured protein aggregates,
CC which probably helps expose new hydrophobic binding sites on the
CC surface of ClpB-bound aggregates, contributing to the solubilization
CC and refolding of denatured protein aggregates by DnaK (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- DOMAIN: The Clp repeat (R) domain probably functions as a substrate-
CC discriminating domain, recruiting aggregated proteins to the ClpB
CC hexamer and/or stabilizing bound proteins. The NBD2 domain is
CC responsible for oligomerization, whereas the NBD1 domain stabilizes the
CC hexamer probably in an ATP-dependent manner. The movement of the
CC coiled-coil domain is essential for ClpB ability to rescue proteins
CC from an aggregated state, probably by pulling apart large aggregated
CC proteins, which are bound between the coiled-coils motifs of adjacent
CC ClpB subunits in the functional hexamer (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family. {ECO:0000305}.
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DR EMBL; AE010300; AAN49078.1; -; Genomic_DNA.
DR RefSeq; NP_712060.1; NC_004342.2.
DR RefSeq; WP_000762672.1; NC_004342.2.
DR AlphaFoldDB; Q8F509; -.
DR SMR; Q8F509; -.
DR STRING; 189518.LA_1879; -.
DR PRIDE; Q8F509; -.
DR EnsemblBacteria; AAN49078; AAN49078; LA_1879.
DR KEGG; lil:LA_1879; -.
DR PATRIC; fig|189518.3.peg.1871; -.
DR HOGENOM; CLU_005070_4_0_12; -.
DR InParanoid; Q8F509; -.
DR OMA; SKMMQGE; -.
DR Proteomes; UP000001408; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0034605; P:cellular response to heat; IBA:GO_Central.
DR GO; GO:0042026; P:protein refolding; IEA:InterPro.
DR Gene3D; 1.10.1780.10; -; 1.
DR Gene3D; 3.40.50.300; -; 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 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; SSF52540; SSF52540; 2.
DR SUPFAM; SSF81923; SSF81923; 1.
DR TIGRFAMs; TIGR03346; chaperone_ClpB; 1.
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; Chaperone; Coiled coil; Cytoplasm; Nucleotide-binding;
KW Reference proteome; Repeat; Stress response.
FT CHAIN 1..860
FT /note="Chaperone protein ClpB"
FT /id="PRO_0000191134"
FT DOMAIN 3..148
FT /note="Clp R"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 6..71
FT /note="Repeat 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 84..148
FT /note="Repeat 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 161..342
FT /note="NBD1"
FT /evidence="ECO:0000250"
FT REGION 343..550
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 560..768
FT /note="NBD2"
FT /evidence="ECO:0000250"
FT REGION 769..860
FT /note="C-terminal"
FT /evidence="ECO:0000250"
FT COILED 393..527
FT /evidence="ECO:0000250"
FT BINDING 208..215
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 610..617
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 860 AA; 96311 MW; 79DC5525C7AEA41C CRC64;
MKLDKLTSKL NEAIYNAQAS AEKLGNPEIS EEHILKEVLS QPDGLVPLLI SKLNLSPKSF
LESTENALGK QPKVGGNTSA DVGFSRSAVS LLKAADEVRK ELKDEYLSTD HILLGLMKNG
TGSLKTEFLK LGLEYHKLLK ITLENRKGKT IMDDSPEGKT DALAKYAKNL NELAKQGKLD
PVIGRDEEIR RTIQVLSRRT KNNPVLIGEP GVGKTAIVEG LANKIVQGEV PEGIKNKTLY
TLDLGSMIAG AKYRGEFEDR LKALLDEVKS SDGEVILFID EIHTLVGAGA TEGALDASNM
LKPMLARGEL RCIGATTLKE YQKYIEKDAA LERRFQPVYV KEPSVEETVT ILRGLKGRYE
LHHGIRILDS ALIAAATLSN RYISDRFLPD KAVDLIDEAS SKMRIEIDSM PEELDRANKR
IQSLKIEREA LKKEQDTASK ERLKTLERDL SEQEQNFQTL KARWDLEKSK IGRLKQIKEE
IEKYKNLEAE AERRGEINRV AEIRYGKLVD LQKELESANE ELKKQESASR LLKEEVSEED
IANIVSRWTG IPVSKMLQGE RAKLLLMEDV LKTKVIGQDH ALRLVSEAVQ RSRAGIADPN
RPIGTFLFLG PTGVGKTETA KALAEFLFDD VNAMTRIDMS EYMEAHSVAR LIGAPPGYVG
YDEGGQLTEA VRRRPYSLIL FDEIEKANPE VFNIFLQILD EGRLTDGKGR NVDFKNTVII
LTSNIGSEVL GSSEYTSEEK ERLVEQRLKK HFKPEFLNRI DEVILFHSIT DSVIHKIADI
QLEGLRQKAK ENGLDVSFTN ELKDYVSKAG FDAEYGARPL KRLIQREVGN ALSRYILDGK
FTNGQNVTVD YRQGKVVVVV
