ID   CLPB_LEPIC              Reviewed;         860 AA.
AC   Q72QU2;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Chaperone protein ClpB;
GN   Name=clpB; OrderedLocusNames=LIC_12017;
OS   Leptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni
OS   (strain Fiocruz L1-130).
OC   Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX   NCBI_TaxID=267671;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fiocruz L1-130;
RX   PubMed=15028702; DOI=10.1128/jb.186.7.2164-2172.2004;
RA   Nascimento A.L.T.O., Ko A.I., Martins E.A.L., Monteiro-Vitorello C.B.,
RA   Ho P.L., Haake D.A., Verjovski-Almeida S., Hartskeerl R.A., Marques M.V.,
RA   Oliveira M.C., Menck C.F.M., Leite L.C.C., Carrer H., Coutinho L.L.,
RA   Degrave W.M., Dellagostin O.A., El-Dorry H., Ferro E.S., Ferro M.I.T.,
RA   Furlan L.R., Gamberini M., Giglioti E.A., Goes-Neto A., Goldman G.H.,
RA   Goldman M.H.S., Harakava R., Jeronimo S.M.B., Junqueira-de-Azevedo I.L.M.,
RA   Kimura E.T., Kuramae E.E., Lemos E.G.M., Lemos M.V.F., Marino C.L.,
RA   Nunes L.R., de Oliveira R.C., Pereira G.G., Reis M.S., Schriefer A.,
RA   Siqueira W.J., Sommer P., Tsai S.M., Simpson A.J.G., Ferro J.A.,
RA   Camargo L.E.A., Kitajima J.P., Setubal J.C., Van Sluys M.A.;
RT   "Comparative genomics of two Leptospira interrogans serovars reveals novel
RT   insights into physiology and pathogenesis.";
RL   J. Bacteriol. 186:2164-2172(2004).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE016823; AAS70592.1; -; Genomic_DNA.
DR   RefSeq; WP_000762669.1; NC_005823.1.
DR   AlphaFoldDB; Q72QU2; -.
DR   SMR; Q72QU2; -.
DR   PaxDb; Q72QU2; -.
DR   EnsemblBacteria; AAS70592; AAS70592; LIC_12017.
DR   GeneID; 61141909; -.
DR   KEGG; lic:LIC_12017; -.
DR   HOGENOM; CLU_005070_4_0_12; -.
DR   OMA; SKMMQGE; -.
DR   Proteomes; UP000007037; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0042026; P:protein refolding; IEA:InterPro.
DR   GO; GO:0009408; P:response to heat; 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; Repeat;
KW   Stress response.
FT   CHAIN           1..860
FT                   /note="Chaperone protein ClpB"
FT                   /id="PRO_0000191133"
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;  96325 MW;  79C4F62FF4BC341C 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
     LTSNIGSEIL GSSEYTSEEK ERLVEQRLKK HFKPEFLNRI DEVILFHSIT DSVIHKIADI
     QLEGLRQKAK ENGLDVSFTN ELKDYVSKAG FDAEYGARPL KRLIQREVGN ALSRYILDGK
     FTNGQNVTVD YRQGKVVVVV