CLPB_VIBCH
ID CLPB_VIBCH Reviewed; 857 AA.
AC Q9KU18;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Chaperone protein ClpB;
GN Name=clpB; OrderedLocusNames=VC_0711;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
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; AE003852; AAF93876.1; -; Genomic_DNA.
DR PIR; A82290; A82290.
DR RefSeq; NP_230360.1; NC_002505.1.
DR RefSeq; WP_001235051.1; NZ_LT906614.1.
DR AlphaFoldDB; Q9KU18; -.
DR SMR; Q9KU18; -.
DR STRING; 243277.VC_0711; -.
DR PRIDE; Q9KU18; -.
DR DNASU; 2615715; -.
DR EnsemblBacteria; AAF93876; AAF93876; VC_0711.
DR GeneID; 57739423; -.
DR KEGG; vch:VC_0711; -.
DR PATRIC; fig|243277.26.peg.681; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_0_6; -.
DR OMA; SKMMQGE; -.
DR BioCyc; VCHO:VC0711-MON; -.
DR Proteomes; UP000000584; Chromosome 1.
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..857
FT /note="Chaperone protein ClpB"
FT /id="PRO_0000191200"
FT DOMAIN 3..146
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 83..146
FT /note="Repeat 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 159..340
FT /note="NBD1"
FT /evidence="ECO:0000250"
FT REGION 341..545
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 555..765
FT /note="NBD2"
FT /evidence="ECO:0000250"
FT REGION 766..857
FT /note="C-terminal"
FT /evidence="ECO:0000250"
FT COILED 391..525
FT /evidence="ECO:0000250"
FT BINDING 206..213
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 605..612
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 857 AA; 95828 MW; 2AAA741648FDEBB1 CRC64;
MRLDRFTSKF QIAISDAQSL ALGRDHQYIE PVHLMVALLD QNGSPIRPLL TMLNVDVMQL
RSKLGEMLDR LPKVSGIGGD VQLSSALGSL FNLCDKVAQK RQDAYISSEI YLLAAIEDKG
PLGHLLKEFG LTEKKVSEAI EKIRGGQKVN DPNAEELRQA LEKFTIDLTE RAEQGKLDPV
IGRDDEIRRT IQVLQRRTKN NPVIIGEPGV GKTAIVEGLA QRIINNEVPE GLRGRRVLSL
DMGALVAGAK YRGEFEERLK SVLNELAKEE GNIILFIDEL HTMVGAGKGE GSMDAGNMLK
PALARGELHC VGATTLDEYR QYIEKDPALE RRFQKVLVDE PTVEDTIAIL RGLKERYELH
HHVEITDPAI VAAASLSHRY ISDRQLPDKA IDLIDEAASS IRMQIDSKPE ALDKLERKII
QLKIEQQALS NEHDEASEKR LAILNEELQE KERDYAELEE VWKAEKAALS GTQHIKAALE
QARMDLEVAR RAGDLNRMSE LQYGRIPELE KQLDLAAQAE MQEMTLLRNK VTDAEIAEVL
SKQTGIPVSK MLEAEKEKLL RMEDVLHKRV IGQKEAVEVV ANAIRRSRAG LSDPNRPIGS
FLFLGPTGVG KTELCKTLAN FLFDSEDAMV RVDMSEFMEK HSVARLVGAP PGYVGYEEGG
YLTEAVRRKP YSVILLDEVE KAHPDVFNIL LQVLDDGRLT DGQGRTVDFR NTVVIMTSNL
GSSRIQENFA RLDYQGIKEQ VMDVVSKHFR PEFLNRVDES VVFHPLGQEH IKSIASIQLA
RLRQRLAERD YQLEVDDEAL DLIAHVGFDP VYGARPLKRA IQQNVENPLA KSILAGKFLP
GSPILLSVKD GNIFASQ
