CLPB_SHIFL
ID CLPB_SHIFL Reviewed; 857 AA.
AC Q7UBW5; Q83QH9;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 2.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Chaperone protein ClpB;
GN Name=clpB; OrderedLocusNames=SF2655, S2831;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP SEQUENCE REVISION TO 344; 353; 357 AND 360.
RA Jin Q., Shen Y., Wang J.H., Liu H., Yang J., Yang F., Zhang X.B.,
RA Zhang J.Y., Yang G.W., Wu H.T., Dong J., Sun L.L., Xue Y., Zhao A.L.,
RA Gao Y.S., Zhu J.P., Chen S.X., Yao Z.J., Wang Y., Lu W.C., Qiang B.Q.,
RA Wen Y.M., Hou Y.D.;
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(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; AE005674; AAN44151.2; -; Genomic_DNA.
DR EMBL; AE014073; AAP17974.1; -; Genomic_DNA.
DR RefSeq; NP_708444.2; NC_004337.2.
DR AlphaFoldDB; Q7UBW5; -.
DR SMR; Q7UBW5; -.
DR STRING; 198214.SF2655; -.
DR EnsemblBacteria; AAN44151; AAN44151; SF2655.
DR EnsemblBacteria; AAP17974; AAP17974; S2831.
DR GeneID; 1027322; -.
DR KEGG; sfl:SF2655; -.
DR KEGG; sfx:S2831; -.
DR PATRIC; fig|198214.7.peg.3164; -.
DR HOGENOM; CLU_005070_4_0_6; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; Chromosome.
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 Acetylation; ATP-binding; Chaperone; Coiled coil; Cytoplasm;
KW Nucleotide-binding; Reference proteome; Repeat; Stress response.
FT CHAIN 1..857
FT /note="Chaperone protein ClpB"
FT /id="PRO_0000191174"
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"
FT MOD_RES 96
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 176
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 640
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT CONFLICT 344
FT /note="Q -> E (in Ref. 3; AAP17974)"
FT /evidence="ECO:0000305"
FT CONFLICT 353
FT /note="V -> L (in Ref. 3; AAP17974)"
FT /evidence="ECO:0000305"
FT CONFLICT 357
FT /note="F -> Y (in Ref. 3; AAP17974)"
FT /evidence="ECO:0000305"
FT CONFLICT 360
FT /note="L -> H (in Ref. 3; AAP17974)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 857 AA; 95560 MW; 38FFC6CA99DAD0AC CRC64;
MRLDRLTNKF QLALADAQSL ALGHDNQFIE PLHLMSALLN QEGGSVSPLL TSAGINAGQL
RTDINQALNR LPQVEGTGGD VQPSQDLVRV LNLCDKLAQK RGDNFISSEL FVLAALESRG
TLADILKATG ATTANITQAI EQMRGGESVN DQGAEDQRQA LKKYTIDLTE RAEQGKLDPV
IGRDEEIRRT IQVLQRRTKN NPVLIGEPGV GKTAIVEGLA QRIINGEVPE GLKGRRVLAL
DMGALVAGAK YRGEFEERLK GVLNDLAKQE GNVILFIDEL HTMVGAGKAD GAMDAGNMLK
PALARGELHC VGATTLDEYR QYIEKDAALE RRFQKVFVAE PSVQDTIAIL RGVKERFELL
HHVQITDPAI VAAATLSHRY IADRQLPDKA IDLIDEAASS IRMQIDSKPE ELDRLDRRII
QLKLEQQALM KESDEASKKR LDMLNEELSD KERQYSELEE EWKAEKASLS GTQTIKAELE
QAKIAIEQAR RVGDLARMSE LQYGKIPELE KQLEAATQLE GKTMRLLRNK VTDAEIAEVL
ARWTGIPVSR MMESEREKLL RMEQELHHRV IGQNEAVDAV SNAIRRSRAG LADPNRPIGS
FLFLGPTGVG KTELCKALAN FMFDSDEAMV RIDMSEFMEK HSVSRLVGAP PGYVGYEEGG
YLTEAVRRRP YSVILLDEVE KAHPDVFNIL LQVLDDGRLT DGQGRTVDFR NTVVIMTSNL
GSDLIQERFG ELDYAHMKEL VLGVVSHNFR PEFINRIDEV VVFHPLGEQH IASIAQIQLK
RLYKRLEERG YEIHISDEAL KLLSENGYDP VYGARPLKRA IQQQIENPLA QQILSGELVP
GKVIRLEVNE DRIVAVQ
