CLPB_MYCTU
ID CLPB_MYCTU Reviewed; 848 AA.
AC P9WPD1; L0T577; O53719; P63288;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=Chaperone protein ClpB;
GN Name=clpB; OrderedLocusNames=Rv0384c; ORFNames=MTV036.19c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP INDUCTION BY SIGH.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=11567012; DOI=10.1128/jb.183.20.6119-6125.2001;
RA Raman S., Song T., Puyang X., Bardarov S., Jacobs W.R. Jr., Husson R.N.;
RT "The alternative sigma factor SigH regulates major components of oxidative
RT and heat stress responses in Mycobacterium tuberculosis.";
RL J. Bacteriol. 183:6119-6125(2001).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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 -!- INDUCTION: Expressed following heat shock under control of SigH. There
CC is another promoter. {ECO:0000269|PubMed:11567012}.
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; AL123456; CCP43114.1; -; Genomic_DNA.
DR PIR; C70834; C70834.
DR RefSeq; NP_214898.1; NC_000962.3.
DR RefSeq; WP_003401905.1; NZ_NVQJ01000002.1.
DR PDB; 6DJU; EM; 3.80 A; A/B/C/D/E/F=1-848.
DR PDB; 6DJV; EM; 3.90 A; A/B/C/D/E/F=1-848.
DR PDB; 6ED3; EM; 6.30 A; A/B/C/D/E/F=1-848.
DR PDB; 6W6E; EM; 3.70 A; A/B/C/D/E/F=1-848.
DR PDB; 6W6G; EM; 3.10 A; A/B/C/D/E/F=1-848.
DR PDB; 6W6H; EM; 3.30 A; A/B/C/D/E/F=1-848.
DR PDB; 6W6I; EM; 3.50 A; A/B/C/D/E/F=1-848.
DR PDB; 6W6J; EM; 3.20 A; A/B/C/D/E/F=1-848.
DR PDB; 7L6N; EM; 7.00 A; A/B/C/D/E/F=1-848.
DR PDBsum; 6DJU; -.
DR PDBsum; 6DJV; -.
DR PDBsum; 6ED3; -.
DR PDBsum; 6W6E; -.
DR PDBsum; 6W6G; -.
DR PDBsum; 6W6H; -.
DR PDBsum; 6W6I; -.
DR PDBsum; 6W6J; -.
DR PDBsum; 7L6N; -.
DR AlphaFoldDB; P9WPD1; -.
DR SMR; P9WPD1; -.
DR STRING; 83332.Rv0384c; -.
DR PaxDb; P9WPD1; -.
DR PRIDE; P9WPD1; -.
DR DNASU; 886440; -.
DR GeneID; 886440; -.
DR KEGG; mtu:Rv0384c; -.
DR TubercuList; Rv0384c; -.
DR eggNOG; COG0542; Bacteria.
DR OMA; SKMMQGE; -.
DR PhylomeDB; P9WPD1; -.
DR BioCyc; MetaCyc:G185E-4508-MON; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Chaperone; Coiled coil; Cytoplasm;
KW Nucleotide-binding; Reference proteome; Repeat; Stress response.
FT CHAIN 1..848
FT /note="Chaperone protein ClpB"
FT /id="PRO_0000191146"
FT DOMAIN 1..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..341
FT /note="NBD1"
FT /evidence="ECO:0000250"
FT REGION 342..547
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 557..755
FT /note="NBD2"
FT /evidence="ECO:0000250"
FT REGION 756..848
FT /note="C-terminal"
FT /evidence="ECO:0000250"
FT COILED 392..524
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 607..614
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT HELIX 8..22
FT /evidence="ECO:0007829|PDB:6W6J"
FT TURN 23..25
FT /evidence="ECO:0007829|PDB:6W6J"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:6W6J"
FT HELIX 31..39
FT /evidence="ECO:0007829|PDB:6W6J"
FT HELIX 47..52
FT /evidence="ECO:0007829|PDB:6W6J"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:6W6J"
FT TURN 60..64
FT /evidence="ECO:0007829|PDB:6W6J"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:6W6J"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:6W6J"
FT HELIX 85..97
FT /evidence="ECO:0007829|PDB:6W6J"
FT TURN 98..102
FT /evidence="ECO:0007829|PDB:6W6J"
FT HELIX 108..118
FT /evidence="ECO:0007829|PDB:6W6J"
FT HELIX 120..129
FT /evidence="ECO:0007829|PDB:6W6J"
FT HELIX 133..136
FT /evidence="ECO:0007829|PDB:6W6J"
FT HELIX 141..144
FT /evidence="ECO:0007829|PDB:6W6J"
FT HELIX 160..164
FT /evidence="ECO:0007829|PDB:6W6G"
FT STRAND 165..168
FT /evidence="ECO:0007829|PDB:6W6G"
FT HELIX 169..173
FT /evidence="ECO:0007829|PDB:6W6G"
FT HELIX 184..194
FT /evidence="ECO:0007829|PDB:6W6G"
FT STRAND 197..199
FT /evidence="ECO:0007829|PDB:6W6H"
FT STRAND 202..206
FT /evidence="ECO:0007829|PDB:6W6G"
FT HELIX 213..225
FT /evidence="ECO:0007829|PDB:6W6G"
FT HELIX 230..232
FT /evidence="ECO:0007829|PDB:6W6G"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:6W6J"
FT HELIX 242..245
FT /evidence="ECO:0007829|PDB:6W6G"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:6W6G"
FT STRAND 251..253
FT /evidence="ECO:0007829|PDB:6W6H"
FT HELIX 255..268
FT /evidence="ECO:0007829|PDB:6W6G"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:6W6J"
FT STRAND 275..279
FT /evidence="ECO:0007829|PDB:6W6G"
FT HELIX 280..282
FT /evidence="ECO:0007829|PDB:6W6G"
FT HELIX 301..305
FT /evidence="ECO:0007829|PDB:6W6G"
FT STRAND 312..316
FT /evidence="ECO:0007829|PDB:6W6G"
FT HELIX 317..323
FT /evidence="ECO:0007829|PDB:6W6G"
FT TURN 324..326
FT /evidence="ECO:0007829|PDB:6W6G"
FT HELIX 328..331
FT /evidence="ECO:0007829|PDB:6W6G"
FT STRAND 335..338
FT /evidence="ECO:0007829|PDB:6W6G"
FT HELIX 344..361
FT /evidence="ECO:0007829|PDB:6W6G"
FT HELIX 368..380
FT /evidence="ECO:0007829|PDB:6W6G"
FT HELIX 387..390
FT /evidence="ECO:0007829|PDB:6W6G"
FT HELIX 392..406
FT /evidence="ECO:0007829|PDB:6W6G"
FT STRAND 407..409
FT /evidence="ECO:0007829|PDB:6W6G"
FT TURN 411..415
FT /evidence="ECO:0007829|PDB:6W6G"
FT HELIX 416..427
FT /evidence="ECO:0007829|PDB:6W6G"
FT STRAND 430..432
FT /evidence="ECO:0007829|PDB:6W6G"
FT HELIX 438..468
FT /evidence="ECO:0007829|PDB:6W6G"
FT HELIX 470..476
FT /evidence="ECO:0007829|PDB:6W6H"
FT HELIX 537..544
FT /evidence="ECO:0007829|PDB:6W6G"
FT STRAND 545..547
FT /evidence="ECO:0007829|PDB:6W6H"
FT HELIX 557..568
FT /evidence="ECO:0007829|PDB:6W6G"
FT TURN 569..571
FT /evidence="ECO:0007829|PDB:6W6G"
FT HELIX 576..590
FT /evidence="ECO:0007829|PDB:6W6G"
FT STRAND 596..598
FT /evidence="ECO:0007829|PDB:6W6G"
FT STRAND 602..606
FT /evidence="ECO:0007829|PDB:6W6G"
FT STRAND 608..612
FT /evidence="ECO:0007829|PDB:6W6G"
FT HELIX 615..623
FT /evidence="ECO:0007829|PDB:6W6G"
FT STRAND 624..626
FT /evidence="ECO:0007829|PDB:6W6G"
FT HELIX 628..630
FT /evidence="ECO:0007829|PDB:6W6H"
FT STRAND 631..635
FT /evidence="ECO:0007829|PDB:6W6G"
FT HELIX 636..638
FT /evidence="ECO:0007829|PDB:6W6G"
FT HELIX 643..647
FT /evidence="ECO:0007829|PDB:6W6G"
FT STRAND 655..657
FT /evidence="ECO:0007829|PDB:6W6G"
FT HELIX 665..668
FT /evidence="ECO:0007829|PDB:6W6G"
FT STRAND 669..671
FT /evidence="ECO:0007829|PDB:6W6G"
FT STRAND 675..680
FT /evidence="ECO:0007829|PDB:6W6G"
FT HELIX 681..683
FT /evidence="ECO:0007829|PDB:6W6G"
FT HELIX 689..695
FT /evidence="ECO:0007829|PDB:6W6G"
FT TURN 696..698
FT /evidence="ECO:0007829|PDB:6W6G"
FT STRAND 700..702
FT /evidence="ECO:0007829|PDB:6W6G"
FT STRAND 704..706
FT /evidence="ECO:0007829|PDB:6W6G"
FT STRAND 708..710
FT /evidence="ECO:0007829|PDB:6W6G"
FT STRAND 715..720
FT /evidence="ECO:0007829|PDB:6W6G"
FT STRAND 722..725
FT /evidence="ECO:0007829|PDB:6W6G"
FT STRAND 727..729
FT /evidence="ECO:0007829|PDB:6W6G"
FT HELIX 730..738
FT /evidence="ECO:0007829|PDB:6W6G"
FT HELIX 741..744
FT /evidence="ECO:0007829|PDB:6W6G"
FT HELIX 758..761
FT /evidence="ECO:0007829|PDB:6W6J"
FT HELIX 762..775
FT /evidence="ECO:0007829|PDB:6W6G"
FT TURN 776..780
FT /evidence="ECO:0007829|PDB:6W6G"
FT STRAND 783..785
FT /evidence="ECO:0007829|PDB:6W6G"
FT HELIX 787..796
FT /evidence="ECO:0007829|PDB:6W6G"
FT TURN 800..802
FT /evidence="ECO:0007829|PDB:6W6H"
FT HELIX 805..823
FT /evidence="ECO:0007829|PDB:6W6G"
FT STRAND 826..828
FT /evidence="ECO:0007829|PDB:6W6G"
FT STRAND 834..838
FT /evidence="ECO:0007829|PDB:6W6G"
FT STRAND 840..844
FT /evidence="ECO:0007829|PDB:6W6G"
SQ SEQUENCE 848 AA; 92568 MW; 41CE8DFA9D5EBAC9 CRC64;
MDSFNPTTKT QAALTAALQA ASTAGNPEIR PAHLLMALLT QNDGIAAPLL EAVGVEPATV
RAETQRLLDR LPQATGASTQ PQLSRESLAA ITTAQQLATE LDDEYVSTEH VMVGLATGDS
DVAKLLTGHG ASPQALREAF VKVRGSARVT SPEPEATYQA LQKYSTDLTA RAREGKLDPV
IGRDNEIRRV VQVLSRRTKN NPVLIGEPGV GKTAIVEGLA QRIVAGDVPE SLRDKTIVAL
DLGSMVAGSK YRGEFEERLK AVLDDIKNSA GQIITFIDEL HTIVGAGATG EGAMDAGNMI
KPMLARGELR LVGATTLDEY RKHIEKDAAL ERRFQQVYVG EPSVEDTIGI LRGLKDRYEV
HHGVRITDSA LVAAATLSDR YITARFLPDK AIDLVDEAAS RLRMEIDSRP VEIDEVERLV
RRLEIEEMAL SKEEDEASAE RLAKLRSELA DQKEKLAELT TRWQNEKNAI EIVRDLKEQL
EALRGESERA ERDGDLAKAA ELRYGRIPEV EKKLDAALPQ AQAREQVMLK EEVGPDDIAD
VVSAWTGIPA GRLLEGETAK LLRMEDELGK RVIGQKAAVT AVSDAVRRSR AGVSDPNRPT
GAFMFLGPTG VGKTELAKAL ADFLFDDERA MVRIDMSEYG EKHTVARLIG APPGYVGYEA
GGQLTEAVRR RPYTVVLFDE IEKAHPDVFD VLLQVLDEGR LTDGHGRTVD FRNTILILTS
NLGSGGSAEQ VLAAVRATFK PEFINRLDDV LIFEGLNPEE LVRIVDIQLA QLGKRLAQRR
LQLQVSLPAK RWLAQRGFDP VYGARPLRRL VQQAIGDQLA KMLLAGQVHD GDTVPVNVSP
DADSLILG
