CLPB_LISMO
ID CLPB_LISMO Reviewed; 866 AA.
AC Q8Y570;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Chaperone protein ClpB;
GN Name=clpB; OrderedLocusNames=lmo2206;
OS Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=169963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
RN [2]
RP FUNCTION IN VIRULENCE.
RC STRAIN=LO28 / Serovar 1/2c;
RX PubMed=14762012; DOI=10.1128/jb.186.4.1165-1174.2004;
RA Chastanet A., Derre I., Nair S., Msadek T.;
RT "clpB, a novel member of the Listeria monocytogenes CtsR regulon, is
RT involved in virulence but not in general stress tolerance.";
RL J. Bacteriol. 186:1165-1174(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 Required for induced thermotolerance, but not for general stress
CC survival. Involved in virulence, maybe acting as a chaperone in a key
CC process for pathogenic development. {ECO:0000250,
CC ECO:0000269|PubMed:14762012}.
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; AL591982; CAD00284.1; -; Genomic_DNA.
DR PIR; AF1350; AF1350.
DR RefSeq; NP_465730.1; NC_003210.1.
DR RefSeq; WP_003723824.1; NZ_CP023861.1.
DR AlphaFoldDB; Q8Y570; -.
DR SMR; Q8Y570; -.
DR STRING; 169963.lmo2206; -.
DR PaxDb; Q8Y570; -.
DR EnsemblBacteria; CAD00284; CAD00284; CAD00284.
DR GeneID; 985416; -.
DR KEGG; lmo:lmo2206; -.
DR PATRIC; fig|169963.11.peg.2258; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_0_9; -.
DR OMA; GPEHILM; -.
DR PhylomeDB; Q8Y570; -.
DR BioCyc; LMON169963:LMO2206-MON; -.
DR Proteomes; UP000000817; Chromosome.
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 1: Evidence at protein level;
KW ATP-binding; Chaperone; Coiled coil; Cytoplasm; Nucleotide-binding;
KW Reference proteome; Repeat; Stress response.
FT CHAIN 1..866
FT /note="Chaperone protein ClpB"
FT /id="PRO_0000191137"
FT DOMAIN 3..148
FT /note="Clp R"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 6..70
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..551
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 561..772
FT /note="NBD2"
FT /evidence="ECO:0000250"
FT REGION 773..866
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 611..618
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 866 AA; 97563 MW; D5BD7B9E68303549 CRC64;
MDLQKFTQQV QQTIADAQNL AIASEHQEID VAHVFKVLLT ESDFAKRVYD VAEVDTDALQ
KVIENTLEKI PVVSGSGVNY GQAMSQALFQ LMRDAEKEQQ QLEDDFVSTE HLILAVMDQK
SNPITAELKN QHKAKKQIKE AILKIRGGKR VTSQNAEENY EALTKYGRDL VAEVRSGKLD
PVIGRDAEIR NVIRILSRKT KNNPVLIGEP GVGKTAIVEG LAQRIVRKDV PEGLKDKTII
SLDIGSLIAG AKYRGEFEER LKAVLQEVKQ SDGQILLFID EIHTIVGAGK TDGAMDAGNM
LKPMLARGEL HCIGATTLDE YRQYIEKDAA LERRFQKVLV PEPTVEDTVS ILRGLKERFE
IHHGVNIHDN ALVAAASLSN RYITDRFLPD KAIDLVDEAC ATIRVEIDSM PSELDEVTRK
VMQLEIEEAA LKEEKDPASE RRLEILQREL ADYKEEANQM KSKWESEKNE ISKIREVREQ
IDHLRHELEE AENNYDLNKA AELRHGRIPA VEKELLELEA ENREKTAQED RILQEEVTEN
EIAEIVGRWT GIPVTKLVEG EREKLLKLAD VLHQKVIGQD DAVQLVSDAV LRARAGIKDP
KRPIGSFIFL GPTGVGKTEL AKALAFNMFD SEDHMIRIDM SEYMEKHSVS RLVGAPPGYI
GYEEGGQLTE AVRRNPYSIV LLDEIEKAHP DVFNILLQVL DDGRITDSQG RLIDFKNTVI
IMTSNIGSNL LLERTEEGEI SPELESDVMQ ILQSEFKPEF LNRVDDIILF KPLTLADIKG
IVEKLVEELQ IRLADQEITI TISDDAKAFI AEEAYDPVYG ARPLKRYIVR HVETPLAREI
VSGKIMPHSS VEIDLADKEF TFKVTE
