CLPB_YEREN
ID CLPB_YEREN Reviewed; 890 AA.
AC Q9F746;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Chaperone protein ClpB;
GN Name=clpB;
OS Yersinia enterocolitica.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=630;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10986262; DOI=10.1128/jb.182.19.5563-5571.2000;
RA Badger J.L., Young B.M., Darwin A.J., Miller V.L.;
RT "Yersinia enterocolitica ClpB affects levels of invasin and motility.";
RL J. Bacteriol. 182:5563-5571(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 Affects level of invasin and motility in Y.enterocolitica.
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; AF285784; AAG00524.1; -; Genomic_DNA.
DR RefSeq; WP_005168523.1; NZ_NWMR01000015.1.
DR AlphaFoldDB; Q9F746; -.
DR SMR; Q9F746; -.
DR OrthoDB; 44062at2; -.
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 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; IPR017729; ATPase_T6SS_ClpV1.
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; 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; TIGR03345; VI_ClpV1; 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..890
FT /note="Chaperone protein ClpB"
FT /id="PRO_0000191210"
FT DOMAIN 9..150
FT /note="Clp R"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 12..77
FT /note="Repeat 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 87..150
FT /note="Repeat 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 171..369
FT /note="NBD1"
FT /evidence="ECO:0000250"
FT REGION 370..566
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 567..789
FT /note="NBD2"
FT /evidence="ECO:0000250"
FT REGION 790..890
FT /note="C-terminal"
FT /evidence="ECO:0000250"
FT COILED 420..544
FT /evidence="ECO:0000250"
FT BINDING 235..242
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 626..633
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 890 AA; 97918 MW; D78CFFC36434D64F CRC64;
MAITRKNLFG KLDATLFKGI ESATTICKLR GNPYVELIHW LNQLWHQEDN DLKHIVRYFA
VDVDAFERGL AQALARLPVG ATSISDFSYH IELAIERAWV YASLECLDTR IRSGHLLLAM
LTNMELRRAL LAIAPEMEKI PLEHLSSDFN FITQASPETN EAATDGSPMY DGTLPGEASN
AINGKSTATL AQYTTDLTAL AREGKIDPVL GRNHEISTMV DILLRRRQNN PLLTGEAGVG
KTAVVEGLAL AIVAGEMPPA LSQVSLLTLD VVALSAGASM KGEFEARLKN VLDEAMASPT
PVILFIDEVH TLVGAGGNAG TGDAANLLKP ALARGQLRTI GATTWSEFKR HIEKDPALTR
RFQVLQVDEP DEDTAISMLR GLTPALEKHH GVWIMDEALQ AAVRLSHRYI PARQLPDKAI
SLLDTACARV AVAQFSQPAE LQQLTFQSET AQTELSSLEK AQHFGKGQDE RTALLEATIA
QHSAAANKLE QRWQAERELV TAITATRTVL YELVSQPTPD EEKRQQYQQQ LAQLEEQLLL
IRSAQPLVQA EVNATVIANI VADWTGIQVG QMLKDDIRAV MELPQRLEER VIGQPHALVQ
LSENIMTARA GMADPRKPLG VFMLVGPSGV GKTETALAIA ESMYGGEQNL ITINMSEYQE
SHTVSSLKGS PPGYVGYGEG GVLTEAVRRK PYSVVLLDEI EKAHSDVHEL FFQVFDKGQM
EDGEGRFIDF KNTILLLTSN VGSELLSNLF ADPDTAPDQD GILSALQPEL LKVFPAAFLG
RVTVIPYLPL QQSALQHIVR LHLDRIGQRL QSQHQLTLQY SDVVVDDVVS RCSVAETGAR
MLIRYIEQNI TPEIGKFILR DHDAIPNQIV FVDKVENKFT VSVLNEKINN
