CLPB_PORGI
ID CLPB_PORGI Reviewed; 863 AA.
AC Q7MVE7;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Chaperone protein ClpB;
GN Name=clpB; OrderedLocusNames=PG_1118;
OS Porphyromonas gingivalis (strain ATCC BAA-308 / W83).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=242619;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-308 / W83;
RX PubMed=12949112; DOI=10.1128/jb.185.18.5591-5601.2003;
RA Nelson K.E., Fleischmann R.D., DeBoy R.T., Paulsen I.T., Fouts D.E.,
RA Eisen J.A., Daugherty S.C., Dodson R.J., Durkin A.S., Gwinn M.L.,
RA Haft D.H., Kolonay J.F., Nelson W.C., Mason T.M., Tallon L., Gray J.,
RA Granger D., Tettelin H., Dong H., Galvin J.L., Duncan M.J., Dewhirst F.E.,
RA Fraser C.M.;
RT "Complete genome sequence of the oral pathogenic bacterium Porphyromonas
RT gingivalis strain W83.";
RL J. Bacteriol. 185:5591-5601(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; AE015924; AAQ66228.1; -; Genomic_DNA.
DR RefSeq; WP_004584414.1; NC_002950.2.
DR AlphaFoldDB; Q7MVE7; -.
DR SMR; Q7MVE7; -.
DR STRING; 242619.PG_1118; -.
DR PRIDE; Q7MVE7; -.
DR EnsemblBacteria; AAQ66228; AAQ66228; PG_1118.
DR KEGG; pgi:PG_1118; -.
DR PATRIC; fig|242619.8.peg.1037; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_0_10; -.
DR OMA; SKMMQGE; -.
DR OrthoDB; 44062at2; -.
DR BioCyc; PGIN242619:G1G02-1047-MON; -.
DR Proteomes; UP000000588; 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 ATP-binding; Chaperone; Coiled coil; Cytoplasm; Nucleotide-binding;
KW Reference proteome; Repeat; Stress response.
FT CHAIN 1..863
FT /note="Chaperone protein ClpB"
FT /id="PRO_0000191156"
FT DOMAIN 3..144
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 81..144
FT /note="Repeat 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 157..338
FT /note="NBD1"
FT /evidence="ECO:0000250"
FT REGION 339..543
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 553..770
FT /note="NBD2"
FT /evidence="ECO:0000250"
FT REGION 771..863
FT /note="C-terminal"
FT /evidence="ECO:0000250"
FT COILED 389..520
FT /evidence="ECO:0000250"
FT BINDING 204..211
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 603..610
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 863 AA; 97766 MW; 63D795897C473889 CRC64;
MNINNYTIKS QEALQQAVEL TRRHGQQAIE PQHLLKAVMD QGESLTDFLF AKMGLNKGSI
ATAVDKLIEK LPHVSGGEPY LSHETNQVLQ AAEDAAHRMK DKYVSLEHIV LAILTTRCEA
STLLKDAGAT EQLLQSAIEE LRKGRNVTSQ SAEEQYNALE KYAVNLCQRA RDGKLDPVIG
RDDEIRRVLQ ILSRRTKNNP ILIGEPGVGK TAIAEGLAYR IVRGDVPENL RNKQIFSLDM
GALIAGAKYK GEFEERLKAV VNEVTGAEGE IILFIDEIHT LVGAGKSEGA MDAANILKPA
LARGELRAIG ATTLDEYRKY FEKDKALERR FQMVMVDEPD ELSSISILRG LKEKYENHHK
VRIKDDAIIA AVKLSHRYIT ERFLPDKAID LMDEAAARLR MEVDSLPEEL DEISRRIKQL
EIEREAIKRE NDEEKVQFLD REIAELKEKE ASEKAQWQNE KDRINQIQQL KIDIEELKFQ
ADRAEREGDY GRVAEIRYGL IKQKETEIDT IQQQLHELQR GGSMIKEEVE ADDIADIVSR
WTGIPVSRML QSERDKLLHL EDELHKRVIG QDEAIRAVAD AVRRSRAGLQ DPKRPIGSFI
FLGTTGVGKT ELARALAELL FDDESMLTRI DMSEYQEKFS ATRLIGAPPG YVGYDEGGQL
TEAIRRKPYS VVLFDEIEKA HPDVFNVLLQ VLDDGRLTDN KGHVVNFKNT LIIMTSNLGS
DIIRERMQNL TAENRRSLTA RTADEVMQLL KHTIRPEFLN RIDETIVFTP LTEKEIYEIV
RLQLDGIVRQ LADNDVVLHY TEAVVTFAAR EGYDPQFGAR PVKRVLQRFV LNELSKALLA
DTVDSTRPVL IDCIDGSIVF RNE
