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Database: UniProt
Entry: B9DW30_STRU0
LinkDB: B9DW30_STRU0
Original site: B9DW30_STRU0 
ID   B9DW30_STRU0            Unreviewed;       813 AA.
AC   B9DW30;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 79.
DE   SubName: Full=Stress response-related Clp ATPase {ECO:0000313|EMBL:CAR43700.1};
GN   Name=clpC {ECO:0000313|EMBL:CAR43700.1};
GN   OrderedLocusNames=SUB1743 {ECO:0000313|EMBL:CAR43700.1};
OS   Streptococcus uberis (strain ATCC BAA-854 / 0140J).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=218495 {ECO:0000313|EMBL:CAR43700.1, ECO:0000313|Proteomes:UP000000449};
RN   [1] {ECO:0000313|Proteomes:UP000000449}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-854 / 0140J {ECO:0000313|Proteomes:UP000000449};
RX   PubMed=19175920; DOI=10.1186/1471-2164-10-54;
RA   Ward P.N., Holden M.T.G., Leigh J.A., Lennard N., Bignell A., Barron A.,
RA   Clark L., Quail M.A., Woodward J., Barrell B.G., Egan S.A., Field T.R.,
RA   Maskell D., Kehoe M., Dowson C.G., Chanter N., Whatmore A.M., Bentley S.D.,
RA   Parkhill J.;
RT   "Evidence for niche adaptation in the genome of the bovine pathogen
RT   Streptococcus uberis.";
RL   BMC Genomics 10:54-54(2009).
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.
CC       {ECO:0000256|ARBA:ARBA00025613}.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|RuleBase:RU004432}.
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DR   EMBL; AM946015; CAR43700.1; -; Genomic_DNA.
DR   RefSeq; WP_015912034.1; NC_012004.1.
DR   AlphaFoldDB; B9DW30; -.
DR   STRING; 218495.SUB1743; -.
DR   KEGG; sub:SUB1743; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_1_9; -.
DR   OMA; SKMMQGE; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000000449; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   CDD; cd00009; AAA; 1.
DR   CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR   Gene3D; 1.10.8.60; -; 2.
DR   Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
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   PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR   PANTHER; PTHR11638:SF18; HEAT SHOCK PROTEIN 104; 1.
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; SSF81923; Double Clp-N motif; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS00870; CLPAB_1; 1.
DR   PROSITE; PS00871; CLPAB_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004432};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU004432};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000449};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          231..377
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          544..684
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          721..810
FT                   /note="Clp ATPase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01086"
SQ   SEQUENCE   813 AA;  90409 MW;  5D2302D78D112317 CRC64;
     MTDYSLKMQA IFKQAQYQAA RFDSPYLETW HLLLAMVVVN NSLAGLVFNE FENKVALEEY
     EAAAILAIGK APNDDIKEFE YKGQSKTLSH ILSFADAIRN VTHANEVGSE HVLFAILLNP
     DIMATRLLEL AGFKIKDDGK GDLKLADLRK AIEIQAAYSK ETIKAIYELR KPKKAKTGGT
     FSDMMKPAGT AGELSDYTRD LTEMASQGLL EPVIGREKEI TRMVQVLSRK TKNNPVLVGE
     AGVGKTALAY GLAQRIVTGE IPYELRDMRV LELDMMSVVA GTRFRGDFEE RMNQIIDDIE
     SDGHIILFVD ELHTIMGSGS GIDSTLDAAN ILKPALSRGT LHMVGATTQE EYQKHIEKDA
     ALSRRFSKVL IEEPSIEDAY KILSGLKKSY ESYHNVTISD QAIKTAVKVA HRYLTSKHLP
     DSAIDLLDEA SATVQSFVKK EAPAFITPID QAIIKGDFKT VSQLLKASKA KPQKPTPVTE
     EDIMSTLSKL SGIPLEKISK ADSQKYLNLE KELHKRVIGQ EDAVSAISRA IRRNQSGIRT
     GKRPIGSFMF LGPTGVGKTE LAKALAELLF DDESALIRFD MSEYMEKFAA SRLNGAPPGY
     VGYDEGGELT EKVRNKPYSV LLFDEVEKAH PDIFNVLLQV LDDGQLTDSR GRKVDFSNTI
     IIMTSNLGAT ALRDDKTVGF GAKDINHDHS AMEKRILEEL KKTYRPEFIN RIDEKVVFHS
     LSQEDMRQVV AIMVQPLIKN LEEKGITLKI QPSALKYLSE VGYDVEMGAR PLRRTIQTEI
     EDKLSEFILS GQLKTGKTLK IGMSQGKLKF DMV
//
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