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
//