ID A3CKB2_STRSV Unreviewed; 638 AA.
AC A3CKB2;
DT 20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 20-MAR-2007, sequence version 1.
DT 24-JAN-2024, entry version 92.
DE SubName: Full=ATPase with chaperone activity, ATP-binding subunit, putative {ECO:0000313|EMBL:ABN43617.1};
GN OrderedLocusNames=SSA_0156 {ECO:0000313|EMBL:ABN43617.1};
OS Streptococcus sanguinis (strain SK36).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=388919 {ECO:0000313|EMBL:ABN43617.1, ECO:0000313|Proteomes:UP000002148};
RN [1] {ECO:0000313|EMBL:ABN43617.1, ECO:0000313|Proteomes:UP000002148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK36 {ECO:0000313|EMBL:ABN43617.1,
RC ECO:0000313|Proteomes:UP000002148};
RX PubMed=17277061; DOI=10.1128/JB.01808-06;
RA Xu P., Alves J.M., Kitten T., Brown A., Chen Z., Ozaki L.S., Manque P.,
RA Ge X., Serrano M.G., Puiu D., Hendricks S., Wang Y., Chaplin M.D., Akan D.,
RA Paik S., Peterson D.L., Macrina F.L., Buck G.A.;
RT "Genome of the opportunistic pathogen Streptococcus sanguinis.";
RL J. Bacteriol. 189:3166-3175(2007).
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}.
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DR EMBL; CP000387; ABN43617.1; -; Genomic_DNA.
DR RefSeq; WP_002896821.1; NC_009009.1.
DR RefSeq; YP_001034167.1; NC_009009.1.
DR AlphaFoldDB; A3CKB2; -.
DR STRING; 388919.SSA_0156; -.
DR KEGG; ssa:SSA_0156; -.
DR PATRIC; fig|388919.9.peg.151; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_3_9; -.
DR OMA; MKQIDNT; -.
DR OrthoDB; 2144783at2; -.
DR Proteomes; UP000002148; 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; 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; IPR001270; ClpA/B.
DR InterPro; IPR018368; ClpA/B_CS1.
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; PF10431; ClpB_D2-small; 1.
DR PRINTS; PR00300; CLPPROTEASEA.
DR SMART; SM00382; AAA; 2.
DR SMART; SM01086; ClpB_D2-small; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00870; CLPAB_1; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000313|EMBL:ABN43617.1};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000002148};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 78..218
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 354..509
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 528..622
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
SQ SEQUENCE 638 AA; 72227 MW; 3C6FE18C715F9939 CRC64;
MLQTEKLQQK EEYQEEIMPD TLKFQDPVSI EEEESLTPYL DKYTENVTEK IRKKIDNFTV
FGRDKEVEQV IVSLLRQTKN SPILVGEAGT GKTAIVDGLV VEILKGNVPD EFKHVTVRSL
ELSNISSKSD GEDMVSRLKR IIEELKVTKG ENILFIDEVH TIVGAGGDGS MLDAGNVIKP
PLARGEIQMI SATTYEEYQS SIETDKALER RVQMVPVEEP TEDQAIFILG NIRRRFEKER
NITITDDAVE QAVRLAVRYI PERFLPDKAI DLLDDATAQA YFEKRKVVDI EDIARVIQKM
KKIPVTTILK DDSERLMNFT DELKKYVKGQ DFAVSQVANT IYISKEGFQR PNKPLGSFLF
LGTTGVGKTE LAKALAKILF DNVDAMIRID CSEYSSKGDK DKLIGKNIVG SKGLLTEPVK
NNPYSVVLLD ELEKAHPDIY DILLQVLDEG HLTTGTGRKI NFKNTIVIAT TNSGADEIKK
TYANEGNFGE MTDLAYEGFM NRIVEELSLT FRPEFINRFG NKVVFNMLTA DIIEAIVDLA
WKKEEKRLAE QKVYLQYEDK AEFYDFLRSK GTSVENGARP LERLIQDRVT GPIAEKLFLL
QRRGAKYNVL IKVIGEAPDG IFHHIDKRTL DFEATKVE
//