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Database: UniProt
Entry: A3CKB2_STRSV
LinkDB: A3CKB2_STRSV
Original site: A3CKB2_STRSV 
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
//
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