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RECA_STRPZ
ID   RECA_STRPZ              Reviewed;         378 AA.
AC   P0C096; B5XJ04; Q59942;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   14-APR-2009, sequence version 2.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Protein RecA {ECO:0000255|HAMAP-Rule:MF_00268};
DE   AltName: Full=Recombinase A {ECO:0000255|HAMAP-Rule:MF_00268};
GN   Name=recA {ECO:0000255|HAMAP-Rule:MF_00268}; OrderedLocusNames=Spy49_1753c;
OS   Streptococcus pyogenes serotype M49 (strain NZ131).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=471876;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7557418; DOI=10.1016/0378-1119(95)00273-9;
RA   Tao L., Hollingshead S.K., Suvorov A.N., Ferretti J.J., McShan W.M.;
RT   "Construction of a Streptococcus pyogenes recA mutant via insertional
RT   inactivation, and cloning and sequencing of the complete recA gene.";
RL   Gene 162:59-62(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NZ131;
RX   PubMed=18820018; DOI=10.1128/jb.00672-08;
RA   McShan W.M., Ferretti J.J., Karasawa T., Suvorov A.N., Lin S., Qin B.,
RA   Jia H., Kenton S., Najar F., Wu H., Scott J., Roe B.A., Savic D.J.;
RT   "Genome sequence of a nephritogenic and highly transformable M49 strain of
RT   Streptococcus pyogenes.";
RL   J. Bacteriol. 190:7773-7785(2008).
CC   -!- FUNCTION: Can catalyze the hydrolysis of ATP in the presence of single-
CC       stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex
CC       DNA, and the ATP-dependent hybridization of homologous single-stranded
CC       DNAs. It interacts with LexA causing its activation and leading to its
CC       autocatalytic cleavage.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00268}.
CC   -!- SIMILARITY: Belongs to the RecA family. {ECO:0000255|HAMAP-
CC       Rule:MF_00268}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA85501.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; U21934; AAA85501.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; CP000829; ACI62003.1; -; Genomic_DNA.
DR   RefSeq; WP_012561071.1; NC_011375.1.
DR   AlphaFoldDB; P0C096; -.
DR   SMR; P0C096; -.
DR   EnsemblBacteria; ACI62003; ACI62003; Spy49_1753c.
DR   KEGG; soz:Spy49_1753c; -.
DR   HOGENOM; CLU_040469_3_2_9; -.
DR   OMA; DYGEQAL; -.
DR   Proteomes; UP000001039; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR   GO; GO:0003684; F:damaged DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003697; F:single-stranded DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR   GO; GO:0009432; P:SOS response; IEA:UniProtKB-UniRule.
DR   CDD; cd00983; recA; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00268; RecA; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR013765; DNA_recomb/repair_RecA.
DR   InterPro; IPR020584; DNA_recomb/repair_RecA_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR020588; RecA_ATP-bd.
DR   InterPro; IPR023400; RecA_C.
DR   InterPro; IPR020587; RecA_monomer-monomer_interface.
DR   PANTHER; PTHR45900; PTHR45900; 1.
DR   Pfam; PF00154; RecA; 1.
DR   PRINTS; PR00142; RECA.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF54752; SSF54752; 1.
DR   TIGRFAMs; TIGR02012; tigrfam_recA; 1.
DR   PROSITE; PS00321; RECA_1; 1.
DR   PROSITE; PS50162; RECA_2; 1.
DR   PROSITE; PS50163; RECA_3; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; DNA damage; DNA recombination; DNA repair;
KW   DNA-binding; Nucleotide-binding; SOS response.
FT   CHAIN           1..378
FT                   /note="Protein RecA"
FT                   /id="PRO_0000122865"
FT   BINDING         79..86
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00268"
FT   CONFLICT        47..48
FT                   /note="EQ -> DE (in Ref. 1; AAA85501)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        54
FT                   /note="S -> R (in Ref. 1; AAA85501)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        64..65
FT                   /note="LG -> WI (in Ref. 1; AAA85501)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        130
FT                   /note="A -> S (in Ref. 1; AAA85501)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        241..242
FT                   /note="TT -> NN (in Ref. 1; AAA85501)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        252..253
FT                   /note="DS -> IA (in Ref. 1; AAA85501)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   378 AA;  40615 MW;  8B9C0B29250538AB CRC64;
     MAKKLKKNEE ITKKFGDERR KALDDALKNI EKDFGKGAVM RLGERAEQKV QVMSSGSLAL
     DIALGAGGYP KGRIIEIYGP ESSGKTTVAL HAVAQAQKEG GIAAFIDAEH ALDPAYAAAL
     GVNIDELLLA QPDSGEQGLE IAGKLIDSGA VDLVVVDSVA ALVPRAEIDG DIGDSHVGLQ
     ARMMSQAMRK LSASINKTKT IAIFINQLRE KVGVMFGNPE TTPGGRALKF YASVRLDVRG
     TTQIKGTGDQ KDSSIGKETK IKVVKNKVAP PFKVAEVEIM YGEGISRTGE LVKIASDLDI
     IQKAGAWFSY NGEKIGQGSE NAKRYLADHP QLFDEIDRKV RVKFGLLEES EEESAMAVAS
     EETDDLALDL DNGIEIED
 
 
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