ID   RECA_STRMU              Reviewed;         383 AA.
AC   P27624; Q54467;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2002, sequence version 3.
DT   03-AUG-2022, entry version 143.
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=SMU_2085;
OS   Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=210007;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700610 / UA159;
RX   PubMed=12397186; DOI=10.1073/pnas.172501299;
RA   Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA   Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA   Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT   "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT   pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 79-308.
RX   PubMed=1628842; DOI=10.1016/0378-1119(92)90626-z;
RA   Quivey R.G. Jr., Faustoferri R.C.;
RT   "In vivo inactivation of the Streptococcus mutans recA gene mediated by PCR
RT   amplification and cloning of a recA DNA fragment.";
RL   Gene 116:35-42(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 105-206.
RX   PubMed=1556091; DOI=10.1128/jb.174.8.2729-2732.1992;
RA   Dybvig K., Hollingshead S.K., Heath D.G., Clewell D.B., Sun F., Woodard A.;
RT   "Degenerate oligonucleotide primers for enzymatic amplification of recA
RT   sequences from Gram-positive bacteria and mycoplasmas.";
RL   J. Bacteriol. 174:2729-2732(1992).
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}.
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DR   EMBL; AE014133; AAN59680.1; -; Genomic_DNA.
DR   EMBL; M61897; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; M81468; AAA26929.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; NP_722374.1; NC_004350.2.
DR   RefSeq; WP_002262392.1; NC_004350.2.
DR   AlphaFoldDB; P27624; -.
DR   SMR; P27624; -.
DR   STRING; 210007.SMU_2085; -.
DR   PRIDE; P27624; -.
DR   EnsemblBacteria; AAN59680; AAN59680; SMU_2085.
DR   GeneID; 66818568; -.
DR   KEGG; smu:SMU_2085; -.
DR   PATRIC; fig|210007.7.peg.1855; -.
DR   eggNOG; COG0468; Bacteria.
DR   HOGENOM; CLU_040469_3_2_9; -.
DR   OMA; DYGEQAL; -.
DR   PhylomeDB; P27624; -.
DR   Proteomes; UP000002512; 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; Reference proteome; SOS response.
FT   CHAIN           1..383
FT                   /note="Protein RecA"
FT                   /id="PRO_0000122857"
FT   REGION          347..369
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         79..86
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00268"
FT   CONFLICT        93
FT                   /note="V -> A (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        174
FT                   /note="D -> N (in Ref. 2)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   383 AA;  41420 MW;  34863AEE6AEA58B6 CRC64;
     MAKRIKKTEE ITKKFGDERK KALDDALKNI EKDFGKGAVM RLGERAEQKV QVMSSGSLAL
     DIALGAGGYP KGRIVEIYGP ESSGKTTVAL HAVAQAQKDG GIAAFIDAEH ALDPAYAAAL
     GVNIDELLLS QPDSGEQGLE IAGKLIDSGA VDLVVVDSVA ALVPRAEIDG DIGDSHVGLQ
     ARMMSQAMRK LSASINKTKT IAIFINQLRE KVGIMFGNPE TTPGGRALKF YSSVRLDVRG
     NTQIKGTGEQ KDSNIGKETK IKVVKNKVAP PFKEAFVEII YGEGISRTGE LVKIASDLGI
     IQKAGAWYSY NGEKIGQGSE NAKKFLADNP EIFDDIDHKV RVQYGLIEED NTEEKQSSKE
     KETDEKADKN LVLELDDTIE LED