RECA_STRA3
ID RECA_STRA3 Reviewed; 379 AA.
AC P65979; Q8DWW8; Q8E2S0;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=gbs2047;
OS Streptococcus agalactiae serotype III (strain NEM316).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=211110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEM316;
RX PubMed=12354221; DOI=10.1046/j.1365-2958.2002.03126.x;
RA Glaser P., Rusniok C., Buchrieser C., Chevalier F., Frangeul L., Msadek T.,
RA Zouine M., Couve E., Lalioui L., Poyart C., Trieu-Cuot P., Kunst F.;
RT "Genome sequence of Streptococcus agalactiae, a pathogen causing invasive
RT neonatal disease.";
RL Mol. Microbiol. 45:1499-1513(2002).
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. {ECO:0000255|HAMAP-Rule:MF_00268}.
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; AL766856; CAD47706.1; -; Genomic_DNA.
DR RefSeq; WP_001085741.1; NC_004368.1.
DR AlphaFoldDB; P65979; -.
DR SMR; P65979; -.
DR STRING; 211110.gbs2047; -.
DR EnsemblBacteria; CAD47706; CAD47706; CAD47706.
DR GeneID; 66886829; -.
DR KEGG; san:recA; -.
DR eggNOG; COG0468; Bacteria.
DR HOGENOM; CLU_040469_3_2_9; -.
DR OMA; DYGEQAL; -.
DR Proteomes; UP000000823; 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..379
FT /note="Protein RecA"
FT /id="PRO_0000122848"
FT BINDING 79..86
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00268"
SQ SEQUENCE 379 AA; 40917 MW; A71E4366C63842B9 CRC64;
MAKKTKKAEE ITKKFGDERR KALDDALKNI EKDFGKGAVM RLGERAEQKV QVMSSGSLAL
DIALGAGGYP KGRIVEIYGP ESSGKTTVAL HAVAQAQKEG GIAAFIDAEH ALDPAYAAAL
GVNIDELLLS QPDSGEQGLE IAGKLIDSGA VDLVVVDSVA ALVPRAEIDG DIGDSHVGLQ
ARMMSQAMRK LSASINKTKT IAIFINQLRE KVGVMFGNPE TTPGGRALKF YSSVRLDVRG
NTQIKGTGEH KDHNVGKETK IKVVKNKVAP PFREAFVEIM YGEGISRTGE LIKIASDLDI
IQKAGAWYSY NGEKIGQGSE NAKKYLADNP AIFDEIDHKV RVHFGMTEDD SPVQSELVEE
KNEADDLVLD LDNAIEIEE