RECA_STRS7
ID RECA_STRS7 Reviewed; 378 AA.
AC C0MGB6;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 73.
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=SZO_18640;
OS Streptococcus equi subsp. zooepidemicus (strain H70).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=553483;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H70;
RX PubMed=19325880; DOI=10.1371/journal.ppat.1000346;
RA Holden M.T.G., Heather Z., Paillot R., Steward K.F., Webb K., Ainslie F.,
RA Jourdan T., Bason N.C., Holroyd N.E., Mungall K., Quail M.A., Sanders M.,
RA Simmonds M., Willey D., Brooks K., Aanensen D.M., Spratt B.G., Jolley K.A.,
RA Maiden M.C.J., Kehoe M., Chanter N., Bentley S.D., Robinson C.,
RA Maskell D.J., Parkhill J., Waller A.S.;
RT "Genomic evidence for the evolution of Streptococcus equi: host
RT restriction, increased virulence, and genetic exchange with human
RT pathogens.";
RL PLoS Pathog. 5:E1000346-E1000346(2009).
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; FM204884; CAX00795.1; -; Genomic_DNA.
DR AlphaFoldDB; C0MGB6; -.
DR SMR; C0MGB6; -.
DR EnsemblBacteria; CAX00795; CAX00795; SZO_18640.
DR KEGG; seq:SZO_18640; -.
DR eggNOG; COG0468; Bacteria.
DR HOGENOM; CLU_040469_3_2_9; -.
DR OMA; DYGEQAL; -.
DR Proteomes; UP000001368; 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_1000204716"
FT BINDING 79..86
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00268"
SQ SEQUENCE 378 AA; 40562 MW; 3DF17344D3E4CED4 CRC64;
MAKKVKKNEE ITKKFGDERR KALDDALKNI EKDFGKGAVM RLGERAEQKV QVMSSGSLAL
DIALGAGGYP KGRIIEIYGP ESSGKTTVAL HAVAQAQKEG GIAAFIDAEH ALDPAYAAAL
GVNIDELLLS QPDSGEQGLE IAGKLIDSGA VDLVVVDSVA ALVPRAEIDG DIGDNHVGLQ
ARMMSQAMRK LSASINKTKT IAIFINQLRE KVGVMFGNPE TTPGGRALKF YASVRLDVRG
TTQIKGTGDQ KDSSIGKETK IKVVKNKVAP PFKVAEVEIM YGEGISRTGE LIKIASDLDI
IQKAGAWFSY NGEKIGQGSE NAKRYLADHP ELFDEIDHKV RVKFGLLEDT EESAAADTVA
AKADELVLEL DDAIEIED