ID   RECA_STRAG              Reviewed;         379 AA.
AC   Q9AGW0;
DT   05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 2.
DT   03-AUG-2022, entry version 84.
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};
OS   Streptococcus agalactiae.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1311;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 13813 / CIP 103227 / DSM 2134 / JCM 5671 / NCTC 8181;
RA   Chiou J.-F.;
RT   "Cloning, sequencing and characterization of the RecA gene from
RT   Streptococcus agalactiae.";
RL   Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK16709.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF326345; AAK16709.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q9AGW0; -.
DR   SMR; Q9AGW0; -.
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_0000122850"
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;  41015 MW;  2719C98389B93833 CRC64;
     MAKKTKKAEE ITKKFGDERR KALDDALKNI EKDFGKGAVM RLGERAEQKV QVMSSGSLAL
     DIALGAGGYP KGRIVEIYGP ESSGKTTVAL HAVAQAQKEG GIAAFIDAEH ALDPAYAAAL
     GVNIDELLLS QPDSGEQDLE IAGKLIDSGA VDLVVVDSVA ALVPRAEIDG DIGDSHVGLQ
     ARMMMQAMHK LTASINKTKT IAIFINQLRE KVGVMFGNPE TTPGGRALKF YSSVRLDVRG
     NTQIKGTGEH KDHNVGKETK IKVVKNKVAP PFREAFVEIM YGEGISRTGE LIKIASDLDI
     IQKAGAWYSY NGEKIGQGSE NAKKYLADNP AIFDEIDHKV RVHFGMTEDD SPVQSELVEE
     KNEADDLVLD LDNAIEIEE