ID   RECA_LACLL              Reviewed;         341 AA.
AC   Q59486;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Protein RecA, plasmid {ECO:0000255|HAMAP-Rule:MF_00268};
DE   AltName: Full=Recombinase A {ECO:0000255|HAMAP-Rule:MF_00268};
DE   AltName: Full=recaLP;
GN   Name=recAL {ECO:0000255|HAMAP-Rule:MF_00268};
OS   Lactococcus lactis subsp. lactis (Streptococcus lactis).
OG   Plasmid pNP40.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=1360;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DRC3;
RX   PubMed=9097419; DOI=10.1128/aem.63.4.1244-1251.1997;
RA   Garvey P., Rince A., Hill C., Fitzgerald G.F.;
RT   "Identification of a recA homolog (recALP) on the conjugative lactococcal
RT   phage resistance plasmid pNP40: evidence of a role for chromosomally
RT   encoded recAL in abortive infection.";
RL   Appl. Environ. Microbiol. 63:1244-1251(1997).
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; U36837; AAB52384.1; -; Genomic_DNA.
DR   RefSeq; WP_012477747.1; NZ_CP064837.1.
DR   RefSeq; YP_001966451.1; NC_010901.1.
DR   AlphaFoldDB; Q59486; -.
DR   SMR; Q59486; -.
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; Plasmid; SOS response.
FT   CHAIN           1..341
FT                   /note="Protein RecA, plasmid"
FT                   /id="PRO_0000122734"
FT   BINDING         80..87
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00268"
SQ   SEQUENCE   341 AA;  37177 MW;  F9D4BCCCEA69EAB5 CRC64;
     MEQPQYNSYK VRKLDDPEEK KLAILKATQS IEKKFGSNTI LNEEGKASQH VQALPSGILS
     LDCAIGIGGY PKGRLIELFG AESSGKTTVA LQAVAETQKN GGYVAYIDAE NSLDIEYAEN
     LGVKSDSLIF AQPDTGEEAF YMINEFVRTG AFDLIVVDSV AALTPASEID GVKMPGQQAK
     MMSEQLSQLV GKVNQTKTVI IFINQIRSTM SGLFLNKETT PGGSALKFYS SVRIEVKSGE
     KIKDGIDTIG KKTTLHTVKN KVSSPYKKPT VINIFGDGFS QEIDVVTTAL QLGVVKKLGE
     WYSFNGQKLG RGIFGVKEYL SHHPSVFNAL DNLTREALQF S