ID   RECA_BIFLO              Reviewed;         397 AA.
AC   Q8G4G9;
DT   30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 103.
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=BL1415;
OS   Bifidobacterium longum (strain NCC 2705).
OC   Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC   Bifidobacterium.
OX   NCBI_TaxID=206672;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCC 2705;
RX   PubMed=12381787; DOI=10.1073/pnas.212527599;
RA   Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G.,
RA   Zwahlen M.-C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F.;
RT   "The genome sequence of Bifidobacterium longum reflects its adaptation to
RT   the human gastrointestinal tract.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(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; AE014295; AAN25214.1; -; Genomic_DNA.
DR   RefSeq; NP_696578.1; NC_004307.2.
DR   RefSeq; WP_007052644.1; NC_004307.2.
DR   AlphaFoldDB; Q8G4G9; -.
DR   SMR; Q8G4G9; -.
DR   STRING; 206672.BL1415; -.
DR   EnsemblBacteria; AAN25214; AAN25214; BL1415.
DR   GeneID; 66505424; -.
DR   KEGG; blo:BL1415; -.
DR   PATRIC; fig|206672.9.peg.274; -.
DR   HOGENOM; CLU_040469_3_2_11; -.
DR   OMA; DYGEQAL; -.
DR   PhylomeDB; Q8G4G9; -.
DR   Proteomes; UP000000439; 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..397
FT                   /note="Protein RecA"
FT                   /id="PRO_0000122662"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..23
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         83..90
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00268"
SQ   SEQUENCE   397 AA;  41801 MW;  AB46F76E024C7223 CRC64;
     MALETKPAKD PAAEDKHELD PKRKAALDTA LAQVEKSFGK GSAMRLGDQP EQNVEVIPTG
     SLALDMALGI GGLPKGRIVE IYGPESSGKT TLALHVVANA QKKGGVAAYI DAEHALDPAY
     ARKLGVDTDS LIVSQPDNGE QALEIADMLI RSGALDVIVI DSVAALVPKA EIEGEMGDSH
     VGLQARLMSQ ALRKMTGALA QAGTTAIFIN QLREKIGVFF GNPETTTGGK ALKFYASVRL
     DIRRIQTLKN GDEAVGNRTR VKVVKNKMAP PFKSAEFDML YGEGISREGS VIDMAQQVGV
     VKKSGSWFTY EGDQLGQGRE KVRQFLKDNP AITEEIENKV KAEFGLIGSA DQFAEDGEAA
     AAAAVSEAAA ADVAKDSKAA AAPAAKTTRA KAGTAKA