ID   RECA_PSEFL              Reviewed;         352 AA.
AC   Q01953;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, 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};
OS   Pseudomonas fluorescens.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=294;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=OE 28.3;
RX   PubMed=8450308; DOI=10.1099/00221287-139-1-49;
RA   de Mot R., Laeremans T., Schoofs G., Vanderleyden J.;
RT   "Characterization of the recA gene from Pseudomonas fluorescens OE 28.3 and
RT   construction of a recA mutant.";
RL   J. Gen. Microbiol. 139:49-57(1993).
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; M96558; AAA25980.1; -; Genomic_DNA.
DR   PIR; A47709; A47709.
DR   AlphaFoldDB; Q01953; -.
DR   SMR; Q01953; -.
DR   STRING; 690597.JH730961_gene4441; -.
DR   eggNOG; COG0468; Bacteria.
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..352
FT                   /note="Protein RecA"
FT                   /id="PRO_0000122802"
FT   REGION          333..352
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         65..72
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00268"
SQ   SEQUENCE   352 AA;  37634 MW;  F579A9D2415D59F0 CRC64;
     MDDNKKKALA AALGQIERQF GKGAVMRMGD HDRQAIPAIS TGSLGLDIAL GIGGLPKGRI
     VEIYGPESSG KTTLTLSVIA QAQKMGATCA FVDAEHALDP EYAGKLGVNV DDLLVSQPDT
     GEQALEITDM LVRSNAIDVI VVDSVAALVP KAEIEGEMGD MHVGLQARLM SQALRKITGN
     IKNANCLVIF INQIRMKIGV MFGSPETTTG GNALKFYASV RLDIRRTGAV KEGDEVVGSE
     TRVKVVKNKV APPFRQAEFQ ILYGKGIYLN GEMIDLGVLH GFVEKSGAWY AYNGSKIGQG
     KANSAKFLAD NPDIVATLEK QIRDKLLTPA PDVKAAANRE PVEEVEEADT DI