ID   RECA_PSEPU              Reviewed;         355 AA.
AC   Q07447;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 107.
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 putida (Arthrobacter siderocapsulatus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=303;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=G2;
RX   PubMed=8294013; DOI=10.1016/0378-1119(93)90476-j;
RA   Luo J., Burns G., Sokatch J.R.;
RT   "Construction of chromosomal recA mutants of Pseudomonas putida PpG2.";
RL   Gene 136:263-266(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=PPS145;
RA   Yan M., McBeth D.L.;
RT   "Cloning, DNA sequencing, and characterization of the Pseudomonas putida
RT   PpS145 recA gene, recA-associated gene and recA region.";
RL   Submitted (OCT-1996) 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.
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; L12684; AAC36872.1; -; Genomic_DNA.
DR   EMBL; U70864; AAB16921.1; -; Genomic_DNA.
DR   PIR; T10482; T10482.
DR   RefSeq; WP_016715435.1; NZ_LKKT01000078.1.
DR   AlphaFoldDB; Q07447; -.
DR   SMR; Q07447; -.
DR   STRING; 1240350.AMZE01000013_gene3499; -.
DR   GeneID; 66675709; -.
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..355
FT                   /note="Protein RecA"
FT                   /id="PRO_0000122806"
FT   BINDING         65..72
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00268"
SQ   SEQUENCE   355 AA;  37532 MW;  137C178CC823F7CD CRC64;
     MDDNKKRALA AALGQIERQF GKGAVMRMGD HERQAIPAIS TGSLGLDIAL GIGGLPKGRI
     VEIYGPESSG KTTLTLSVIA EAQKNGATCA FVDAEHALDP EYAGKLGVNV DDLLVSQPDT
     GEQALEITDM LVRSNAVDVI IVDSVAALVP KAEIEGEMGD MHVGLQARLM SQALRKITGN
     IKNANCLVIF INQIRMKIGV MFGSPETTTG GNALKFYASV RLDIRRTGAV KEGDEVVGSE
     TRVKIVKNKV SPPFRQAEFQ ILYGKGIYRN GEIIDLGVSQ GLVEKSGAWY AYQGNKIGQG
     KANAAKYLAE NPAIGAEIEK QIRDKLLTSG AVAAAGKAAA VEADADDMAD ADAGY