ID   RECA_PSETO              Reviewed;         352 AA.
AC   Q9RDU0;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 97.
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 tolaasii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=29442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=1116S;
RX   PubMed=11053404; DOI=10.1128/jb.182.22.6532-6535.2000;
RA   Sinha H., Pain A., Johnstone K.;
RT   "Analysis of the role of recA in phenotypic switching of Pseudomonas
RT   tolaasii.";
RL   J. Bacteriol. 182:6532-6535(2000).
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. Plays a functional role in the DNA
CC       rearrangement associated with the phenotypic switching from a
CC       pathogenic smooth to a nonpathogenic rough form in this bacterium.
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; AJ249265; CAB65373.1; -; Genomic_DNA.
DR   RefSeq; WP_016970800.1; NZ_VZPT01000003.1.
DR   AlphaFoldDB; Q9RDU0; -.
DR   SMR; Q9RDU0; -.
DR   GeneID; 55845948; -.
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_0000122810"
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;  37626 MW;  C879ECD25E53B916 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 NPDIAATLEK QIRDKLLTAA PDVKAAANRE PVDEMEEVDT DI