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RECA_PSEPG
ID   RECA_PSEPG              Reviewed;         355 AA.
AC   B0KT20;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 1.
DT   03-AUG-2022, entry version 75.
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};
GN   OrderedLocusNames=PputGB1_1231;
OS   Pseudomonas putida (strain GB-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=76869;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Bruce D., Goodwin L., Chertkov O., Brettin T.,
RA   Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., McCarthy J.K., Richardson P.;
RT   "Complete sequence of Pseudomonas putida GB-1.";
RL   Submitted (JAN-2008) 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. {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; CP000926; ABY97138.1; -; Genomic_DNA.
DR   RefSeq; WP_012270915.1; NC_010322.1.
DR   AlphaFoldDB; B0KT20; -.
DR   SMR; B0KT20; -.
DR   STRING; 76869.PputGB1_1231; -.
DR   PRIDE; B0KT20; -.
DR   EnsemblBacteria; ABY97138; ABY97138; PputGB1_1231.
DR   KEGG; ppg:PputGB1_1231; -.
DR   eggNOG; COG0468; Bacteria.
DR   HOGENOM; CLU_040469_3_2_6; -.
DR   OMA; EGARHMS; -.
DR   Proteomes; UP000002157; 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; SOS response.
FT   CHAIN           1..355
FT                   /note="Protein RecA"
FT                   /id="PRO_1000078675"
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;  37504 MW;  7FBC3C7CCA5546F7 CRC64;
     MDDNKKRALA AALGQIERQF GKGAVMRMGD QERQGIPAIS 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 QIREKLLKAG AAAEAGKAAA VDASADDVAD AEAGY
 
 
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