RECA_XANCP
ID RECA_XANCP Reviewed; 343 AA.
AC Q60101;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 138.
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=XCC1722;
OS Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS 528 / LMG 568 / P 25).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=190485;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Xc17;
RX PubMed=8619877; DOI=10.1006/bbrc.1996.0617;
RA Lee T.C., Lin N.T., Tseng Y.H.;
RT "Isolation and characterization of the recA gene of Xanthomonas campestris
RT pv. campestris.";
RL Biochem. Biophys. Res. Commun. 221:459-465(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Xc33-1;
RX PubMed=12007798; DOI=10.1111/j.1574-6968.2002.tb11124.x;
RA Yang Y.-C., Hsu C.-H., Chou C.-P., Yang M.-K.;
RT "Genetic organization of the lexA, recA and recX genes in Xanthomonas
RT campestris.";
RL FEMS Microbiol. Lett. 209:149-154(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
RX PubMed=12024217; DOI=10.1038/417459a;
RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT specificities.";
RL Nature 417:459-463(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.
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; U49086; AAC44078.1; -; Genomic_DNA.
DR EMBL; AF399933; AAK85398.1; -; Genomic_DNA.
DR EMBL; AE008922; AAM41016.1; -; Genomic_DNA.
DR PIR; JC4718; JC4718.
DR RefSeq; NP_637092.1; NC_003902.1.
DR RefSeq; WP_011036899.1; NC_003902.1.
DR AlphaFoldDB; Q60101; -.
DR SMR; Q60101; -.
DR STRING; 340.xcc-b100_2537; -.
DR EnsemblBacteria; AAM41016; AAM41016; XCC1722.
DR GeneID; 58013723; -.
DR KEGG; xcc:XCC1722; -.
DR PATRIC; fig|190485.4.peg.1838; -.
DR eggNOG; COG0468; Bacteria.
DR HOGENOM; CLU_040469_1_2_6; -.
DR OMA; EGARHMS; -.
DR Proteomes; UP000001010; 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..343
FT /note="Protein RecA"
FT /id="PRO_0000122903"
FT BINDING 65..72
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00268"
SQ SEQUENCE 343 AA; 37018 MW; 89DFAC288977B83C CRC64;
MDENKKRALS AALSQIEKQF GKGSVMRMGD RVIEAVEVIP TGSLMLDIAL GIGGLPKGRV
VEIYGPESSG KTTLTLQAIA ECQKLGGTAA FIDAEHALDP IYAAKLGVNV DDLLLSQPDT
GEQALEIADM LVRSSSVDIV VIDSVAALTP KAEIEGEMGD QLPGLQARLM SQALRKLTGN
IKRSNTLVVF INQLRMKIGV MMPGQSPEVT TGGNALKFYA SVRLDIRRIG AIKKGDEIIG
NQTKIKVVKN KLAPPFKQVI TEILYGEGIS REGELIDMGV EAKLVDKAGA WYSYGDERIG
QGKDNARGYL RDNPQVAIKL EAELREKFQP AEAPREAGET ESE
