RECA_SYNP2
ID RECA_SYNP2 Reviewed; 348 AA.
AC P14582; B1XNZ3;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 143.
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=SYNPCC7002_A0426;
OS Synechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum
OS quadruplicatum).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=32049;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2105307; DOI=10.1128/jb.172.2.967-976.1990;
RA Murphy R.C., Gasparich G.E., Bryant D.A., Porter R.D.;
RT "Nucleotide sequence and further characterization of the Synechococcus sp.
RT strain PCC 7002 recA gene: complementation of a cyanobacterial recA
RT mutation by the Escherichia coli recA gene.";
RL J. Bacteriol. 172:967-976(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27264 / PCC 7002 / PR-6;
RA Li T., Zhao J., Zhao C., Liu Z., Zhao F., Marquardt J., Nomura C.T.,
RA Persson S., Detter J.C., Richardson P.M., Lanz C., Schuster S.C., Wang J.,
RA Li S., Huang X., Cai T., Yu Z., Luo J., Zhao J., Bryant D.A.;
RT "Complete sequence of Synechococcus sp. PCC 7002.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 198-296.
RX PubMed=3108239; DOI=10.1128/jb.169.6.2739-2747.1987;
RA Murphy R.C., Bryant D.A., Porter R.D., Tandeau de Marsac N.;
RT "Molecular cloning and characterization of the recA gene from the
RT cyanobacterium Synechococcus sp. strain PCC 7002.";
RL J. Bacteriol. 169:2739-2747(1987).
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; M29495; AAA88636.1; -; Genomic_DNA.
DR EMBL; CP000951; ACA98436.1; -; Genomic_DNA.
DR EMBL; M16491; AAA27363.1; -; Genomic_DNA.
DR PIR; A35120; RQYCA.
DR RefSeq; WP_012306060.1; NC_010475.1.
DR AlphaFoldDB; P14582; -.
DR SMR; P14582; -.
DR STRING; 32049.SYNPCC7002_A0426; -.
DR EnsemblBacteria; ACA98436; ACA98436; SYNPCC7002_A0426.
DR KEGG; syp:SYNPCC7002_A0426; -.
DR eggNOG; COG0468; Bacteria.
DR HOGENOM; CLU_040469_3_2_3; -.
DR OMA; DYGEQAL; -.
DR Proteomes; UP000001688; 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; IGI:CACAO.
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..348
FT /note="Protein RecA"
FT /id="PRO_0000122874"
FT BINDING 69..76
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00268"
FT CONFLICT 198
FT /note="L -> I (in Ref. 3; AAA27363)"
FT /evidence="ECO:0000305"
FT CONFLICT 238..243
FT /note="SEGEFG -> AKGIC (in Ref. 3; AAA27363)"
FT /evidence="ECO:0000305"
FT CONFLICT 281..289
FT /note="LAEQTGVIT -> SRNKQCHYA (in Ref. 3; AAA27363)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 348 AA; 37244 MW; 066DE28B4023DE1A CRC64;
MSAISNNPDK EKALNLVLNQ IERNFGKGAI MRLGDAAQMK VATIPSGALT LDQAMGGGFP
RGRIVEIYGP ESSGKTTVAL HAIAEVQKAG GVAAFIDAEH ALDPTYSAAL GVDIENLLVA
QPDNGESALE IADQLVRSAA VDLIVIDSVA ALVPRAEIEG EMGDVQVGLQ ARLMSKALRK
IAGNMGRSGC TVIFLNQLRQ KIGISYGNPE VTTGGTALKF YASVRLDIRR IQTLKKGSEG
EFGIRAKVKV AKNKVAPPFR IAEFDIIFGK GISRVGCMLD LAEQTGVITR KGAWYSYEGD
NIAQGRDNAV KYLEENPDVA AIVTQKVREN LDMSSMGFGD EHHTTEEE
