RECA_SYNE7
ID RECA_SYNE7 Reviewed; 356 AA.
AC Q31RD9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
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=Synpcc7942_0348;
OS Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS R2).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=1140;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7942 / FACHB-805;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) 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; CP000100; ABB56380.1; -; Genomic_DNA.
DR RefSeq; WP_011243477.1; NC_007604.1.
DR AlphaFoldDB; Q31RD9; -.
DR SMR; Q31RD9; -.
DR STRING; 1140.Synpcc7942_0348; -.
DR PRIDE; Q31RD9; -.
DR EnsemblBacteria; ABB56380; ABB56380; Synpcc7942_0348.
DR KEGG; syf:Synpcc7942_0348; -.
DR eggNOG; COG0468; Bacteria.
DR HOGENOM; CLU_040469_3_2_3; -.
DR OMA; DYGEQAL; -.
DR OrthoDB; 1080436at2; -.
DR BioCyc; SYNEL:SYNPCC7942_0348-MON; -.
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..356
FT /note="Protein RecA"
FT /id="PRO_1000048022"
FT BINDING 71..78
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00268"
SQ SEQUENCE 356 AA; 37928 MW; 9C75F6BB846A97A7 CRC64;
MASKSDAIAP EKEKALNLVL SQIERNFGKG AIMRLGDAAR LRVETISTGA LTLDLALGGG
LPKGRIIEVY GPESSGKTTL TLHAIAEVQK QGGIAAFVDA EHALDPVYAT SVGVDIDNLL
ISQPDTGEMA LEIVDQLVRS AAVDIVVIDS VAALVPRAEI EGEMGDAQVG LQARLMSQAM
RKITGNIGKS GCTVIFLNQL RQKIGVTYGS PETTTGGQAL KFYASVRLDI RRIQTLKKGT
EEYGTRAKVK VVKNKVAPPF RIAEFDILFG KGISTLGCLV DLAEETGVIL RKGAWYSYNG
DNIGQGRDNT ITHLEEHPDF RATVEQQVRE KLALGAQVSA NTVGAAPAKT AEDTDS