RECA_SYNPW
ID RECA_SYNPW Reviewed; 382 AA.
AC A5GIV0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=SynWH7803_0439;
OS Synechococcus sp. (strain WH7803).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=32051;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH7803;
RG Genoscope;
RL Submitted (MAY-2006) 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; CT971583; CAK22865.1; -; Genomic_DNA.
DR RefSeq; WP_011932353.1; NC_009481.1.
DR AlphaFoldDB; A5GIV0; -.
DR SMR; A5GIV0; -.
DR STRING; 32051.SynWH7803_0439; -.
DR EnsemblBacteria; CAK22865; CAK22865; SynWH7803_0439.
DR KEGG; syx:SynWH7803_0439; -.
DR eggNOG; COG0468; Bacteria.
DR HOGENOM; CLU_040469_3_2_3; -.
DR OMA; DYGEQAL; -.
DR OrthoDB; 1080436at2; -.
DR Proteomes; UP000001566; 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..382
FT /note="Protein RecA"
FT /id="PRO_1000048023"
FT REGION 362..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 79..86
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00268"
SQ SEQUENCE 382 AA; 40592 MW; 7B8C7F211E62D6C2 CRC64;
MPVEVKSSQS SGGDVRPGER DQALNLVLGQ IERNFGKGSI MRLGDASRMR VETISTGALT
LDLALGGGYP KGRVVEVYGP ESSGKTTLTL HAIAEVQRRG GVAAFVDAEH ALDPVYAASL
GVDIENLLVS QPDTGEMALE IVDQLVRSAA VDIVVVDSVA ALTPRAEIEG EMGDLAVGSQ
ARLMSQAMRK ITGNIGKSGC TVIFLNQLRL KIGVTYGNPE TTTGGNALKF YASVRLDIRR
IQTLKRGTEE YGIRAKVKVA KNKVAPPFRI AEFDILFGRG ISTLGCLLDL AEETGVVTRK
GAWYSYEGDN IGQGRDNTIG WLEQNPEAKD TIETLVRQKL TEGSEVTSNS MRPLAAAARS
AATKSAAKGS EVQADVKTKG AA
