RECA_VIBAN
ID RECA_VIBAN Reviewed; 348 AA.
AC P26348;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 108.
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};
OS Vibrio anguillarum (Listonella anguillarum).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=55601;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1809840; DOI=10.1111/j.1365-2958.1991.tb01861.x;
RA Gammie A.E., Crosa J.H.;
RT "Co-operative autoregulation of a replication protein gene.";
RL Mol. Microbiol. 5:3015-3023(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=531A;
RX PubMed=1544576; DOI=10.1016/0378-1119(92)90442-r;
RA Tolmasky M.E., Gammie A.E., Crosa J.H.;
RT "Characterization of the recA gene of Vibrio anguillarum.";
RL Gene 110:41-48(1992).
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; M80525; AAA27554.1; -; Genomic_DNA.
DR PIR; JQ1461; JQ1461.
DR AlphaFoldDB; P26348; -.
DR SMR; P26348; -.
DR STRING; 55601.VANGNB10_cI0448; -.
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..348
FT /note="Protein RecA"
FT /id="PRO_0000122890"
FT BINDING 65..72
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00268"
SQ SEQUENCE 348 AA; 37558 MW; E2D981A4FAD25844 CRC64;
MDENKQKALA AALGQIEKQF GKGSIMRLGD NRTMDVETIS TGSLSLDIAL GAGGLPMGRI
VEVYGPESSG KTTLTLELIA AAQRVGKTCA FIDAEHALDP IYAKKLGVNI DELLVSQPDT
GEQALEICDA LARSGAIDVI VIDSVAALTP KAEIEGEMGD SHMGLQARML SQAMRKLTGN
LKQSNCMCIF INQIRMKIGV MFGNPETTTG GNALKFYASV RLDIRRTGSI KEGDEAVGNE
TRIKVVKNKI AAPFKQADTQ ILYGQGFNRE GELVDLGVKH KLVEKAGAWY SYNGDKIGQG
KANACKFLRE NPAAAMALDT KLREMLLNPA ELIVEEPILS EMPQEEEL
