ID RECA_DESVM Reviewed; 357 AA.
AC B8DP00;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 76.
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=DvMF_0876;
OS Desulfovibrio vulgaris (strain DSM 19637 / Miyazaki F).
OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC Desulfovibrionaceae; Nitratidesulfovibrio.
OX NCBI_TaxID=883;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19637 / Miyazaki F;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Hazen T.C.,
RA Richardson P.;
RT "Complete sequence of Desulfovibrio vulgaris str. 'Miyazaki F'.";
RL Submitted (OCT-2008) 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; CP001197; ACL07832.1; -; Genomic_DNA.
DR AlphaFoldDB; B8DP00; -.
DR SMR; B8DP00; -.
DR STRING; 883.DvMF_0876; -.
DR KEGG; dvm:DvMF_0876; -.
DR eggNOG; COG0468; Bacteria.
DR HOGENOM; CLU_040469_1_2_7; -.
DR OrthoDB; 9776733at2; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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; P-loop containing nucleotide triphosphate hydrolases; 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; IPR049261; RecA-like_C.
DR InterPro; IPR049428; RecA-like_N.
DR InterPro; IPR020588; RecA_ATP-bd.
DR InterPro; IPR023400; RecA_C_sf.
DR InterPro; IPR020587; RecA_monomer-monomer_interface.
DR NCBIfam; TIGR02012; tigrfam_recA; 1.
DR PANTHER; PTHR45900:SF1; MITOCHONDRIAL DNA REPAIR PROTEIN RECA HOMOLOG-RELATED; 1.
DR PANTHER; PTHR45900; RECA; 1.
DR Pfam; PF00154; RecA; 1.
DR Pfam; PF21096; RecA_C; 1.
DR PRINTS; PR00142; RECA.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF54752; RecA protein, C-terminal domain; 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..357
FT /note="Protein RecA"
FT /id="PRO_1000193305"
FT BINDING 73..80
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00268"
SQ SEQUENCE 357 AA; 38640 MW; 7C27F276ACDE20DE CRC64;
MAKKPALTPE EMRREALSTA LSTIERKYGQ GSVMKLSDTA HVNIPVIPTG SIGLDLALGV
GGIPRGRVSE IYGPESSGKT TLALHIIAEC QKLGGTAAFI DAEHALDTNY ARRLGVKTDE
LLISQPDFGE QALDIADMLV RSSAVDIVVI DSVAALIPQA ELEGVMGEMQ VGGQARLMSH
ALRKLTGTIH KSRTAVIFIN QIRMKIGTMG YGNPETTTGG NALKFYSSIR MDIRKIQTLK
DKEEVYGSRT RVKVVKNKVA PPFREALFDI LYGTGISRTG ELIDLGSDVG IIEKSGSWFA
FGSERLGQGK ENVRALLEEN EALRLNVEAK LIEHLGMMPS KVVDPDDNAG AMDDDEF
//
