RECA_SHEWM
ID RECA_SHEWM Reviewed; 353 AA.
AC B1KPS6;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, 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}; OrderedLocusNames=Swoo_3340;
OS Shewanella woodyi (strain ATCC 51908 / MS32).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=392500;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51908 / MS32;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., 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 Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Lykidis A., Zhao J.-S., Richardson P.;
RT "Complete sequence of Shewanella woodyi ATCC 51908.";
RL Submitted (FEB-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; CP000961; ACA87609.1; -; Genomic_DNA.
DR RefSeq; WP_012325944.1; NC_010506.1.
DR AlphaFoldDB; B1KPS6; -.
DR SMR; B1KPS6; -.
DR STRING; 392500.Swoo_3340; -.
DR PRIDE; B1KPS6; -.
DR EnsemblBacteria; ACA87609; ACA87609; Swoo_3340.
DR KEGG; swd:Swoo_3340; -.
DR eggNOG; COG0468; Bacteria.
DR HOGENOM; CLU_040469_3_2_6; -.
DR OMA; DYGEQAL; -.
DR OrthoDB; 1080436at2; -.
DR Proteomes; UP000002168; 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..353
FT /note="Protein RecA"
FT /id="PRO_1000114368"
FT BINDING 67..74
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00268"
SQ SEQUENCE 353 AA; 37812 MW; 0D18E720455CBFFA CRC64;
MKIDANKEKA LNAVLGQIEK QFGKGSIMKL GENRSMDVET ISTGSLSLDV ALGAGGLPMG
RIVEIYGPES SGKTTLTLEL IAAAQREGKV CAFIDAEHAL DPIYAKKLGV DIDNLLCSQP
DTGEQALEIC DALTRSGAVD VIVVDSVAAL TPKAEIEGEI GDSHMGLAAR MMSQAMRKLA
GNLKQTNTML IFINQIRMKI GVMFGNPETT TGGNALKFYA SVRLDIRRTG AIKERDEVVG
NETRVKVVKN KIAAPFKQAE FQILYGQGIN RTGELVDLGV AHKLVEKAGA WYSYKGDKIG
QGRANAGKFL LDNPAIAEEI DTALRGMLLA SVEPAVESEV GDENVDLETG EIF