ID RECA_SHIBS Reviewed; 353 AA.
AC Q31X64;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 01-MAY-2013, entry version 53.
DE RecName: Full=Protein RecA;
DE AltName: Full=Recombinase A;
GN Name=recA; OrderedLocusNames=SBO_2819;
OS Shigella boydii serotype 4 (strain Sb227).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300268;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sb227;
RX PubMed=16275786; DOI=10.1093/nar/gki954;
RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X.,
RA Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S.,
RA Nie H., Peng J., Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y.,
RA Qiang B., Hou Y., Yu J., Jin Q.;
RT "Genome dynamics and diversity of Shigella species, the etiologic
RT agents of bacillary dysentery.";
RL Nucleic Acids Res. 33:6445-6458(2005).
CC -!- FUNCTION: Can catalyze the hydrolysis of ATP in the presence of
CC single-stranded DNA, the ATP-dependent uptake of single-stranded
CC DNA by duplex DNA, and the ATP-dependent hybridization of
CC homologous single-stranded DNAs. It interacts with LexA causing
CC its activation and leading to its autocatalytic cleavage (By
CC similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the RecA family.
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DR EMBL; CP000036; ABB67344.1; -; Genomic_DNA.
DR RefSeq; YP_409172.1; NC_007613.1.
DR ProteinModelPortal; Q31X64; -.
DR SMR; Q31X64; 7-329.
DR STRING; 300268.SBO_2819; -.
DR PRIDE; Q31X64; -.
DR EnsemblBacteria; ABB67344; ABB67344; SBO_2819.
DR GeneID; 3781802; -.
DR KEGG; sbo:SBO_2819; -.
DR PATRIC; 18685132; VBIShiBoy33460_3465.
DR eggNOG; COG0468; -.
DR HOGENOM; HOG000264120; -.
DR KO; K03553; -.
DR OMA; TRKGAWY; -.
DR ProtClustDB; PRK09354; -.
DR BioCyc; SBOY300268:GJFL-2816-MONOMER; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR GO; GO:0003684; F:damaged DNA binding; IEA:HAMAP.
DR GO; GO:0008094; F:DNA-dependent ATPase activity; IEA:HAMAP.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:HAMAP.
DR GO; GO:0006310; P:DNA recombination; IEA:HAMAP.
DR GO; GO:0006281; P:DNA repair; IEA:HAMAP.
DR GO; GO:0009432; P:SOS response; IEA:HAMAP.
DR Gene3D; 3.30.250.10; -; 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; IPR020588; DNA_recomb_RecA/RadB_ATP-bd.
DR InterPro; IPR023400; RecA_C.
DR InterPro; IPR020587; RecA_monomer-monomer_interface.
DR PANTHER; PTHR22942:SF1; PTHR22942:SF1; 1.
DR Pfam; PF00154; RecA; 1.
DR PRINTS; PR00142; RECA.
DR SMART; SM00382; AAA; 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; Complete proteome; Cytoplasm; DNA damage;
KW DNA recombination; DNA repair; DNA-binding; Nucleotide-binding;
KW SOS response.
FT CHAIN 1 353 Protein RecA.
FT /FTId=PRO_1000048001.
FT NP_BIND 67 74 ATP (By similarity).
SQ SEQUENCE 353 AA; 37973 MW; 866EF8F83BE32A36 CRC64;
MAIDENKQKA LAAALGQIEK QFGKGSIMRL GEDRSMDVET ISTGSLSLDI ALGAGGLPMG
RIVEIYGPES SGKTTLTLQV IAAAQREGKT CAFIDAEHAL DPIYARKLGV DIDNLLCSQP
DTGEQALEIC DALARSGAVD VIVVDSVAAL TPKAEIEGEI GDSHMGLAAR MMSQAMRKLA
GNLKQSNTLL IFINQIRMKI GVMFGNPETT TGGNALKFYA SVRLDIRRIG AVKEGENVVG
SETRVKVVKN KIAAPFKQAE FQILYGEGIN FYGELVDLGV KEKLIEKAGA WYSYKGEKIG
QGKANATAWL KDNPETAKEI EKKVRELLLS NPNSTPDFSV DDSEGVAETN EDF
//
