ID RECA_ERWCT Reviewed; 357 AA.
AC Q6D1S8;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 01-MAY-2013, entry version 60.
DE RecName: Full=Protein RecA;
DE AltName: Full=Recombinase A;
GN Name=recA; OrderedLocusNames=ECA3369;
OS Erwinia carotovora subsp. atroseptica (strain SCRI 1043 / ATCC
OS BAA-672) (Pectobacterium atrosepticum).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Pectobacterium.
OX NCBI_TaxID=218491;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCRI 1043 / ATCC BAA-672;
RX PubMed=15263089; DOI=10.1073/pnas.0402424101;
RA Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J.,
RA Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K.,
RA Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J.,
RA Fraser A., Hance Z., Hauser H., Jagels K., Moule S., Norbertczak H.,
RA Ormond D., Price C., Quail M.A., Sanders M., Walker D., Whitehead S.,
RA Salmond G.P.C., Birch P.R.J., Parkhill J., Toth I.K.;
RT "Genome sequence of the enterobacterial phytopathogen Erwinia
RT carotovora subsp. atroseptica and characterization of virulence
RT factors.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(2004).
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; BX950851; CAG76267.1; -; Genomic_DNA.
DR RefSeq; YP_051458.1; NC_004547.2.
DR ProteinModelPortal; Q6D1S8; -.
DR SMR; Q6D1S8; 2-333.
DR STRING; 218491.ECA3369; -.
DR PRIDE; Q6D1S8; -.
DR EnsemblBacteria; CAG76267; CAG76267; ECA3369.
DR GeneID; 2885057; -.
DR KEGG; eca:ECA3369; -.
DR PATRIC; 20482125; VBIPecAtr54885_3423.
DR eggNOG; COG0468; -.
DR HOGENOM; HOG000264120; -.
DR KO; K03553; -.
DR OMA; TRKGAWY; -.
DR ProtClustDB; PRK09354; -.
DR BioCyc; PATR218491:GJNB-3436-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 1 357 Protein RecA.
FT /FTId=PRO_0000122715.
FT NP_BIND 67 74 ATP (By similarity).
SQ SEQUENCE 357 AA; 38284 MW; 48F1FFB8232E0098 CRC64;
MAIDENKQKA LAAALGQIEK QFGKGSIMRL GEDRSMDVET ISTGSLSLDI ALGAGGLPMG
RIVEIYGPES SGKTTLTLQV IAAAQREGKT CAFIDAEHAL DPIYAKKLGV DIDNLLCSQP
DTGEQALEIC DALTRSGAVD VIIVDSVAAL TPKAEIEGEI GDSHMGLAAR MMSQAMRKLA
GNLKQANTLL IFINQIRMKI GVMFGNPETT TGGNALKFYA SVRLDIRRTG AIKEGEEVVG
SETRVKVVKN KVAAPFKQAE FQILYGEGIN IHGELVDLGV KHKLIEKAGA WYSYNGDKIG
QGKANACNFL KENPTISAEL DKKLREMLLH KGNELKPAAA GNSHDEDELA GEGKEEF
//