ID RECA_BORA1 Reviewed; 353 AA.
AC Q2KYE8;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 01-MAY-2013, entry version 63.
DE RecName: Full=Protein RecA;
DE AltName: Full=Recombinase A;
GN Name=recA; OrderedLocusNames=BAV2309;
OS Bordetella avium (strain 197N).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=360910;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=197N;
RX PubMed=16885469; DOI=10.1128/JB.01927-05;
RA Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D.,
RA King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D.,
RA Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R.,
RA Squares S., Woodward J., Parkhill J., Temple L.M.;
RT "Comparison of the genome sequence of the poultry pathogen Bordetella
RT avium with those of B. bronchiseptica, B. pertussis, and B.
RT parapertussis reveals extensive diversity in surface structures
RT associated with host interaction.";
RL J. Bacteriol. 188:6002-6015(2006).
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; AM167904; CAJ49919.1; -; Genomic_DNA.
DR RefSeq; YP_786823.1; NC_010645.1.
DR ProteinModelPortal; Q2KYE8; -.
DR SMR; Q2KYE8; 3-332.
DR STRING; 360910.BAV2309; -.
DR GeneID; 6267635; -.
DR KEGG; bav:BAV2309; -.
DR PATRIC; 21130849; VBIBorAvi43433_2334.
DR eggNOG; COG0468; -.
DR HOGENOM; HOG000264120; -.
DR KO; K03553; -.
DR OMA; MLIFINQ; -.
DR ProtClustDB; PRK09354; -.
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_1000193291.
FT NP_BIND 73 80 ATP (By similarity).
SQ SEQUENCE 353 AA; 37879 MW; C21923851E879EA5 CRC64;
MDEKTSKAAS EKAKALAAAL SQIEKQFGKG SIMRYGDNEV EHDIQVVSTG SLGLDIALGV
GGLPRGRVVE IYGPESSGKT TLTLQVIAEM QKVGGTCAFV DAEHALDVQY ASKLGVNLGD
LLISQPDTGE QALEITDALV RSGSVDLIVI DSVAALVPKA EIEGEMGDAL PGLQARLMSQ
ALRKLTATIK RTNCMVIFIN QIRMKIGVMF GNPETTTGGN ALKFYSSVRL DIRRIGSIKK
GDEVVGNETR VKVVKNKVAP PFKQAEFDIM YGAGISREGE IIDLGVAANV IEKSGAWYSY
SGNRIGQGKD NVREYLKENR AMAIEIENKI RDNQGIVARA AEFAPTAEES AED
//
