ID RECA_BACCR Reviewed; 343 AA.
AC Q81A16;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 01-MAY-2013, entry version 70.
DE RecName: Full=Protein RecA;
DE AltName: Full=Recombinase A;
GN Name=recA; OrderedLocusNames=BC_3779;
OS Bacillus cereus (strain ATCC 14579 / DSM 31).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=226900;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14579 / DSM 31;
RX PubMed=12721630; DOI=10.1038/nature01582;
RA Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B.,
RA Kapatral V., Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A.,
RA Chu L., Mazur M., Goltsman E., Larsen N., D'Souza M., Walunas T.,
RA Grechkin Y., Pusch G., Haselkorn R., Fonstein M., Ehrlich S.D.,
RA Overbeek R., Kyrpides N.C.;
RT "Genome sequence of Bacillus cereus and comparative analysis with
RT Bacillus anthracis.";
RL Nature 423:87-91(2003).
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; AE016877; AAP10703.1; -; Genomic_DNA.
DR RefSeq; NP_833502.1; NC_004722.1.
DR ProteinModelPortal; Q81A16; -.
DR SMR; Q81A16; 3-327.
DR STRING; 226900.BC3779; -.
DR EnsemblBacteria; AAP10703; AAP10703; BC_3779.
DR GeneID; 1206124; -.
DR KEGG; bce:BC3779; -.
DR PATRIC; 32603583; VBIBacCer54481_3895.
DR eggNOG; COG0468; -.
DR KO; K03553; -.
DR OMA; TRKGAWY; -.
DR ProtClustDB; PRK09354; -.
DR BioCyc; BCER226900:GJEU-3775-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 Reference proteome; SOS response.
FT CHAIN 1 343 Protein RecA.
FT /FTId=PRO_0000122650.
FT NP_BIND 64 71 ATP (By similarity).
SQ SEQUENCE 343 AA; 37241 MW; CCFB4FDB70F131C5 CRC64;
MSDRQAALDM ALKQIEKQFG KGSIMKLGEQ AERRVSTVSS GSLALDVALG VGGYPRGRII
EIYGPESSGK TTVSLHAIAE VQRQGGQAAF IDAEHAMDPV YAQKLGVNID ELLLSQPDTG
EQGLEIAEAL VRSGAVDIIV IDSVAALVPK AEIEGDMGDS HVGLQARLMS QALRKLSGAI
NKSKTIAIFI NQIREKVGVM FGNPETTPGG RALKFYSTVR LEVRRAEQLK QGNDIVGNKT
KVKVVKNKVA PPFRVAEVDI MYGEGISREG EILDMASELD IVQKSGAWYS YNEERLGQGR
ENSKQFLKEN TDLREEIAFF IREHHGISED SGAEGAEDST LLD
//
