ID RECA_MYCSJ Reviewed; 347 AA.
AC A3PYE3;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 29-MAY-2013, entry version 51.
DE RecName: Full=Protein RecA;
DE AltName: Full=Recombinase A;
GN Name=recA; OrderedLocusNames=Mjls_2134;
OS Mycobacterium sp. (strain JLS).
OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC Corynebacterineae; Mycobacteriaceae; Mycobacterium.
OX NCBI_TaxID=164757;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JLS;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Miller C.D., Anderson A.J., Sims R.C., Richardson P.;
RT "Complete sequence of Mycobacterium sp. JLS.";
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000580; ABN97920.1; -; Genomic_DNA.
DR RefSeq; YP_001070411.1; NC_009077.1.
DR ProteinModelPortal; A3PYE3; -.
DR SMR; A3PYE3; 1-329.
DR STRING; 164757.Mjls_2134; -.
DR EnsemblBacteria; ABN97920; ABN97920; Mjls_2134.
DR GeneID; 4877854; -.
DR KEGG; mjl:Mjls_2134; -.
DR PATRIC; 18090396; VBIMycSp51234_2138.
DR eggNOG; COG0468; -.
DR HOGENOM; HOG000264120; -.
DR KO; K03553; -.
DR OMA; MLIFINQ; -.
DR ProtClustDB; PRK09354; -.
DR BioCyc; MSP164757:GHV3-2145-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; IPR027417; P-loop_NTPase.
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; 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; Complete proteome; Cytoplasm; DNA damage;
KW DNA recombination; DNA repair; DNA-binding; Nucleotide-binding;
KW SOS response.
FT CHAIN 1 347 Protein RecA.
FT /FTId=PRO_1000078671.
FT NP_BIND 68 75 ATP (By similarity).
SQ SEQUENCE 347 AA; 36913 MW; 96029E92DCEA325A CRC64;
MAPQAPDREK ALELALAQIE KSHGKGSVMR LGDEVRAPIS VIPTGSIALD VALGIGGLPR
GRVIEIYGPE SSGKTTVALH AVANAQAAGG IAAFIDAEHA LDPDYAKKLG VDTDSLLVSQ
PDTGEQALEI ADMLIRSGAL DILVIDSVAA LVPRAEIEGE MGDSHVGLQA RLMSQALRKI
TGALSNSGTT AIFINQLREK IGVMFGSPET TTGGKALKFY ASVRMDVRRI ETLKDGTDAV
GNRTRVKIVK NKVSPPFKQA EFDILYGKGI SKEGSLIDMG VEHGFIRKSG SWFTYEGEQL
GQGKENARKF LLENGDVANE IEKKIKEKLN IGAVVTADDV LPAPVDF
//
