ID RECA_RHILO Reviewed; 365 AA.
AC Q98NQ6;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 01-MAY-2013, entry version 66.
DE RecName: Full=Protein RecA;
DE AltName: Full=Recombinase A;
GN Name=recA; OrderedLocusNames=mlr0030;
OS Rhizobium loti (strain MAFF303099) (Mesorhizobium loti).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC Phyllobacteriaceae; Mesorhizobium.
OX NCBI_TaxID=266835;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAFF303099;
RX PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T.,
RA Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Mochizuki Y., Nakayama S., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takeuchi C., Yamada M., Tabata S.;
RT "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT Mesorhizobium loti.";
RL DNA Res. 7:331-338(2000).
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; BA000012; BAB47705.1; -; Genomic_DNA.
DR RefSeq; NP_101919.1; NC_002678.2.
DR ProteinModelPortal; Q98NQ6; -.
DR SMR; Q98NQ6; 15-336.
DR STRING; 266835.mlr0030; -.
DR EnsemblBacteria; BAB47705; BAB47705; BAB47705.
DR GeneID; 1224582; -.
DR KEGG; mlo:mlr0030; -.
DR PATRIC; 22474196; VBIMesLot2464_0025.
DR eggNOG; COG0468; -.
DR HOGENOM; HOG000264120; -.
DR KO; K03553; -.
DR OMA; TRKGAWY; -.
DR ProtClustDB; PRK09354; -.
DR BioCyc; MLOT266835:GJ9L-24-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 1 365 Protein RecA.
FT /FTId=PRO_0000122813.
FT NP_BIND 77 84 ATP (By similarity).
SQ SEQUENCE 365 AA; 39062 MW; D15179C534FA8ACB CRC64;
MAQNSLRLVE DKAVDKSKAL DAALSQIERA FGKGSIMRLG ANEQVVEIET VPTGSLGLDI
ALGVGGLPRG RIIEIYGPES SGKTTLALHT VAEAQKKGGI CAFVDAEHAL DPVYARKLGV
DLENLLISQP DTGEQALEIC DTLVRSGAID VLVVDSVAAL TPRAEIEGEM GDSLPGLQAR
LMSQALRKLT ASISRSNTMV IFINQIRMKI GVMFGSPETT TGGNALKFYA SVRLDIRRIG
SVKDRDEVVG NQTRVKVVKN KLAPPFKVVE FDIMYGEGVS KTGELVDLGV KAGVVEKSGA
WFSYNSQRLG QGRENAKLFL RDNPDTAREI ELALRQNAGL IAEKFLENGG SEGGDDGFED
EAGAM
//