ID RECA_IDILO Reviewed; 372 AA.
AC Q5QUB8;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 01-MAY-2013, entry version 56.
DE RecName: Full=Protein RecA;
DE AltName: Full=Recombinase A;
GN Name=recA; OrderedLocusNames=IL0742;
OS Idiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae; Idiomarina.
OX NCBI_TaxID=283942;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-735 / DSM 15497 / L2-TR;
RX PubMed=15596722; DOI=10.1073/pnas.0407638102;
RA Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y.,
RA Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S.,
RA Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S.,
RA Campbell S., Denery J., Aizawa S., Shibata S., Malahoff A., Alam M.;
RT "Genome sequence of the deep-sea gamma-proteobacterium Idiomarina
RT loihiensis reveals amino acid fermentation as a source of carbon and
RT energy.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(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; AE017340; AAV81583.1; -; Genomic_DNA.
DR RefSeq; YP_155132.1; NC_006512.1.
DR ProteinModelPortal; Q5QUB8; -.
DR SMR; Q5QUB8; 1-345.
DR STRING; 283942.IL0742; -.
DR EnsemblBacteria; AAV81583; AAV81583; IL0742.
DR GeneID; 3173656; -.
DR KEGG; ilo:IL0742; -.
DR PATRIC; 22139515; VBIIdiLoi21852_0744.
DR eggNOG; COG0468; -.
DR HOGENOM; HOG000264120; -.
DR KO; K03553; -.
DR OMA; TRKGAWY; -.
DR BioCyc; ILOI283942:GI0U-776-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 1 372 Protein RecA.
FT /FTId=PRO_0000122728.
FT NP_BIND 65 72 ATP (By similarity).
SQ SEQUENCE 372 AA; 40387 MW; E7A59175ED73D59E CRC64;
MSNDRQKALD AALGQIERQF GKGSIMRLGD NQTLDIDSVS TGSLGLDIAL GIGGLPFGRV
VEIYGPESSG KTTMTLEVIA EAQKMGKTCA FVDAEHALDP IYAEALGVNV DDLLISQPDT
GEQALEICDM LVRSGAVDIV IVDSVAALTP KAEIEGEMGD SHVGLQARLM SQALRKLTSN
IKKSNTMCIF INQIRMKIGV MFGNPETTTG GNALKFYSSV RLDIRRTGAL KEGDEVVGNE
TRVKVVKNKV APPFKEAHFQ ILYGKGISKE GELIDLGVKH KMVDKAGAWY SYNGDKIGQG
KANSMKFLQD NPKIADELEG RIRELLLSKP EKRTKEIREA ERAAAKEDAK SEAKADKKTE
KKGNEKDDIS LS
//
