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Database: UniProt
Entry: Q5QUB8
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Original site: Q5QUB8 
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   03-SEP-2014, entry version 64.
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; WP_011233994.1; NC_006512.1.
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; NTYGELI; -.
DR   OrthoDB; EOG6ZKXNZ; -.
DR   BioCyc; ILOI283942:GI0U-741-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003684; F:damaged DNA binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008094; F:DNA-dependent ATPase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003697; F:single-stranded DNA binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009432; P:SOS response; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.30.250.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 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; IPR027417; P-loop_NTPase.
DR   InterPro; IPR020588; RecA_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; 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    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
//
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