ID   Y500_DEIRA              Reviewed;         287 AA.
AC   Q9RX15;
DT   28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=DegV domain-containing protein DR_0500;
GN   OrderedLocusNames=DR_0500;
OS   Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS   4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=243230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC   9279 / R1 / VKM B-1422;
RX   PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA   White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA   Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA   Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA   Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA   Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA   Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA   Fraser C.M.;
RT   "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT   R1.";
RL   Science 286:1571-1577(1999).
CC   -!- FUNCTION: May bind long-chain fatty acids, such as palmitate, and may
CC       play a role in lipid transport or fatty acid metabolism. {ECO:0000250}.
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DR   EMBL; AE000513; AAF10080.1; -; Genomic_DNA.
DR   PIR; A75511; A75511.
DR   RefSeq; NP_294223.1; NC_001263.1.
DR   RefSeq; WP_010887145.1; NZ_CP015081.1.
DR   AlphaFoldDB; Q9RX15; -.
DR   SMR; Q9RX15; -.
DR   STRING; 243230.DR_0500; -.
DR   EnsemblBacteria; AAF10080; AAF10080; DR_0500.
DR   KEGG; dra:DR_0500; -.
DR   PATRIC; fig|243230.17.peg.678; -.
DR   eggNOG; COG1307; Bacteria.
DR   HOGENOM; CLU_048251_0_1_0; -.
DR   InParanoid; Q9RX15; -.
DR   OMA; TELYFTI; -.
DR   OrthoDB; 1288126at2; -.
DR   Proteomes; UP000002524; Chromosome I.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1180.10; -; 1.
DR   InterPro; IPR003797; DegV.
DR   InterPro; IPR043168; DegV_C.
DR   Pfam; PF02645; DegV; 1.
DR   TIGRFAMs; TIGR00762; DegV; 1.
DR   PROSITE; PS51482; DEGV; 1.
PE   3: Inferred from homology;
KW   Lipid-binding; Reference proteome.
FT   CHAIN           1..287
FT                   /note="DegV domain-containing protein DR_0500"
FT                   /id="PRO_0000209762"
FT   DOMAIN          7..280
FT                   /note="DegV"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00815"
FT   BINDING         62
FT                   /ligand="hexadecanoate"
FT                   /ligand_id="ChEBI:CHEBI:7896"
FT                   /evidence="ECO:0000250|UniProtKB:Q9X1H9"
FT   BINDING         93
FT                   /ligand="hexadecanoate"
FT                   /ligand_id="ChEBI:CHEBI:7896"
FT                   /evidence="ECO:0000250|UniProtKB:Q9X1H9"
SQ   SEQUENCE   287 AA;  30591 MW;  4E247F9B2D278771 CRC64;
     MTAMPSFAVV TDGGLDAYPT LLNDVPVAPF SVAFGERSYP MNEVSRQWLY DELGRNPAHP
     TSSQPSPQQW LDAYAAVPSG TDILAVTISS GLSGSRNAAA QARDLAGRQV TLHDSMTLSA
     AQAFQVHAAN VAAQRGESME TAIAWMNAVQ AETELQFTIE TLEYLRRGGR IGTVAAALGG
     LLNLKPVVMV DKKTGTYVNA GRARSYRGGI EAVTSQVTRK YGEGTPLRVG LLYGTHPEDA
     DQALEQLAAR HPIVWSDRTG VNPVLSVHVG PRALGVAAAP GAWPWER