ID   Y1438_STAAR             Reviewed;         279 AA.
AC   Q6GGY2;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=DegV domain-containing protein SAR1438;
GN   OrderedLocusNames=SAR1438;
OS   Staphylococcus aureus (strain MRSA252).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282458;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MRSA252;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
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; BX571856; CAG40435.1; -; Genomic_DNA.
DR   RefSeq; WP_000166055.1; NC_002952.2.
DR   AlphaFoldDB; Q6GGY2; -.
DR   SMR; Q6GGY2; -.
DR   KEGG; sar:SAR1438; -.
DR   HOGENOM; CLU_048251_3_2_9; -.
DR   OMA; IHMTSGL; -.
DR   OrthoDB; 1288126at2; -.
DR   Proteomes; UP000000596; Chromosome.
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.
FT   CHAIN           1..279
FT                   /note="DegV domain-containing protein SAR1438"
FT                   /id="PRO_0000209790"
FT   DOMAIN          4..278
FT                   /note="DegV"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00815"
FT   BINDING         61
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   279 AA;  30616 MW;  2EF596AD28571FC6 CRC64;
     MTKQIIVTDS TSDLSKEYLE ANNIHVIPLS LTIEGASYVD QVDITSEEFI NHIENDEDVK
     TSQPAIGEFI SAYEELGKDG SEIISIHLSS GLSGTFNTAY QASQMVDANV TVIDSKSISF
     GLGYQIQHLV ELVKEGVSTS EIVKKLNHLR ENIKLFVVIG QLNQLIKGGR ISKTKGLIGN
     LMKIKPIGTL DDGRLELVHN ARTQNSSIQY LKKEIAEFIG DHEIKSVGVA HANVIEYVDK
     LKKVFNEAFH VDNYDINVTT PVISAHTGQG AIGLVVLKK