ID   Y926_STRP8              Reviewed;         282 AA.
AC   Q8P1E4;
DT   28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=DegV domain-containing protein spyM18_0926;
GN   OrderedLocusNames=spyM18_0926;
OS   Streptococcus pyogenes serotype M18 (strain MGAS8232).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=186103;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGAS8232;
RX   PubMed=11917108; DOI=10.1073/pnas.062526099;
RA   Smoot J.C., Barbian K.D., Van Gompel J.J., Smoot L.M., Chaussee M.S.,
RA   Sylva G.L., Sturdevant D.E., Ricklefs S.M., Porcella S.F., Parkins L.D.,
RA   Beres S.B., Campbell D.S., Smith T.M., Zhang Q., Kapur V., Daly J.A.,
RA   Veasy L.G., Musser J.M.;
RT   "Genome sequence and comparative microarray analysis of serotype M18 group
RT   A Streptococcus strains associated with acute rheumatic fever outbreaks.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:4668-4673(2002).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE009949; AAL97570.1; -; Genomic_DNA.
DR   RefSeq; WP_011017667.1; NC_003485.1.
DR   AlphaFoldDB; Q8P1E4; -.
DR   SMR; Q8P1E4; -.
DR   KEGG; spm:spyM18_0926; -.
DR   HOGENOM; CLU_048251_3_1_9; -.
DR   OMA; MALGFCA; -.
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..282
FT                   /note="DegV domain-containing protein spyM18_0926"
FT                   /id="PRO_0000209803"
FT   DOMAIN          3..280
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         94
FT                   /ligand="hexadecanoate"
FT                   /ligand_id="ChEBI:CHEBI:7896"
FT                   /evidence="ECO:0000250|UniProtKB:Q9X1H9"
SQ   SEQUENCE   282 AA;  31389 MW;  D44245E9E264C710 CRC64;
     MKLAVITDST ATLPIDLKQD KAIFSLDIPV IIDDETYFEG RNLSIDDFYQ KMADSQNLPK
     TSQPSLSELD NLLGLLSSKG YTHVIGLFLA GGISGFWQNI QFLAEEHPEI EMAFPDSKIT
     SAPLGSMVKN VLDWSRQGMT FQAILNKLQE QIDRTTAFIM VDDLNHLVKG GRLSNGSALL
     GNLLSIKPIL RFDEEGKIVV YEKVRTEKKA MKRLVEILND LIADGQYNVS IIHSKAQDKA
     DYLKRLLQDS GYQYDIEEVH FGAVIATHLG EGAIAFGVTP RL