Y1493_STRP1
ID Y1493_STRP1 Reviewed; 279 AA.
AC P67372; Q48XT1; Q99YY0;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=DegV domain-containing protein SPy_1493/M5005_Spy1226;
GN OrderedLocusNames=SPy_1493, M5005_Spy1226;
OS Streptococcus pyogenes serotype M1.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=301447;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700294 / SF370 / Serotype M1;
RX PubMed=11296296; DOI=10.1073/pnas.071559398;
RA Ferretti J.J., McShan W.M., Ajdic D.J., Savic D.J., Savic G., Lyon K.,
RA Primeaux C., Sezate S., Suvorov A.N., Kenton S., Lai H.S., Lin S.P.,
RA Qian Y., Jia H.G., Najar F.Z., Ren Q., Zhu H., Song L., White J., Yuan X.,
RA Clifton S.W., Roe B.A., McLaughlin R.E.;
RT "Complete genome sequence of an M1 strain of Streptococcus pyogenes.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4658-4663(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-947 / MGAS5005 / Serotype M1;
RX PubMed=16088826; DOI=10.1086/432514;
RA Sumby P., Porcella S.F., Madrigal A.G., Barbian K.D., Virtaneva K.,
RA Ricklefs S.M., Sturdevant D.E., Graham M.R., Vuopio-Varkila J., Hoe N.P.,
RA Musser J.M.;
RT "Evolutionary origin and emergence of a highly successful clone of serotype
RT M1 group A Streptococcus involved multiple horizontal gene transfer
RT events.";
RL J. Infect. Dis. 192:771-782(2005).
RN [3] {ECO:0007744|PDB:2G7Z}
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH HEPTADECANOATE,
RP FUNCTION, AND SUBUNIT.
RG Midwest center for structural genomics (MCSG);
RT "Conserved hypothetical protein from Streptococcus pyogenes M1 GAS
RT discloses long-fatty acid (heptadecanoic acid) binding function.";
RL Submitted (MAR-2006) to the PDB data bank.
CC -!- FUNCTION: Binds long-chain fatty acids, such as palmitate, and may play
CC a role in lipid transport or fatty acid metabolism.
CC {ECO:0000269|Ref.3}.
CC -!- SUBUNIT: Monomer. {ECO:0000305|Ref.3}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAZ51844.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE004092; AAK34292.1; -; Genomic_DNA.
DR EMBL; CP000017; AAZ51844.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_269571.1; NC_002737.2.
DR PDB; 2G7Z; X-ray; 2.05 A; A/B=1-279.
DR PDBsum; 2G7Z; -.
DR AlphaFoldDB; P67372; -.
DR SMR; P67372; -.
DR STRING; 1314.HKU360_01268; -.
DR PaxDb; P67372; -.
DR EnsemblBacteria; AAK34292; AAK34292; SPy_1493.
DR KEGG; spy:SPy_1493; -.
DR KEGG; spz:M5005_Spy1226; -.
DR PATRIC; fig|160490.10.peg.1303; -.
DR HOGENOM; CLU_048251_3_2_9; -.
DR OMA; EIHAKIN; -.
DR EvolutionaryTrace; P67372; -.
DR Proteomes; UP000000750; 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 1: Evidence at protein level;
KW 3D-structure; Lipid-binding; Reference proteome.
FT CHAIN 1..279
FT /note="DegV domain-containing protein
FT SPy_1493/M5005_Spy1226"
FT /id="PRO_0000209804"
FT DOMAIN 4..278
FT /note="DegV"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00815"
FT BINDING 62
FT /ligand="heptadecanoate"
FT /ligand_id="ChEBI:CHEBI:32366"
FT /evidence="ECO:0007744|PDB:2G7Z"
FT BINDING 95
FT /ligand="heptadecanoate"
FT /ligand_id="ChEBI:CHEBI:32366"
FT /evidence="ECO:0007744|PDB:2G7Z"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:2G7Z"
FT HELIX 16..22
FT /evidence="ECO:0007829|PDB:2G7Z"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:2G7Z"
FT STRAND 30..33
FT /evidence="ECO:0007829|PDB:2G7Z"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:2G7Z"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:2G7Z"
FT HELIX 48..55
FT /evidence="ECO:0007829|PDB:2G7Z"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:2G7Z"
FT HELIX 67..79
FT /evidence="ECO:0007829|PDB:2G7Z"
FT STRAND 84..89
FT /evidence="ECO:0007829|PDB:2G7Z"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:2G7Z"
FT HELIX 97..108
FT /evidence="ECO:0007829|PDB:2G7Z"
FT STRAND 112..116
FT /evidence="ECO:0007829|PDB:2G7Z"
FT HELIX 121..137
FT /evidence="ECO:0007829|PDB:2G7Z"
FT HELIX 141..153
FT /evidence="ECO:0007829|PDB:2G7Z"
FT STRAND 155..162
FT /evidence="ECO:0007829|PDB:2G7Z"
FT HELIX 165..170
FT /evidence="ECO:0007829|PDB:2G7Z"
FT HELIX 172..175
FT /evidence="ECO:0007829|PDB:2G7Z"
FT STRAND 187..193
FT /evidence="ECO:0007829|PDB:2G7Z"
FT STRAND 196..205
FT /evidence="ECO:0007829|PDB:2G7Z"
FT HELIX 207..220
FT /evidence="ECO:0007829|PDB:2G7Z"
FT STRAND 225..234
FT /evidence="ECO:0007829|PDB:2G7Z"
FT HELIX 237..246
FT /evidence="ECO:0007829|PDB:2G7Z"
FT TURN 247..249
FT /evidence="ECO:0007829|PDB:2G7Z"
FT STRAND 255..258
FT /evidence="ECO:0007829|PDB:2G7Z"
FT HELIX 261..267
FT /evidence="ECO:0007829|PDB:2G7Z"
FT STRAND 269..278
FT /evidence="ECO:0007829|PDB:2G7Z"
SQ SEQUENCE 279 AA; 29952 MW; 9DADBF96BD822A0D CRC64;
MGTIKIVTDS SITIEPELIK ALDITVVPLS VMIDSKLYSD NDLKEEGHFL SLMKASKSLP
KTSQPPVGLF AETYENLVKK GVTDIVAIHL SPALSGTIEA SRQGAEIAEA PVTVLDSGFT
DQAMKFQVVE AAKMAKAGAS LNEILAAVQA IKSKTELYIG VSTLENLVKG GRIGRVTGVL
SSLLNVKVVM ALKNDELKTL VKGRGNKTFT KWLDSYLAKN SHRPIAEIAI SYAGEASLAL
TLKERIAAYY NHSISVLETG SIIQTHTGEG AFAVMVRYE
