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LPLT_SALTI
ID   LPLT_SALTI              Reviewed;         400 AA.
AC   Q8Z407; Q7C7F6;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 106.
DE   RecName: Full=Lysophospholipid transporter LplT {ECO:0000255|HAMAP-Rule:MF_01585};
GN   Name=lplT {ECO:0000255|HAMAP-Rule:MF_01585};
GN   OrderedLocusNames=STY3152, t2918;
OS   Salmonella typhi.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT18;
RX   PubMed=11677608; DOI=10.1038/35101607;
RA   Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA   Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA   Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA   Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA   Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA   Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA   Barrell B.G.;
RT   "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT   serovar Typhi CT18.";
RL   Nature 413:848-852(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700931 / Ty2;
RX   PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA   Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA   Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT   "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT   CT18.";
RL   J. Bacteriol. 185:2330-2337(2003).
CC   -!- FUNCTION: Catalyzes the facilitated diffusion of 2-acyl-glycero-3-
CC       phosphoethanolamine (2-acyl-GPE) into the cell. {ECO:0000255|HAMAP-
CC       Rule:MF_01585}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01585}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01585}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily. LplT (TC
CC       2.A.1.42) family. {ECO:0000255|HAMAP-Rule:MF_01585}.
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DR   EMBL; AE014613; AAO70472.1; -; Genomic_DNA.
DR   EMBL; AL513382; CAD02834.1; -; Genomic_DNA.
DR   RefSeq; NP_457403.1; NC_003198.1.
DR   RefSeq; WP_000004684.1; NZ_WSUR01000055.1.
DR   AlphaFoldDB; Q8Z407; -.
DR   SMR; Q8Z407; -.
DR   STRING; 220341.16504088; -.
DR   EnsemblBacteria; AAO70472; AAO70472; t2918.
DR   KEGG; stt:t2918; -.
DR   KEGG; sty:STY3152; -.
DR   PATRIC; fig|220341.7.peg.3206; -.
DR   eggNOG; COG0477; Bacteria.
DR   HOGENOM; CLU_047399_0_0_6; -.
DR   OMA; ICFGFNP; -.
DR   Proteomes; UP000000541; Chromosome.
DR   Proteomes; UP000002670; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051978; F:lysophospholipid:sodium symporter activity; IEA:InterPro.
DR   Gene3D; 1.20.1250.20; -; 1.
DR   HAMAP; MF_01585; MFS_LplT; 1.
DR   InterPro; IPR023727; LysoPLipid__transptr_LplT.
DR   InterPro; IPR011701; MFS.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   Pfam; PF07690; MFS_1; 1.
DR   SUPFAM; SSF103473; SSF103473; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Lipid transport; Membrane;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..400
FT                   /note="Lysophospholipid transporter LplT"
FT                   /id="PRO_0000309832"
FT   TRANSMEM        19..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01585"
FT   TRANSMEM        53..73
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01585"
FT   TRANSMEM        91..111
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01585"
FT   TRANSMEM        139..159
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01585"
FT   TRANSMEM        164..184
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01585"
FT   TRANSMEM        195..213
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01585"
FT   TRANSMEM        227..247
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01585"
FT   TRANSMEM        257..277
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01585"
FT   TRANSMEM        281..301
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01585"
FT   TRANSMEM        304..324
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01585"
FT   TRANSMEM        352..372
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01585"
FT   TRANSMEM        373..393
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01585"
SQ   SEQUENCE   400 AA;  41588 MW;  9D22D0AFC0C9BCD5 CRC64;
     MSESVRTNTS IWSKGMLSVI VAQFLSAFGD NALLFATLAL LKAQFYPDWS QPVLQMVFVG
     AYILFAPFVG QIADSFAKGR VMMVANGLKL AGAAGICLGV NPFVGYTLVG IGAAAYSPAK
     YGILGELTTG DKLVKANGLM EASTIAAILL GSVAGGVLAD WHVIAALVAC ALAYAGAVAA
     NLFIPKLVAA RPGQSWRLSA MTRSFFCACV VLWRNGETRF SLVGTGLFWG AGVTLRFLLV
     LWVPVALGIT DNATPTYLNA MVAVGIVVGA GAAAKLVTLE TVSRCMPAGI LIGVVVAIFS
     LQHALLPAYA LLLLIGMLGG FFVVPLNALL QERGKKSVGA GNAIAVQNLG ENSAMLLMLG
     LYSLAVLVGV PAVAIGIGFG VLFALAIAAL WIWQRRQASY
 
 
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