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LPLT_SHIDS
ID   LPLT_SHIDS              Reviewed;         397 AA.
AC   Q32C86;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Lysophospholipid transporter LplT {ECO:0000255|HAMAP-Rule:MF_01585};
GN   Name=lplT {ECO:0000255|HAMAP-Rule:MF_01585}; OrderedLocusNames=SDY_3052;
OS   Shigella dysenteriae serotype 1 (strain Sd197).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300267;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sd197;
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA   Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA   Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA   Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT   bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
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; CP000034; ABB63069.1; -; Genomic_DNA.
DR   RefSeq; WP_000004606.1; NC_007606.1.
DR   RefSeq; YP_404560.1; NC_007606.1.
DR   AlphaFoldDB; Q32C86; -.
DR   SMR; Q32C86; -.
DR   STRING; 300267.SDY_3052; -.
DR   EnsemblBacteria; ABB63069; ABB63069; SDY_3052.
DR   KEGG; sdy:SDY_3052; -.
DR   PATRIC; fig|300267.13.peg.3657; -.
DR   HOGENOM; CLU_047399_0_0_6; -.
DR   OMA; ICFGFNP; -.
DR   Proteomes; UP000002716; 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   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..397
FT                   /note="Lysophospholipid transporter LplT"
FT                   /id="PRO_0000309835"
FT   TOPO_DOM        1..17
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01585"
FT   TRANSMEM        18..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01585"
FT   TOPO_DOM        39..52
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01585"
FT   TRANSMEM        53..73
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01585"
FT   TOPO_DOM        74..90
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01585"
FT   TRANSMEM        91..111
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01585"
FT   TOPO_DOM        112..144
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01585"
FT   TRANSMEM        145..165
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01585"
FT   TOPO_DOM        166
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01585"
FT   TRANSMEM        167..187
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01585"
FT   TOPO_DOM        188..226
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01585"
FT   TRANSMEM        227..247
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01585"
FT   TOPO_DOM        248..256
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01585"
FT   TRANSMEM        257..277
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01585"
FT   TOPO_DOM        278..280
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01585"
FT   TRANSMEM        281..301
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01585"
FT   TOPO_DOM        302..304
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01585"
FT   TRANSMEM        305..325
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01585"
FT   TOPO_DOM        326..343
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01585"
FT   TRANSMEM        344..364
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01585"
FT   TOPO_DOM        365..366
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01585"
FT   TRANSMEM        367..387
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01585"
FT   TOPO_DOM        388..397
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01585"
SQ   SEQUENCE   397 AA;  41570 MW;  80136BBFAD91B3AE CRC64;
     MSESVHTNTS LWSKGMKAVI VAQFLSAFGD NALLFATLAL LKAQFYPEWS QPILQMVFVG
     AYILFAPFVG QVADSFAKGR VMMFANGLKL LGAASICFGI NPFLGYTLVG VGAAAYSPAK
     YGILGELTTG SKLVKANGLM EASTIAAILL GSVAGGVLAD WHVLVALAAC ALAYGGAVVA
     NIYIPKLAAA RPGQSWNLIN MTRSFLNACT SLWCNGETRF SLVGTSLFWG AGVTLRFLLV
     LWVPVALGIT DNATPTYLNA MVAIGIVVGA GAAAKLVTLE TVSRCMPAGI LIGVVVLIFS
     LQHELLPAYA LLMLIGVLGG FFVVPLNALL QERGKKSVGA GNAIAVQNLG ENSAMLLMLG
     IYSLAVMVGI PVVPIGIGFG ALFALAITAL WIWQRRH
 
 
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