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LPLT_SHIFL
ID   LPLT_SHIFL              Reviewed;         396 AA.
AC   Q83QB9; Q7UBR4;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=Lysophospholipid transporter LplT {ECO:0000255|HAMAP-Rule:MF_01585};
GN   Name=lplT {ECO:0000255|HAMAP-Rule:MF_01585};
GN   OrderedLocusNames=SF2845, S3043;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA   Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA   Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA   Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA   Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA   Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella flexneri
RT   serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(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; AE005674; AAN44331.1; -; Genomic_DNA.
DR   EMBL; AE014073; AAP18157.1; -; Genomic_DNA.
DR   RefSeq; NP_708624.1; NC_004337.2.
DR   RefSeq; WP_000004638.1; NZ_WPGW01000008.1.
DR   AlphaFoldDB; Q83QB9; -.
DR   SMR; Q83QB9; -.
DR   STRING; 198214.SF2845; -.
DR   EnsemblBacteria; AAN44331; AAN44331; SF2845.
DR   EnsemblBacteria; AAP18157; AAP18157; S3043.
DR   GeneID; 1025795; -.
DR   KEGG; sfl:SF2845; -.
DR   KEGG; sft:NCTC1_03131; -.
DR   KEGG; sfx:S3043; -.
DR   PATRIC; fig|198214.7.peg.3385; -.
DR   HOGENOM; CLU_047399_0_0_6; -.
DR   OrthoDB; 961884at2; -.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; 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..396
FT                   /note="Lysophospholipid transporter LplT"
FT                   /id="PRO_0000309836"
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..225
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01585"
FT   TRANSMEM        226..246
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01585"
FT   TOPO_DOM        247..255
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01585"
FT   TRANSMEM        256..276
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01585"
FT   TOPO_DOM        277..279
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01585"
FT   TRANSMEM        280..300
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01585"
FT   TOPO_DOM        301..303
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01585"
FT   TRANSMEM        304..324
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01585"
FT   TOPO_DOM        325..342
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01585"
FT   TRANSMEM        343..363
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01585"
FT   TOPO_DOM        364..365
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01585"
FT   TRANSMEM        366..386
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01585"
FT   TOPO_DOM        387..396
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01585"
FT   CONFLICT        116
FT                   /note="Y -> C (in Ref. 2; AAP18157)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   396 AA;  41419 MW;  B5D29F825AE441F1 CRC64;
     MSESVHTNTS LWSKGMKAVI VAQFLSAFGD NALLFATLAL LKAQFYPEWS QPILQMVFVG
     AYILLAPFVG QVADSFAKGR VMMFANGLKL LGAASICFGI NPFLGYTLVG VGAAAYSPAK
     YGILGELTTG SKLVKANGLM EASAIAAILL GSVAGGVLAD WHVLVALAAC ALAYGGAVVA
     NIYIPKLAAR PGQSWNLINM TRSFLNACTS LWCNGETRFS LVGTSLFWGA GVTLRFLLVL
     WVPVALGITD NATPTYLNAM VAIGIVVGAG AAAKLVTLET VSRCMPAGIL IGVVVPIFSL
     QHELLPAYAL LMLIGVLGGF FVVPLNALLQ ERGKKSVGAG NAIAVQNLGE NSAMLLMLGI
     YSLAVMVGIP VVPIGIGFGA LFALAITALW IWQRRH
 
 
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