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
