LPLT_SHISS
ID LPLT_SHISS Reviewed; 397 AA.
AC Q3YY22;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Lysophospholipid transporter LplT {ECO:0000255|HAMAP-Rule:MF_01585};
GN Name=lplT {ECO:0000255|HAMAP-Rule:MF_01585}; OrderedLocusNames=SSON_2995;
OS Shigella sonnei (strain Ss046).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300269;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ss046;
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; CP000038; AAZ89590.1; -; Genomic_DNA.
DR AlphaFoldDB; Q3YY22; -.
DR SMR; Q3YY22; -.
DR EnsemblBacteria; AAZ89590; AAZ89590; SSON_2995.
DR KEGG; ssn:SSON_2995; -.
DR HOGENOM; CLU_047399_0_0_6; -.
DR OMA; ICFGFNP; -.
DR Proteomes; UP000002529; 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..397
FT /note="Lysophospholipid transporter LplT"
FT /id="PRO_0000309838"
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; 41674 MW; 0BA8B0D5A7F1A2A3 CRC64;
MSESVHTNTS LWSKGMKAVI VAQFLSAFGD NALLFATLAL LKAQFYPEWS QPILQMVFVG
AYILFAPFVG QVADSFAKGR VMMFANGLKL LGAASICFGI NPFLGYTLVG VGAAAYSPAK
YGILGELTTG SKLVKANGLM EASTIAAILL GSVAGGVLAD WHVLVALAAC ALAYGGAVVA
NIYIPKLAAA RPGQSWNLIN MTRSFLNACT SLWRNGETRF SLVGTSLFWG AGVTLRFLLV
LWVPVALGIT DNATPTYLNA MVAIGIVVGA GAAAKLVTLE TMSRCMPAGI LIGVVVLIFS
LQHELLPAYA LLMLIGVMGG FFVVPLNALL QERGKKSVGA GNAIAVQNLG ENSAMLLMLG
IYSLAVMVGI PVVPIGIGFG ALFALAITAL WIWQRRH
