LPLT_YERPB
ID LPLT_YERPB Reviewed; 406 AA.
AC B2JZ74;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Lysophospholipid transporter LplT {ECO:0000255|HAMAP-Rule:MF_01585};
GN Name=lplT {ECO:0000255|HAMAP-Rule:MF_01585}; OrderedLocusNames=YPTS_3163;
OS Yersinia pseudotuberculosis serotype IB (strain PB1/+).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=502801;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB1/+;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C.,
RA Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Challacombe J.F., Green L., Lindler L.E., Nikolich M.P., Richardson P.;
RT "Complete sequence of Yersinia pseudotuberculosis PB1/+.";
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001048; ACC90118.1; -; Genomic_DNA.
DR RefSeq; WP_002209842.1; NZ_CP009780.1.
DR AlphaFoldDB; B2JZ74; -.
DR SMR; B2JZ74; -.
DR GeneID; 66844527; -.
DR KEGG; ypb:YPTS_3163; -.
DR PATRIC; fig|502801.10.peg.2596; -.
DR OMA; ICFGFNP; -.
DR BioCyc; YPSE502801:YPTS_RS15940-MON; -.
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..406
FT /note="Lysophospholipid transporter LplT"
FT /id="PRO_1000201283"
FT TRANSMEM 16..36
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 227..247
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01585"
FT TRANSMEM 253..273
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01585"
FT TRANSMEM 285..305
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01585"
FT TRANSMEM 310..330
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01585"
FT TRANSMEM 349..369
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01585"
FT TRANSMEM 372..392
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01585"
SQ SEQUENCE 406 AA; 42841 MW; 75DC17EBEC1D1FDE CRC64;
MSQDVLADKP LLSRSMVAVL CAQFFSAFGD NALLFATLAL IKQQLYPDWS QPILQMAFVA
TYIVLAPFVG QIADGFAKGR VMMVANGLKL AGALVICFGL NPFLGYSLVG VGAAAYSPAK
YGILGEITSG EQLVKANGMM EASTIAAILL GSVAGGILAD WHLMAALGVC ALVYAIAVIA
NLFIPRLAAA RSGASWRPRA MTGSFFTACR LLWQDSETRF SLAGTSLFWG AGVTLRFLLV
LWVPVALGIA DNATPTLLNA MVAIGIVVGA GAAARFVTLK TVKRCLPAGV LIGVMVTIFS
LQNSMPMAYL LLIIIGILGG FFVVPLNALL QERGKHSVGA GNAIAVQNLG ENTAMLFMLG
LYSLVVKLGA PVVAVGVGFG VVFALAIALL WGWQWRQQRQ KTRQPE