LPLT_ECOLI
ID LPLT_ECOLI Reviewed; 397 AA.
AC P39196; Q2MA02; Q46934;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Lysophospholipid transporter LplT;
GN Name=lplT; Synonyms=ygeD; OrderedLocusNames=b2835, JW2803;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-142.
RC STRAIN=K12;
RX PubMed=8300626; DOI=10.1016/s0021-9258(17)42029-1;
RA Jackowski S., Jackson P.D., Rock C.O.;
RT "Sequence and function of the aas gene in Escherichia coli.";
RL J. Biol. Chem. 269:2921-2928(1994).
RN [4]
RP FUNCTION IN ACYL-GPE TRANSPORT.
RC STRAIN=K12 / BW25113;
RX PubMed=15661733; DOI=10.1074/jbc.m414368200;
RA Harvat E.M., Zhang Y.-M., Tran C.V., Zhang Z., Frank M.W., Rock C.O.,
RA Saier M.H. Jr.;
RT "Lysophospholipid flipping across the Escherichia coli inner membrane
RT catalyzed by a transporter (LplT) belonging to the major facilitator
RT superfamily.";
RL J. Biol. Chem. 280:12028-12034(2005).
RN [5]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
CC -!- FUNCTION: Catalyzes the facilitated diffusion of 2-acyl-glycero-3-
CC phosphoethanolamine (2-acyl-GPE) into the cell.
CC {ECO:0000269|PubMed:15661733}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. LplT (TC
CC 2.A.1.42) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=L14681; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U29581; AAB40482.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75874.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76904.1; -; Genomic_DNA.
DR EMBL; L14681; -; NOT_ANNOTATED_CDS; Unassigned_DNA.
DR PIR; D65066; D65066.
DR RefSeq; NP_417312.1; NC_000913.3.
DR RefSeq; WP_000004616.1; NZ_STEB01000034.1.
DR AlphaFoldDB; P39196; -.
DR SMR; P39196; -.
DR BioGRID; 4263140; 265.
DR STRING; 511145.b2835; -.
DR TCDB; 2.A.1.42.1; the major facilitator superfamily (mfs).
DR jPOST; P39196; -.
DR PaxDb; P39196; -.
DR PRIDE; P39196; -.
DR EnsemblBacteria; AAC75874; AAC75874; b2835.
DR EnsemblBacteria; BAE76904; BAE76904; BAE76904.
DR GeneID; 66673298; -.
DR GeneID; 947317; -.
DR KEGG; ecj:JW2803; -.
DR KEGG; eco:b2835; -.
DR PATRIC; fig|1411691.4.peg.3899; -.
DR EchoBASE; EB2349; -.
DR eggNOG; COG0477; Bacteria.
DR HOGENOM; CLU_047399_0_0_6; -.
DR InParanoid; P39196; -.
DR OMA; ICFGFNP; -.
DR PhylomeDB; P39196; -.
DR BioCyc; EcoCyc:EG12455-MON; -.
DR BioCyc; MetaCyc:EG12455-MON; -.
DR PRO; PR:P39196; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; ISM:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0051978; F:lysophospholipid:sodium symporter activity; IEA:InterPro.
DR GO; GO:0006650; P:glycerophospholipid metabolic process; IMP:EcoCyc.
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 1: Evidence at protein level;
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_0000169338"
FT TOPO_DOM 1..17
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 18..38
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 39..52
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 74..90
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 112..144
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 145..165
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 166
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 188..226
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 227..247
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 248..256
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 257..277
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 278..280
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 281..301
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 302..304
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 326..343
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 344..364
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 365..366
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 367..387
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 388..397
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 397 AA; 41656 MW; 0BB3B0DEA7FF534C 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 TVSRCMPAGI LIGVVVLIFS
LQHELLPAYA LLMLIGVMGG FFVVPLNALL QERGKKSVGA GNAIAVQNLG ENSAMLLMLG
IYSLAVMIGI PVVPIGIGFG ALFALAITAL WIWQRRH
