LPLT_SALA4
ID LPLT_SALA4 Reviewed; 400 AA.
AC B5F4V3;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 25-MAY-2022, entry version 62.
DE RecName: Full=Lysophospholipid transporter LplT {ECO:0000255|HAMAP-Rule:MF_01585};
GN Name=lplT {ECO:0000255|HAMAP-Rule:MF_01585}; OrderedLocusNames=SeAg_B3156;
OS Salmonella agona (strain SL483).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=454166;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SL483;
RX PubMed=21602358; DOI=10.1128/jb.00297-11;
RA Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA Leclerc J.E., Ravel J., Cebula T.A.;
RT "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT CRISPR-mediated adaptive sublineage evolution.";
RL J. Bacteriol. 193:3556-3568(2011).
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; CP001138; ACH51354.1; -; Genomic_DNA.
DR RefSeq; WP_000004686.1; NC_011149.1.
DR AlphaFoldDB; B5F4V3; -.
DR SMR; B5F4V3; -.
DR EnsemblBacteria; ACH51354; ACH51354; SeAg_B3156.
DR KEGG; sea:SeAg_B3156; -.
DR HOGENOM; CLU_047399_0_0_6; -.
DR OMA; ICFGFNP; -.
DR Proteomes; UP000008819; 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..400
FT /note="Lysophospholipid transporter LplT"
FT /id="PRO_1000201273"
FT TRANSMEM 19..39
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 195..213
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 257..277
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01585"
FT TRANSMEM 281..301
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01585"
FT TRANSMEM 304..324
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01585"
FT TRANSMEM 352..372
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01585"
FT TRANSMEM 373..393
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01585"
SQ SEQUENCE 400 AA; 41571 MW; 897D9BA08496F7D5 CRC64;
MSESVRTNTS IWSKGMLSVI VAQFLSAFGD NALLFATLAL LKAQFYPDWS QPVLQMVFVG
AYILFAPFVG QIADSFAKGR VMMVANGLKL AGAAGICLGV NPFVGYTLVG IGAAAYSPAK
YGILGELTTG DKLVKANGLM EASTIAAILL GSVAGGVLAD WHVIAALVAC ALAYAGAVAA
NLFIPKLVAA RPGQSWRLSA MTRSFFSACV VLWRNGETRF SLVGTGLFWG AGVTLRFLLV
LWVPVALGIT DNATPTYLNA MVAVGIVVGA GAAAKLVTLE TVSRCMPAGI LIGVVVAIFS
LQHALLPAYA LLLLIGMLGG FFVVPLNALL QERGKKSVGA GNAIAVQNLG ENSAMLLMLG
LYSLAVLVGV PAVAIGIGFG VLFALAIAAL WIWQRRQASY