LPLT_PECCP
ID LPLT_PECCP Reviewed; 407 AA.
AC C6DE42;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 1.
DT 25-MAY-2022, entry version 63.
DE RecName: Full=Lysophospholipid transporter LplT {ECO:0000255|HAMAP-Rule:MF_01585};
GN Name=lplT {ECO:0000255|HAMAP-Rule:MF_01585}; OrderedLocusNames=PC1_3462;
OS Pectobacterium carotovorum subsp. carotovorum (strain PC1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Pectobacterium.
OX NCBI_TaxID=561230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PC1;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C.,
RA Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Balakrishnan V., Glasner J., Perna N.T.;
RT "Complete sequence of Pectobacterium carotovorum subsp. carotovorum PC1.";
RL Submitted (JUL-2009) 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; CP001657; ACT14478.1; -; Genomic_DNA.
DR RefSeq; WP_015841601.1; NC_012917.1.
DR AlphaFoldDB; C6DE42; -.
DR SMR; C6DE42; -.
DR STRING; 561230.PC1_3462; -.
DR EnsemblBacteria; ACT14478; ACT14478; PC1_3462.
DR KEGG; pct:PC1_3462; -.
DR eggNOG; COG0477; Bacteria.
DR HOGENOM; CLU_047399_0_0_6; -.
DR OMA; ICFGFNP; -.
DR OrthoDB; 961884at2; -.
DR Proteomes; UP000002736; 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..407
FT /note="Lysophospholipid transporter LplT"
FT /id="PRO_1000215630"
FT TRANSMEM 18..38
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 163..183
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01585"
FT TRANSMEM 229..249
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 286..306
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 343..365
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01585"
FT TRANSMEM 375..395
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01585"
SQ SEQUENCE 407 AA; 42614 MW; AE66E799243745DD CRC64;
MSQQTEPATP LLSRSMNAVI IAQFFSAFGD NALLFATLAL IKQLVYPDWS QPFLQMGFVA
AYIILAPFVG QIADSFSKGQ VMMFANTLKL AGALLICVGG NPFLGYTLVG VGAAAYSPAK
YGILGEITRG DQLVKANGLM EASTIAAILT GSVAGGVLAD WNIYGALSIC AVAYGIALGA
NMLIPRLNAA RPGQPWHPVQ MASSFFSACR VLWRDGDARL SLVGTSMFWG AGVTLRFLLV
LWVPHALGIT DNATPTLLNA MVAVGIVVGA GAAAKLVTLD SVRRCLPAGF LIGVVVVIFT
LQHNLMSAYS LLILLGALGG FFIVPLNALL QERGKASVGA GNAIAVQNLG ENGAMLLMLG
LYSLVVKLGV SVIAIGIGFG VLFALAIALL WVWLILAKRR DRSASAE