LPLT_KLEP7
ID LPLT_KLEP7 Reviewed; 397 AA.
AC A6TDH1;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=Lysophospholipid transporter LplT {ECO:0000255|HAMAP-Rule:MF_01585};
GN Name=lplT {ECO:0000255|HAMAP-Rule:MF_01585};
GN OrderedLocusNames=KPN78578_31810; ORFNames=KPN_03244;
OS Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=272620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700721 / MGH 78578;
RG The Klebsiella pneumonia Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P.,
RA Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.;
RL Submitted (SEP-2006) 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; CP000647; ABR78642.1; -; Genomic_DNA.
DR RefSeq; WP_002915976.1; NC_009648.1.
DR AlphaFoldDB; A6TDH1; -.
DR SMR; A6TDH1; -.
DR STRING; 272620.KPN_03244; -.
DR EnsemblBacteria; ABR78642; ABR78642; KPN_03244.
DR KEGG; kpn:KPN_03244; -.
DR HOGENOM; CLU_047399_0_0_6; -.
DR OMA; ICFGFNP; -.
DR Proteomes; UP000000265; 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 Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..397
FT /note="Lysophospholipid transporter LplT"
FT /id="PRO_1000069312"
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 281..301
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01585"
FT TRANSMEM 305..325
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 397 AA; 41698 MW; F7F7B4F83036ED85 CRC64;
MSESVHTNPS LYSKGMLAVI CAQFLSAFGD NALLFATLAL MKQLYYPEWS QPVLQMLFVG
AYILFAPFVG QFADSFAKGR VMMVANGLKL LGAGCICFGV NPFIGYTLVG IGAAAYSPAK
YGILGELTTG DKLVKANGLM ESSTIAAILL GSMAGGILAD WHVLAALIVC ALVYGGAVVA
NLWIPRLPAA RPGQSWRFKP MTHSFFSACR TLWRNGETRF SLMGTSLFWG AGVTLRFLLV
IWVPVALGIT SNAMPTYLNA MVAVGIVLGA GAAAKLVTLE TVSRCMPAGI LIGIAVIAFA
VQQSLLPAFG LLLLLGVFGG FFIVPLNALL QERGKHSVGA GNAIAVQNLG ENVAMLLMLG
LYSLAVSVGV PPVAVGIGFG AVFAVAIAAL WVWGRRK