LPLT_SERP5
ID LPLT_SERP5 Reviewed; 398 AA.
AC A8GII5;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 25-MAY-2022, entry version 73.
DE RecName: Full=Lysophospholipid transporter LplT {ECO:0000255|HAMAP-Rule:MF_01585};
GN Name=lplT {ECO:0000255|HAMAP-Rule:MF_01585}; OrderedLocusNames=Spro_3829;
OS Serratia proteamaculans (strain 568).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=399741;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=568;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Taghavi S., Newman L.,
RA Vangronsveld J., van der Lelie D., Richardson P.;
RT "Complete sequence of chromosome of Serratia proteamaculans 568.";
RL Submitted (SEP-2007) 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; CP000826; ABV42925.1; -; Genomic_DNA.
DR RefSeq; WP_012146532.1; NC_009832.1.
DR AlphaFoldDB; A8GII5; -.
DR STRING; 399741.Spro_3829; -.
DR EnsemblBacteria; ABV42925; ABV42925; Spro_3829.
DR KEGG; spe:Spro_3829; -.
DR eggNOG; COG0477; Bacteria.
DR HOGENOM; CLU_047399_0_0_6; -.
DR OMA; ICFGFNP; -.
DR OrthoDB; 961884at2; -.
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..398
FT /note="Lysophospholipid transporter LplT"
FT /id="PRO_1000069313"
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 163..183
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 253..273
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 344..364
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 398 AA; 41526 MW; 9EAD888B44D2DAD8 CRC64;
MNPTLPTDSP LLSRSMIAVI CAQFLSAFGD NALLFATLAL IKQQLYPDWS QPILQMAFVA
TYIILAPFVG QVADSFAKGR VMMVANGLKL AGALVICFGF NPFLGYTLVG VGAAAYSPAK
YGILGEITSG EKLVKANGLM EASTIAAILI GSVAGGILAD WHIVAALAVC AVVYAAAVIA
NLYIPRLPAA HPAVSWTPRA MTQAFFNACV VLWRDGQTRF SLIGTSLFWG AGVTLRFLLV
LWVPVALGIA DNATPTLLNA MVAVGIVIGA GAAARFVTLE TVRRCMPAGI LIGVAVAIFA
LQTTLFNAYA LLLIIGVLGG FFVVPLNALL QERGKNSVGA GNAIAVQNLG ENTAMLLMLG
LYSLAVKVSV PVVGVGIGFG VVFALAISAL WLSQRRAK