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Database: UniProt
Entry: Q5WUZ2_LEGPL
LinkDB: Q5WUZ2_LEGPL
Original site: Q5WUZ2_LEGPL 
ID   Q5WUZ2_LEGPL            Unreviewed;       374 AA.
AC   Q5WUZ2;
DT   23-NOV-2004, integrated into UniProtKB/TrEMBL.
DT   23-NOV-2004, sequence version 1.
DT   27-MAR-2024, entry version 91.
DE   RecName: Full=Intermembrane phospholipid transport system permease protein MlaE {ECO:0000256|ARBA:ARBA00020857};
GN   OrderedLocusNames=lpl2025 {ECO:0000313|EMBL:CAH16265.1};
OS   Legionella pneumophila (strain Lens).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=297245 {ECO:0000313|EMBL:CAH16265.1, ECO:0000313|Proteomes:UP000002517};
RN   [1] {ECO:0000313|EMBL:CAH16265.1, ECO:0000313|Proteomes:UP000002517}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lens {ECO:0000313|EMBL:CAH16265.1,
RC   ECO:0000313|Proteomes:UP000002517};
RX   PubMed=15467720; DOI=10.1038/ng1447;
RA   Cazalet C., Rusniok C., Bruggemann H., Zidane N., Magnier A., Ma L.,
RA   Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J.,
RA   Glaser P., Buchrieser C.;
RT   "Evidence in the Legionella pneumophila genome for exploitation of host
RT   cell functions and high genome plasticity.";
RL   Nat. Genet. 36:1165-1173(2004).
CC   -!- FUNCTION: Part of the ABC transporter complex MlaFEDB, which is
CC       involved in a phospholipid transport pathway that maintains lipid
CC       asymmetry in the outer membrane by retrograde trafficking of
CC       phospholipids from the outer membrane to the inner membrane. Probably
CC       responsible for the translocation of the substrate across the membrane.
CC       {ECO:0000256|ARBA:ARBA00002460}.
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins (MlaF),
CC       two transmembrane proteins (MlaE), two cytoplasmic solute-binding
CC       proteins (MlaB) and six periplasmic solute-binding proteins (MlaD).
CC       {ECO:0000256|ARBA:ARBA00011380}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000256|RuleBase:RU362044}; Multi-pass membrane protein
CC       {ECO:0000256|RuleBase:RU362044}.
CC   -!- SIMILARITY: Belongs to the MlaE permease family.
CC       {ECO:0000256|RuleBase:RU362044}.
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DR   EMBL; CR628337; CAH16265.1; -; Genomic_DNA.
DR   RefSeq; WP_011216005.1; NC_006369.1.
DR   AlphaFoldDB; Q5WUZ2; -.
DR   KEGG; lpf:lpl2025; -.
DR   LegioList; lpl2025; -.
DR   HOGENOM; CLU_045686_0_0_6; -.
DR   Proteomes; UP000002517; Chromosome.
DR   GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
DR   InterPro; IPR003453; ABC_MlaE_roteobac.
DR   InterPro; IPR030802; Permease_MalE.
DR   InterPro; IPR036513; STAS_dom_sf.
DR   NCBIfam; TIGR00056; MlaE family lipid ABC transporter permease subunit; 1.
DR   PANTHER; PTHR30188:SF3; ABC TRANSPORTER PERMEASE PROTEIN; 1.
DR   PANTHER; PTHR30188; ABC TRANSPORTER PERMEASE PROTEIN-RELATED; 1.
DR   Pfam; PF02405; MlaE; 1.
DR   SUPFAM; SSF52091; SpoIIaa-like; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane {ECO:0000256|RuleBase:RU362044};
KW   Cell membrane {ECO:0000256|RuleBase:RU362044};
KW   Membrane {ECO:0000256|RuleBase:RU362044};
KW   Transmembrane {ECO:0000256|RuleBase:RU362044};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU362044}.
FT   TRANSMEM        168..187
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362044"
FT   TRANSMEM        199..222
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362044"
FT   TRANSMEM        261..283
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362044"
FT   TRANSMEM        313..334
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362044"
FT   TRANSMEM        354..372
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362044"
SQ   SEQUENCE   374 AA;  41028 MW;  22909E5E938E4488 CRC64;
     MEQASAQIVF EQKNATYQCC GSWSVLTLEG LPKKFITGSL PDSQQITING EKISAFDSAG
     ALALKKCIDE LKKRNNQIEL VNFSDSQQQM LELIESKQEI LSYQLPAVSK EGVLYQIGKE
     SENKLHQVDG LIILIGDLST RLFEAFAYWR RFHLPSIVSV IDSAGLKALP IIGLLSFLIG
     VVLAYQMGLQ LETYGANIFI AYLSGMAIFR EFGPLITAII VAGRTSSSFT AQIGSMKINE
     EVDAILTMGL SPTELLVLPK VLGLLIVFPL LIFWADVFSI WGAMIMSKNM LNIGFEDFLS
     RLRDSVGLNQ MMLGLYKAPA FSILIALVGC FQGFRVESSA DSIGSQTTKS VVQALFLIII
     ADAAFSIAYS WMGL
//
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