ID Q87PY8_VIBPA Unreviewed; 357 AA.
AC Q87PY8;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE RecName: Full=Intermembrane phospholipid transport system permease protein MlaE {ECO:0000256|ARBA:ARBA00020857};
GN OrderedLocusNames=VP1361 {ECO:0000313|EMBL:BAC59625.1};
OS Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=223926 {ECO:0000313|EMBL:BAC59625.1, ECO:0000313|Proteomes:UP000002493};
RN [1] {ECO:0000313|EMBL:BAC59625.1, ECO:0000313|Proteomes:UP000002493}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIMD 2210633 {ECO:0000313|Proteomes:UP000002493};
RX PubMed=12620739; DOI=10.1016/S0140-6736(03)12659-1;
RA Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT distinct from that of V. cholerae.";
RL Lancet 361:743-749(2003).
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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU362044}.
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DR EMBL; BA000031; BAC59625.1; -; Genomic_DNA.
DR RefSeq; NP_797741.1; NC_004603.1.
DR RefSeq; WP_005454927.1; NC_004603.1.
DR AlphaFoldDB; Q87PY8; -.
DR GeneID; 1188869; -.
DR KEGG; vpa:VP1361; -.
DR PATRIC; fig|223926.6.peg.1301; -.
DR eggNOG; COG0767; Bacteria.
DR HOGENOM; CLU_045686_0_2_6; -.
DR Proteomes; UP000002493; Chromosome 1.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
DR Gene3D; 3.30.750.24; STAS domain; 1.
DR InterPro; IPR003453; ABC_MlaE_roteobac.
DR InterPro; IPR030802; Permease_MalE.
DR InterPro; IPR002645; STAS_dom.
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 Pfam; PF13466; STAS_2; 1.
DR SUPFAM; SSF52091; SpoIIaa-like; 1.
DR PROSITE; PS50801; STAS; 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 Reference proteome {ECO:0000313|Proteomes:UP000002493};
KW Transmembrane {ECO:0000256|RuleBase:RU362044};
KW Transmembrane helix {ECO:0000256|RuleBase:RU362044}.
FT TRANSMEM 156..173
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362044"
FT TRANSMEM 253..278
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362044"
FT TRANSMEM 298..317
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362044"
FT TRANSMEM 329..356
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362044"
FT DOMAIN 1..112
FT /note="STAS"
FT /evidence="ECO:0000259|PROSITE:PS50801"
SQ SEQUENCE 357 AA; 38204 MW; 1C2F4BB07098F17C CRC64;
MDESNLEIEL AESITSAMVG DLWEKANDIL ESYPDSPIVV NASNLTFVDI SGVAFLSDLQ
TRFRPPGAEI SIIGLSASLA ELVPPSNIEN APQIPRGEDG FFERVGNATR EMLVYVGSVV
RFIKECVLVF KLGINRRKNV NWTTVSNIAT RAGADAVPII LLIGFLMGVI IAFEIGLVAQ
QFGAVLFVAD GIGISMFREL GPLMTAIVFA GRTGAAFAAE IGTQKVNEEI NALHTFGICP
VEFLVIPRIY ASVLVLPLLT VLADIIGVLG GALVLLKFDI SFVQYYHQLL NALSVWDLFF
GLIKATTFGF IIAVIGCERG LATGQGSTSV GLAATSAVVS SIIWIVVIDG FFTVLLT
//
