MLAE_ECOLI
ID MLAE_ECOLI Reviewed; 260 AA.
AC P64606; P45392; Q2M918;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Intermembrane phospholipid transport system permease protein MlaE {ECO:0000305};
GN Name=mlaE {ECO:0000303|PubMed:19383799}; Synonyms=yrbE;
GN OrderedLocusNames=b3194, JW3161;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [3]
RP TOPOLOGY [LARGE SCALE ANALYSIS], AND SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [4]
RP FUNCTION IN PHOSPHOLIPID TRANSPORT, SUBUNIT, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MC4100 / JA176;
RX PubMed=19383799; DOI=10.1073/pnas.0903229106;
RA Malinverni J.C., Silhavy T.J.;
RT "An ABC transport system that maintains lipid asymmetry in the gram-
RT negative outer membrane.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:8009-8014(2009).
RN [5]
RP FUNCTION, AND SUBUNIT.
RC STRAIN=K12;
RX PubMed=27529189; DOI=10.7554/elife.19042;
RA Thong S., Ercan B., Torta F., Fong Z.Y., Wong H.Y., Wenk M.R., Chng S.S.;
RT "Defining key roles for auxiliary proteins in an ABC transporter that
RT maintains bacterial outer membrane lipid asymmetry.";
RL Elife 5:E19042-E19042(2016).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBUNIT.
RC STRAIN=K12;
RX PubMed=28388411; DOI=10.1016/j.cell.2017.03.019;
RA Ekiert D.C., Bhabha G., Isom G.L., Greenan G., Ovchinnikov S.,
RA Henderson I.R., Cox J.S., Vale R.D.;
RT "Architectures of lipid transport systems for the bacterial outer
RT membrane.";
RL Cell 169:273-285(2017).
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:0000269|PubMed:19383799, ECO:0000269|PubMed:27529189}.
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:0000269|PubMed:27529189, ECO:0000269|PubMed:28388411,
CC ECO:0000305|PubMed:19383799}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996,
CC ECO:0000305|PubMed:19383799}; Multi-pass membrane protein {ECO:0000255,
CC ECO:0000305|PubMed:19383799}.
CC -!- DISRUPTION PHENOTYPE: Mutation leads to accumulation of phospholipid in
CC the outer leaflet of the outer membrane and increased outer membrane
CC permeability. It confers sensitivity to SDS-EDTA.
CC {ECO:0000269|PubMed:19383799}.
CC -!- SIMILARITY: Belongs to the MlaE permease family. {ECO:0000305}.
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DR EMBL; U18997; AAA57995.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76226.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77238.1; -; Genomic_DNA.
DR PIR; D65110; D65110.
DR RefSeq; NP_417661.1; NC_000913.3.
DR RefSeq; WP_000925795.1; NZ_STEB01000012.1.
DR PDB; 7CGE; EM; 2.90 A; A/D=1-260.
DR PDB; 7CGN; EM; 4.30 A; A/D=1-260.
DR PDB; 7CH0; EM; 3.70 A; A/D=1-260.
DR PDB; 7CH6; EM; 3.40 A; A/B=1-260.
DR PDB; 7CH7; EM; 3.90 A; A/B=1-260.
DR PDBsum; 7CGE; -.
DR PDBsum; 7CGN; -.
DR PDBsum; 7CH0; -.
DR PDBsum; 7CH6; -.
DR PDBsum; 7CH7; -.
DR AlphaFoldDB; P64606; -.
DR SMR; P64606; -.
DR BioGRID; 4263406; 34.
DR ComplexPortal; CPX-3464; MlaFEDB lipid transport complex.
DR IntAct; P64606; 1.
DR STRING; 511145.b3194; -.
DR TCDB; 3.A.1.27.3; the atp-binding cassette (abc) superfamily.
DR jPOST; P64606; -.
DR PaxDb; P64606; -.
DR PRIDE; P64606; -.
DR EnsemblBacteria; AAC76226; AAC76226; b3194.
DR EnsemblBacteria; BAE77238; BAE77238; BAE77238.
DR GeneID; 66672904; -.
DR GeneID; 947732; -.
DR KEGG; ecj:JW3161; -.
DR KEGG; eco:b3194; -.
DR PATRIC; fig|1411691.4.peg.3537; -.
DR EchoBASE; EB2652; -.
DR eggNOG; COG0767; Bacteria.
DR HOGENOM; CLU_045686_1_1_6; -.
DR InParanoid; P64606; -.
DR OMA; NYLVFPK; -.
DR PhylomeDB; P64606; -.
DR BioCyc; EcoCyc:YRBE-MON; -.
DR PRO; PR:P64606; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; IC:ComplexPortal.
DR GO; GO:1990531; C:phospholipid-translocating ATPase complex; IPI:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0120014; F:phospholipid transfer activity; IDA:EcoCyc.
DR GO; GO:0005548; F:phospholipid transporter activity; IBA:GO_Central.
DR GO; GO:0120010; P:intermembrane phospholipid transfer; IDA:EcoCyc.
DR GO; GO:0015914; P:phospholipid transport; IBA:GO_Central.
DR InterPro; IPR003453; ABC_MlaE_Proteobac.
DR InterPro; IPR030802; Permease_MalE.
DR PANTHER; PTHR30188; PTHR30188; 1.
DR Pfam; PF02405; MlaE; 1.
DR TIGRFAMs; TIGR00056; TIGR00056; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..260
FT /note="Intermembrane phospholipid transport system permease
FT protein MlaE"
FT /id="PRO_0000169465"
FT TOPO_DOM 1..50
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:15919996"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 72..88
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:15919996"
FT TRANSMEM 89..109
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 110..147
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:15919996"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 169..198
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:15919996"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 220..238
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:15919996"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 260
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
FT HELIX 6..31
FT /evidence="ECO:0007829|PDB:7CGE"
FT TURN 37..39
FT /evidence="ECO:0007829|PDB:7CGE"
FT HELIX 41..50
FT /evidence="ECO:0007829|PDB:7CGE"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:7CGE"
FT HELIX 56..78
FT /evidence="ECO:0007829|PDB:7CGE"
FT TURN 79..82
FT /evidence="ECO:0007829|PDB:7CGE"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:7CGE"
FT HELIX 87..96
FT /evidence="ECO:0007829|PDB:7CGE"
FT TURN 97..99
FT /evidence="ECO:0007829|PDB:7CGE"
FT HELIX 100..125
FT /evidence="ECO:0007829|PDB:7CGE"
FT HELIX 128..133
FT /evidence="ECO:0007829|PDB:7CGE"
FT TURN 134..136
FT /evidence="ECO:0007829|PDB:7CGE"
FT HELIX 139..142
FT /evidence="ECO:0007829|PDB:7CGE"
FT HELIX 144..174
FT /evidence="ECO:0007829|PDB:7CGE"
FT TURN 175..178
FT /evidence="ECO:0007829|PDB:7CGE"
FT HELIX 182..190
FT /evidence="ECO:0007829|PDB:7CGE"
FT TURN 195..198
FT /evidence="ECO:0007829|PDB:7CGE"
FT HELIX 199..222
FT /evidence="ECO:0007829|PDB:7CGE"
FT HELIX 228..257
FT /evidence="ECO:0007829|PDB:7CGE"
SQ SEQUENCE 260 AA; 27863 MW; 057409EA1E6E25EB CRC64;
MLLNALASLG HKGIKTLRTF GRAGLMLFNA LVGKPEFRKH APLLVRQLYN VGVLSMLIIV
VSGVFIGMVL GLQGYLVLTT YSAETSLGML VALSLLRELG PVVAALLFAG RAGSALTAEI
GLMRATEQLS SMEMMAVDPL RRVISPRFWA GVISLPLLTV IFVAVGIWGG SLVGVSWKGI
DSGFFWSAMQ NAVDWRMDLV NCLIKSVVFA ITVTWISLFN GYDAIPTSAG ISRATTRTVV
HSSLAVLGLD FVLTALMFGN
