MLAD_ECOLI
ID MLAD_ECOLI Reviewed; 183 AA.
AC P64604; P45391; Q2M919;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Intermembrane phospholipid transport system binding protein MlaD {ECO:0000305};
GN Name=mlaD {ECO:0000303|PubMed:19383799}; Synonyms=yrbD;
GN OrderedLocusNames=b3193, JW3160;
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 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 [4]
RP FUNCTION, SUBUNIT, PHOSPHOLIPID-BINDING, AND DOMAIN.
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 [5]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 32-183, SUBUNIT, INTERACTION WITH
RP MLAC, AND DOMAIN.
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
CC (PubMed:19383799, PubMed:27529189). MlaD functions in substrate binding
CC with strong affinity for phospholipids and modulates ATP hydrolytic
CC activity of the complex (PubMed:27529189).
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 (PubMed:27529189, PubMed:28388411). Interacts with MlaC
CC (PubMed:28388411). {ECO:0000269|PubMed:27529189,
CC ECO:0000269|PubMed:28388411, ECO:0000305|PubMed:19383799}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000305|PubMed:19383799}; Single-pass type II membrane protein
CC {ECO:0000305|PubMed:19383799}; Periplasmic side
CC {ECO:0000305|PubMed:19383799}.
CC -!- DOMAIN: Forms hexameric rings with a central hydrophobic pore via its
CC periplasmic domain, which also binds phospholipids. Contains at least
CC four binding sites. {ECO:0000269|PubMed:27529189,
CC ECO:0000269|PubMed:28388411}.
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 MlaD family. {ECO:0000305}.
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DR EMBL; U18997; AAA57994.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76225.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77237.1; -; Genomic_DNA.
DR PIR; C65110; C65110.
DR RefSeq; NP_417660.1; NC_000913.3.
DR RefSeq; WP_001296448.1; NZ_STEB01000012.1.
DR PDB; 5UW2; X-ray; 2.85 A; A/B/C=32-183.
DR PDB; 5UW8; X-ray; 2.15 A; A/B/C/D/E/F/G=32-140.
DR PDB; 6ZY9; EM; 3.30 A; A/D/I/J/K/L=1-183.
DR PDB; 7CGE; EM; 2.90 A; G/H/I/J/K/L=1-183.
DR PDB; 7CGN; EM; 4.30 A; G/H/I/J/K/L=1-183.
DR PDB; 7CH0; EM; 3.70 A; G/H/I/J/K/L=1-183.
DR PDBsum; 5UW2; -.
DR PDBsum; 5UW8; -.
DR PDBsum; 6ZY9; -.
DR PDBsum; 7CGE; -.
DR PDBsum; 7CGN; -.
DR PDBsum; 7CH0; -.
DR AlphaFoldDB; P64604; -.
DR SMR; P64604; -.
DR BioGRID; 4262424; 31.
DR ComplexPortal; CPX-3464; MlaFEDB lipid transport complex.
DR DIP; DIP-12906N; -.
DR IntAct; P64604; 3.
DR MINT; P64604; -.
DR STRING; 511145.b3193; -.
DR TCDB; 3.A.1.27.3; the atp-binding cassette (abc) superfamily.
DR jPOST; P64604; -.
DR PaxDb; P64604; -.
DR PRIDE; P64604; -.
DR EnsemblBacteria; AAC76225; AAC76225; b3193.
DR EnsemblBacteria; BAE77237; BAE77237; BAE77237.
DR GeneID; 66672905; -.
DR GeneID; 947712; -.
DR KEGG; ecj:JW3160; -.
DR KEGG; eco:b3193; -.
DR PATRIC; fig|1411691.4.peg.3538; -.
DR EchoBASE; EB2651; -.
DR eggNOG; COG1463; Bacteria.
DR HOGENOM; CLU_107027_0_0_6; -.
DR InParanoid; P64604; -.
DR OMA; QYQFPKD; -.
DR PhylomeDB; P64604; -.
DR BioCyc; EcoCyc:EG12799-MON; -.
DR PRO; PR:P64604; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
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:0005543; F:phospholipid binding; 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; IC:ComplexPortal.
DR InterPro; IPR030970; ABC_MlaD.
DR InterPro; IPR003399; Mce/MlaD.
DR Pfam; PF02470; MlaD; 1.
DR TIGRFAMs; TIGR04430; OM_asym_MlaD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Membrane;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..183
FT /note="Intermembrane phospholipid transport system binding
FT protein MlaD"
FT /id="PRO_0000013918"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:19383799"
FT TRANSMEM 8..28
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..183
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:19383799"
FT REGION 39..116
FT /note="MCE/MlaD"
FT /evidence="ECO:0000305"
FT REGION 155..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 5..26
FT /evidence="ECO:0007829|PDB:7CGE"
FT TURN 27..29
FT /evidence="ECO:0007829|PDB:7CGE"
FT STRAND 39..43
FT /evidence="ECO:0007829|PDB:7CGE"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:7CGE"
FT STRAND 63..68
FT /evidence="ECO:0007829|PDB:7CGE"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:6ZY9"
FT TURN 75..77
FT /evidence="ECO:0007829|PDB:7CGE"
FT STRAND 83..87
FT /evidence="ECO:0007829|PDB:7CGE"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:7CGE"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:7CGE"
FT HELIX 144..151
FT /evidence="ECO:0007829|PDB:7CGE"
SQ SEQUENCE 183 AA; 19576 MW; 6BD8B922002EFD28 CRC64;
MQTKKNEIWV GIFLLAALLA ALFVCLKAAN VTSIRTEPTY TLYATFDNIG GLKARSPVSI
GGVVVGRVAD ITLDPKTYLP RVTLEIEQRY NHIPDTSSLS IRTSGLLGEQ YLALNVGFED
PELGTAILKD GDTIQDTKSA MVLEDLIGQF LYGSKGDDNK NSGDAPAAAP GNNETTEPVG
TTK
