ID   MLAD_ECO57              Reviewed;         183 AA.
AC   P64605; P45391;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Intermembrane phospholipid transport system binding protein MlaD {ECO:0000250|UniProtKB:P64604};
GN   Name=mlaD {ECO:0000250|UniProtKB:P64604}; OrderedLocusNames=Z4556, ECs4072;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
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. MlaD
CC       functions in substrate binding with strong affinity for phospholipids
CC       and modulates ATP hydrolytic activity of the complex.
CC       {ECO:0000250|UniProtKB:P64604}.
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:0000250|UniProtKB:P64604}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000250|UniProtKB:P64604}; Single-pass type II membrane protein
CC       {ECO:0000250|UniProtKB:P64604}; Periplasmic side
CC       {ECO:0000250|UniProtKB:P64604}.
CC   -!- SIMILARITY: Belongs to the MlaD family. {ECO:0000305}.
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DR   EMBL; AE005174; AAG58327.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB37495.1; -; Genomic_DNA.
DR   PIR; C85983; C85983.
DR   PIR; H91137; H91137.
DR   RefSeq; NP_312099.1; NC_002695.1.
DR   RefSeq; WP_001296448.1; NZ_SWKA01000005.1.
DR   AlphaFoldDB; P64605; -.
DR   SMR; P64605; -.
DR   STRING; 155864.EDL933_4421; -.
DR   EnsemblBacteria; AAG58327; AAG58327; Z4556.
DR   EnsemblBacteria; BAB37495; BAB37495; ECs_4072.
DR   GeneID; 66672905; -.
DR   GeneID; 916081; -.
DR   KEGG; ece:Z4556; -.
DR   KEGG; ecs:ECs_4072; -.
DR   PATRIC; fig|386585.9.peg.4251; -.
DR   eggNOG; COG1463; Bacteria.
DR   HOGENOM; CLU_107027_0_0_6; -.
DR   OMA; QYQFPKD; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
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:0015914; P:phospholipid transport; IEA:InterPro.
DR   InterPro; IPR030970; ABC_MlaD.
DR   InterPro; IPR003399; Mce/MlaD.
DR   Pfam; PF02470; MlaD; 1.
DR   TIGRFAMs; TIGR04430; OM_asym_MlaD; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW   Signal-anchor; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..183
FT                   /note="Intermembrane phospholipid transport system binding
FT                   protein MlaD"
FT                   /id="PRO_0000013919"
FT   TOPO_DOM        1..7
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P64604"
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:0000250|UniProtKB:P64604"
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"
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