ID   MLAD_HAEIN              Reviewed;         167 AA.
AC   P45029;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Intermembrane phospholipid transport system binding protein MlaD {ECO:0000250|UniProtKB:P64604};
GN   Name=mlaD {ECO:0000250|UniProtKB:P64604}; OrderedLocusNames=HI_1085;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
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; L42023; AAC22741.1; -; Genomic_DNA.
DR   PIR; C64166; C64166.
DR   RefSeq; NP_439242.1; NC_000907.1.
DR   RefSeq; WP_005693409.1; NC_000907.1.
DR   AlphaFoldDB; P45029; -.
DR   SMR; P45029; -.
DR   STRING; 71421.HI_1085; -.
DR   EnsemblBacteria; AAC22741; AAC22741; HI_1085.
DR   KEGG; hin:HI_1085; -.
DR   PATRIC; fig|71421.8.peg.1130; -.
DR   eggNOG; COG1463; Bacteria.
DR   HOGENOM; CLU_107027_0_0_6; -.
DR   OMA; QYQFPKD; -.
DR   PhylomeDB; P45029; -.
DR   BioCyc; HINF71421:G1GJ1-1120-MON; -.
DR   Proteomes; UP000000579; 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:0005543; F:phospholipid binding; IBA:GO_Central.
DR   GO; GO:0005548; F:phospholipid transporter activity; IBA:GO_Central.
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..167
FT                   /note="Intermembrane phospholipid transport system binding
FT                   protein MlaD"
FT                   /id="PRO_0000169464"
FT   TOPO_DOM        1..6
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P64604"
FT   TRANSMEM        7..27
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        28..167
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P64604"
FT   REGION          40..118
FT                   /note="MCE/MlaD"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   167 AA;  18111 MW;  92A10F1B0FA72544 CRC64;
     MRQTIKYEFW VGLFLLLGIG ALVFLGLRVA NVQGFAETKS YTVTATFDNI GGLKVRAPLK
     IGGVVIGRVS AITLDEKSYL PKVSIAINQE YNEIPENSSL SIKTSGLLGE QYIALTMGFD
     DGDTAMLKNG SQIQDTTSAM VLEDLIGQFL YGSKKSDGNE KSESTEQ