ID   MLAF_HAEIN              Reviewed;         264 AA.
AC   P45031;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=Intermembrane phospholipid transport system ATP-binding protein MlaF {ECO:0000250|UniProtKB:P63386};
DE            EC=7.6.2.- {ECO:0000250|UniProtKB:P63386};
GN   Name=mlaF {ECO:0000250|UniProtKB:P63386}; OrderedLocusNames=HI_1087;
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).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=10675023;
RX   DOI=10.1002/(sici)1522-2683(20000101)21:2<411::aid-elps411>3.0.co;2-4;
RA   Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., Gray C.,
RA   Fountoulakis M.;
RT   "Two-dimensional map of the proteome of Haemophilus influenzae.";
RL   Electrophoresis 21:411-429(2000).
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       Responsible for energy coupling to the transport system.
CC       {ECO:0000250|UniProtKB:P63386}.
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:P63386}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000250|UniProtKB:P63386}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P63386}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:P63386}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. MlaF family.
CC       {ECO:0000305}.
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DR   EMBL; L42023; AAC22743.1; -; Genomic_DNA.
DR   PIR; B64182; B64182.
DR   RefSeq; NP_439244.1; NC_000907.1.
DR   RefSeq; WP_005693412.1; NC_000907.1.
DR   AlphaFoldDB; P45031; -.
DR   SMR; P45031; -.
DR   STRING; 71421.HI_1087; -.
DR   EnsemblBacteria; AAC22743; AAC22743; HI_1087.
DR   KEGG; hin:HI_1087; -.
DR   PATRIC; fig|71421.8.peg.1132; -.
DR   eggNOG; COG1127; Bacteria.
DR   HOGENOM; CLU_000604_1_22_6; -.
DR   OMA; PKYLFCD; -.
DR   PhylomeDB; P45031; -.
DR   BioCyc; HINF71421:G1GJ1-1122-MON; -.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR030296; MlaF/Mkl.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR43023:SF6; PTHR43023:SF6; 1.
DR   Pfam; PF00005; ABC_tran; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW   Nucleotide-binding; Reference proteome; Translocase; Transport.
FT   CHAIN           1..264
FT                   /note="Intermembrane phospholipid transport system ATP-
FT                   binding protein MlaF"
FT                   /id="PRO_0000093174"
FT   DOMAIN          6..242
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         38..45
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   264 AA;  29395 MW;  0DB1F7DCE9853C25 CRC64;
     MNQNLIEVKN LTFKRGDRVI YDNLNLQVKK GKITAIMGPS GIGKTTLLKL IGGQLMPEQG
     EILFDGQDIC RLSNRELYEV RKRMGMLFQS GALFTDISTF DNVAFPIREH THLPENLIRQ
     IVLMKLEAVG LRGAAALMPS ELSGGMARRA ALARAIALDP DLIMFDEPFT GQDPISMGVI
     LSLIKRLNEA LNLTSIVVSH DVEEVLSIAD YAYIIADQKV IAEGTSEQLL QSQDLRVVQF
     LKGESDGPVR FKYPAQDYVK ELFE