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 27-MAR-2024, entry version 135.
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; Pseudomonadota; 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 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 OrthoDB; 9802264at2; -.
DR PhylomeDB; P45031; -.
DR BioCyc; HINF71421:G1GJ1-1122-MONOMER; -.
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 GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR CDD; cd03261; ABC_Org_Solvent_Resistant; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR43023; PROTEIN TRIGALACTOSYLDIACYLGLYCEROL 3, CHLOROPLASTIC; 1.
DR PANTHER; PTHR43023:SF3; PROTEIN TRIGALACTOSYLDIACYLGLYCEROL 3, CHLOROPLASTIC; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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
//
