MLAF_ECOL6
ID MLAF_ECOL6 Reviewed; 269 AA.
AC P63387; P45393;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=c3955;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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; AE014075; AAN82395.1; -; Genomic_DNA.
DR RefSeq; WP_000438245.1; NC_004431.1.
DR AlphaFoldDB; P63387; -.
DR SMR; P63387; -.
DR STRING; 199310.c3955; -.
DR EnsemblBacteria; AAN82395; AAN82395; c3955.
DR GeneID; 67415971; -.
DR KEGG; ecc:c3955; -.
DR eggNOG; COG1127; Bacteria.
DR HOGENOM; CLU_000604_1_22_6; -.
DR OMA; PKYLFCD; -.
DR BioCyc; ECOL199310:C3955-MON; -.
DR Proteomes; UP000001410; 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 3: Inferred from homology;
KW ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW Nucleotide-binding; Translocase; Transport.
FT CHAIN 1..269
FT /note="Intermembrane phospholipid transport system ATP-
FT binding protein MlaF"
FT /id="PRO_0000093172"
FT DOMAIN 9..245
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 41..48
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 269 AA; 29097 MW; 742EF8DEDA742CF2 CRC64;
MEQSVANLVD MRDVSFTRGN RCIFDNISLT VPRGKITAIM GPSGIGKTTL LRLIGGQIAP
DHGEILFDGE NIPAMSRSRL YTVRKRMSML FQSGALFTDM NVFDNVAYPL REHTQLPAPL
LHSTVMMKLE AVGLRGAAKL MPSELSGGMA RRAALARAIA LEPDLIMFDE PFVGQDPITM
GVLVKLISEL NSALGVTCVV VSHDVPEVLS IADHAWILAD KKIVAHGSAQ ALQANPDPRV
RQFLDGIADG PVPFRYPAGD YHADLLPGS