MLAF_ECOLI
ID MLAF_ECOLI Reviewed; 269 AA.
AC P63386; P45393; Q2M917;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Intermembrane phospholipid transport system ATP-binding protein MlaF {ECO:0000305};
DE EC=7.6.2.- {ECO:0000305|PubMed:19383799};
GN Name=mlaF {ECO:0000303|PubMed:19383799}; Synonyms=yrbF;
GN OrderedLocusNames=b3195, JW3162;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [3]
RP FUNCTION IN PHOSPHOLIPID TRANSPORT, SUBUNIT, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MC4100 / JA176;
RX PubMed=19383799; DOI=10.1073/pnas.0903229106;
RA Malinverni J.C., Silhavy T.J.;
RT "An ABC transport system that maintains lipid asymmetry in the gram-
RT negative outer membrane.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:8009-8014(2009).
RN [4]
RP FUNCTION, AND SUBUNIT.
RC STRAIN=K12;
RX PubMed=27529189; DOI=10.7554/elife.19042;
RA Thong S., Ercan B., Torta F., Fong Z.Y., Wong H.Y., Wenk M.R., Chng S.S.;
RT "Defining key roles for auxiliary proteins in an ABC transporter that
RT maintains bacterial outer membrane lipid asymmetry.";
RL Elife 5:E19042-E19042(2016).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBUNIT.
RC STRAIN=K12;
RX PubMed=28388411; DOI=10.1016/j.cell.2017.03.019;
RA Ekiert D.C., Bhabha G., Isom G.L., Greenan G., Ovchinnikov S.,
RA Henderson I.R., Cox J.S., Vale R.D.;
RT "Architectures of lipid transport systems for the bacterial outer
RT membrane.";
RL Cell 169:273-285(2017).
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:0000269|PubMed:19383799, ECO:0000269|PubMed:27529189}.
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:0000269|PubMed:27529189, ECO:0000269|PubMed:28388411,
CC ECO:0000305|PubMed:19383799}.
CC -!- INTERACTION:
CC P63386; P0A6F5: groEL; NbExp=4; IntAct=EBI-561408, EBI-543750;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000305|PubMed:19383799}; Peripheral membrane protein
CC {ECO:0000305|PubMed:19383799}; Cytoplasmic side
CC {ECO:0000305|PubMed:19383799}.
CC -!- DISRUPTION PHENOTYPE: Mutation leads to accumulation of phospholipid in
CC the outer leaflet of the outer membrane and increased outer membrane
CC permeability. It confers sensitivity to SDS-EDTA.
CC {ECO:0000269|PubMed:19383799}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. MlaF family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U18997; AAA57996.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76227.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77239.1; -; Genomic_DNA.
DR PIR; E65110; E65110.
DR RefSeq; NP_417662.1; NC_000913.3.
DR RefSeq; WP_000438245.1; NZ_STEB01000012.1.
DR PDB; 6XGZ; X-ray; 2.60 A; A/C/E/G=1-269.
DR PDB; 7CGE; EM; 2.90 A; B/E=1-269.
DR PDB; 7CGN; EM; 4.30 A; B/E=1-269.
DR PDB; 7CH0; EM; 3.70 A; B/E=1-269.
DR PDB; 7CH6; EM; 3.40 A; C/D=1-269.
DR PDB; 7CH7; EM; 3.90 A; C/D=1-269.
DR PDBsum; 6XGZ; -.
DR PDBsum; 7CGE; -.
DR PDBsum; 7CGN; -.
DR PDBsum; 7CH0; -.
DR PDBsum; 7CH6; -.
DR PDBsum; 7CH7; -.
DR AlphaFoldDB; P63386; -.
DR SMR; P63386; -.
DR BioGRID; 4263401; 121.
DR BioGRID; 852042; 1.
DR ComplexPortal; CPX-3464; MlaFEDB lipid transport complex.
DR DIP; DIP-35865N; -.
DR IntAct; P63386; 9.
DR STRING; 511145.b3195; -.
DR TCDB; 3.A.1.27.3; the atp-binding cassette (abc) superfamily.
DR jPOST; P63386; -.
DR PaxDb; P63386; -.
DR PRIDE; P63386; -.
DR EnsemblBacteria; AAC76227; AAC76227; b3195.
DR EnsemblBacteria; BAE77239; BAE77239; BAE77239.
DR GeneID; 67415971; -.
DR GeneID; 947729; -.
DR KEGG; ecj:JW3162; -.
DR KEGG; eco:b3195; -.
DR PATRIC; fig|1411691.4.peg.3536; -.
DR EchoBASE; EB2653; -.
DR eggNOG; COG1127; Bacteria.
DR HOGENOM; CLU_000604_1_22_6; -.
DR InParanoid; P63386; -.
DR OMA; PKYLFCD; -.
DR PhylomeDB; P63386; -.
DR BioCyc; EcoCyc:YRBF-MON; -.
DR PRO; PR:P63386; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016020; C:membrane; IC:ComplexPortal.
DR GO; GO:1990531; C:phospholipid-translocating ATPase complex; IPI:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; ISM:EcoCyc.
DR GO; GO:0016887; F:ATP hydrolysis activity; IMP:EcoCyc.
DR GO; GO:0120014; F:phospholipid transfer activity; IDA:EcoCyc.
DR GO; GO:0120010; P:intermembrane phospholipid transfer; IDA:EcoCyc.
DR GO; GO:0015914; P:phospholipid transport; IC:ComplexPortal.
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 3D-structure; ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW Nucleotide-binding; Reference proteome; Translocase; Transport.
FT CHAIN 1..269
FT /note="Intermembrane phospholipid transport system ATP-
FT binding protein MlaF"
FT /id="PRO_0000093171"
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"
FT STRAND 6..18
FT /evidence="ECO:0007829|PDB:6XGZ"
FT STRAND 21..32
FT /evidence="ECO:0007829|PDB:6XGZ"
FT STRAND 35..40
FT /evidence="ECO:0007829|PDB:6XGZ"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:7CGE"
FT HELIX 47..54
FT /evidence="ECO:0007829|PDB:6XGZ"
FT STRAND 61..67
FT /evidence="ECO:0007829|PDB:6XGZ"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:6XGZ"
FT HELIX 77..84
FT /evidence="ECO:0007829|PDB:6XGZ"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:6XGZ"
FT TURN 92..95
FT /evidence="ECO:0007829|PDB:7CH6"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:7CGE"
FT HELIX 102..113
FT /evidence="ECO:0007829|PDB:6XGZ"
FT HELIX 118..132
FT /evidence="ECO:0007829|PDB:6XGZ"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:6XGZ"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:7CH6"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:6XGZ"
FT HELIX 147..158
FT /evidence="ECO:0007829|PDB:6XGZ"
FT STRAND 164..170
FT /evidence="ECO:0007829|PDB:6XGZ"
FT TURN 171..174
FT /evidence="ECO:0007829|PDB:6XGZ"
FT HELIX 177..194
FT /evidence="ECO:0007829|PDB:6XGZ"
FT STRAND 197..201
FT /evidence="ECO:0007829|PDB:6XGZ"
FT HELIX 205..209
FT /evidence="ECO:0007829|PDB:6XGZ"
FT STRAND 213..219
FT /evidence="ECO:0007829|PDB:6XGZ"
FT STRAND 222..227
FT /evidence="ECO:0007829|PDB:6XGZ"
FT HELIX 229..233
FT /evidence="ECO:0007829|PDB:6XGZ"
FT HELIX 238..245
FT /evidence="ECO:0007829|PDB:6XGZ"
FT STRAND 246..249
FT /evidence="ECO:0007829|PDB:6XGZ"
FT HELIX 261..265
FT /evidence="ECO:0007829|PDB:6XGZ"
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
