MLAB_ECOLI
ID MLAB_ECOLI Reviewed; 97 AA.
AC P64602; P45389; Q2M921;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Intermembrane phospholipid transport system binding protein MlaB {ECO:0000305};
GN Name=mlaB {ECO:0000303|PubMed:19383799}; Synonyms=yrbB;
GN OrderedLocusNames=b3191, JW5535;
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, SUBUNIT, AND MUTAGENESIS OF THR-52.
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 (PubMed:19383799, PubMed:27529189). MlaB plays critical roles in both
CC the assembly and activity of the complex. May act by modulating MlaF
CC structure and stability (PubMed:27529189).
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 -!- SUBCELLULAR LOCATION: Cytoplasm {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 -!- SEQUENCE CAUTION:
CC Sequence=AAA57992.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U18997; AAA57992.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC76223.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE77235.1; -; Genomic_DNA.
DR RefSeq; NP_417658.4; NC_000913.3.
DR RefSeq; WP_000004488.1; NZ_SSZK01000007.1.
DR PDB; 6XGY; X-ray; 2.90 A; B=2-97.
DR PDB; 6XGZ; X-ray; 2.60 A; B/D/F/H=2-97.
DR PDB; 6ZY2; EM; 3.60 A; B/C=1-97.
DR PDB; 6ZY3; EM; 3.30 A; B/C=1-97.
DR PDB; 6ZY4; EM; 4.10 A; B/C=1-97.
DR PDB; 6ZY9; EM; 3.30 A; B/C=1-97.
DR PDB; 7CGE; EM; 2.90 A; C/F=1-97.
DR PDB; 7CGN; EM; 4.30 A; C/F=1-97.
DR PDB; 7CH0; EM; 3.70 A; C/F=1-97.
DR PDB; 7CH6; EM; 3.40 A; E/F=1-97.
DR PDB; 7CH7; EM; 3.90 A; E/F=1-97.
DR PDBsum; 6XGY; -.
DR PDBsum; 6XGZ; -.
DR PDBsum; 6ZY2; -.
DR PDBsum; 6ZY3; -.
DR PDBsum; 6ZY4; -.
DR PDBsum; 6ZY9; -.
DR PDBsum; 7CGE; -.
DR PDBsum; 7CGN; -.
DR PDBsum; 7CH0; -.
DR PDBsum; 7CH6; -.
DR PDBsum; 7CH7; -.
DR AlphaFoldDB; P64602; -.
DR SMR; P64602; -.
DR BioGRID; 4260758; 427.
DR BioGRID; 852263; 2.
DR ComplexPortal; CPX-3464; MlaFEDB lipid transport complex.
DR DIP; DIP-47898N; -.
DR IntAct; P64602; 6.
DR STRING; 511145.b3191; -.
DR ChEMBL; CHEMBL3309025; -.
DR TCDB; 3.A.1.27.3; the atp-binding cassette (abc) superfamily.
DR jPOST; P64602; -.
DR PaxDb; P64602; -.
DR PRIDE; P64602; -.
DR EnsemblBacteria; AAC76223; AAC76223; b3191.
DR EnsemblBacteria; BAE77235; BAE77235; BAE77235.
DR GeneID; 58388204; -.
DR GeneID; 947954; -.
DR KEGG; ecj:JW5535; -.
DR KEGG; eco:b3191; -.
DR PATRIC; fig|1411691.4.peg.3540; -.
DR EchoBASE; EB2649; -.
DR eggNOG; COG3113; Bacteria.
DR HOGENOM; CLU_115403_13_4_6; -.
DR OMA; NPLWDAR; -.
DR PhylomeDB; P64602; -.
DR BioCyc; EcoCyc:G7658-MON; -.
DR PRO; PR:P64602; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; IC:ComplexPortal.
DR GO; GO:1990531; C:phospholipid-translocating ATPase complex; IPI:ComplexPortal.
DR GO; GO:0120014; F:phospholipid transfer activity; IDA:EcoCyc.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:EcoCyc.
DR GO; GO:0120010; P:intermembrane phospholipid transfer; IDA:EcoCyc.
DR GO; GO:0015914; P:phospholipid transport; IC:ComplexPortal.
DR GO; GO:0046677; P:response to antibiotic; IMP:EcoCyc.
DR Gene3D; 3.30.750.24; -; 1.
DR InterPro; IPR002645; STAS_dom.
DR InterPro; IPR036513; STAS_dom_sf.
DR Pfam; PF13466; STAS_2; 1.
DR SUPFAM; SSF52091; SSF52091; 1.
DR PROSITE; PS50801; STAS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Reference proteome; Transport.
FT CHAIN 1..97
FT /note="Intermembrane phospholipid transport system binding
FT protein MlaB"
FT /id="PRO_0000169462"
FT DOMAIN 1..97
FT /note="STAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00198"
FT MUTAGEN 52
FT /note="T->A: Does not affect the assembly of the MlaFEB
FT complex, but abolishes ATPase activity."
FT /evidence="ECO:0000269|PubMed:27529189"
FT STRAND 3..10
FT /evidence="ECO:0007829|PDB:6XGZ"
FT STRAND 13..20
FT /evidence="ECO:0007829|PDB:6XGZ"
FT TURN 22..24
FT /evidence="ECO:0007829|PDB:6XGZ"
FT HELIX 26..30
FT /evidence="ECO:0007829|PDB:6XGZ"
FT HELIX 32..35
FT /evidence="ECO:0007829|PDB:6XGZ"
FT TURN 36..38
FT /evidence="ECO:0007829|PDB:6XGZ"
FT STRAND 41..50
FT /evidence="ECO:0007829|PDB:6XGZ"
FT HELIX 52..67
FT /evidence="ECO:0007829|PDB:6XGZ"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:6XGZ"
FT HELIX 79..87
FT /evidence="ECO:0007829|PDB:6XGZ"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:6XGZ"
SQ SEQUENCE 97 AA; 10680 MW; BB71D8F0A23D0225 CRC64;
MSESLSWMQT GDTLALSGEL DQDVLLPLWE MREEAVKGIT CIDLSRVSRV DTGGLALLLH
LIDLAKKQGN NVTLQGVNDK VYTLAKLYNL PADVLPR
