MLAE_SHIFL
ID MLAE_SHIFL Reviewed; 260 AA.
AC P64609; P45392;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=Intermembrane phospholipid transport system permease protein MlaE {ECO:0000250|UniProtKB:P64606};
GN Name=mlaE {ECO:0000250|UniProtKB:P64606}; OrderedLocusNames=SF3234, S3452;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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. Probably
CC responsible for the translocation of the substrate across the membrane.
CC {ECO:0000250|UniProtKB:P64606}.
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:P64606}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:P64606}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the MlaE permease family. {ECO:0000305}.
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DR EMBL; AE005674; AAN44700.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP18514.1; -; Genomic_DNA.
DR RefSeq; NP_708993.1; NC_004337.2.
DR RefSeq; WP_000925795.1; NZ_WPGW01000004.1.
DR AlphaFoldDB; P64609; -.
DR SMR; P64609; -.
DR STRING; 198214.SF3234; -.
DR EnsemblBacteria; AAN44700; AAN44700; SF3234.
DR EnsemblBacteria; AAP18514; AAP18514; S3452.
DR GeneID; 1027117; -.
DR GeneID; 66672904; -.
DR KEGG; sfl:SF3234; -.
DR KEGG; sfx:S3452; -.
DR PATRIC; fig|198214.7.peg.3835; -.
DR HOGENOM; CLU_045686_1_1_6; -.
DR OMA; NYLVFPK; -.
DR OrthoDB; 1253502at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; Chromosome.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
DR InterPro; IPR003453; ABC_MlaE_Proteobac.
DR InterPro; IPR030802; Permease_MalE.
DR PANTHER; PTHR30188; PTHR30188; 1.
DR Pfam; PF02405; MlaE; 1.
DR TIGRFAMs; TIGR00056; TIGR00056; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..260
FT /note="Intermembrane phospholipid transport system permease
FT protein MlaE"
FT /id="PRO_0000169468"
FT TOPO_DOM 1..50
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P64606"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 72..88
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P64606"
FT TRANSMEM 89..109
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 110..147
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P64606"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 169..198
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P64606"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 220..238
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P64606"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 260
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P64606"
SQ SEQUENCE 260 AA; 27863 MW; 057409EA1E6E25EB CRC64;
MLLNALASLG HKGIKTLRTF GRAGLMLFNA LVGKPEFRKH APLLVRQLYN VGVLSMLIIV
VSGVFIGMVL GLQGYLVLTT YSAETSLGML VALSLLRELG PVVAALLFAG RAGSALTAEI
GLMRATEQLS SMEMMAVDPL RRVISPRFWA GVISLPLLTV IFVAVGIWGG SLVGVSWKGI
DSGFFWSAMQ NAVDWRMDLV NCLIKSVVFA ITVTWISLFN GYDAIPTSAG ISRATTRTVV
HSSLAVLGLD FVLTALMFGN
