ID   MLAB_SHIFL              Reviewed;          97 AA.
AC   P64603; P45389;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=Intermembrane phospholipid transport system binding protein MlaB {ECO:0000250|UniProtKB:P64602};
GN   Name=mlaB {ECO:0000250|UniProtKB:P64602}; OrderedLocusNames=SF3231, S3449;
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. MlaB plays
CC       critical roles in both the assembly and activity of the complex. May
CC       act by modulating MlaF structure and stability.
CC       {ECO:0000250|UniProtKB:P64602}.
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:P64602}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P64602}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN44697.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAP18511.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE005674; AAN44697.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AE014073; AAP18511.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_000004488.1; NZ_WPGW01000004.1.
DR   AlphaFoldDB; P64603; -.
DR   SMR; P64603; -.
DR   STRING; 198214.SF3231; -.
DR   EnsemblBacteria; AAN44697; AAN44697; SF3231.
DR   EnsemblBacteria; AAP18511; AAP18511; S3449.
DR   GeneID; 58388204; -.
DR   KEGG; sfx:S3449; -.
DR   PATRIC; fig|623.156.peg.1709; -.
DR   HOGENOM; CLU_115403_13_4_6; -.
DR   OrthoDB; 1864829at2; -.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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   3: Inferred from homology;
KW   Cytoplasm; Reference proteome; Transport.
FT   CHAIN           1..97
FT                   /note="Intermembrane phospholipid transport system binding
FT                   protein MlaB"
FT                   /id="PRO_0000169463"
FT   DOMAIN          1..97
FT                   /note="STAS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00198"
SQ   SEQUENCE   97 AA;  10680 MW;  BB71D8F0A23D0225 CRC64;
     MSESLSWMQT GDTLALSGEL DQDVLLPLWE MREEAVKGIT CIDLSRVSRV DTGGLALLLH
     LIDLAKKQGN NVTLQGVNDK VYTLAKLYNL PADVLPR