SCTG_SHIFL
ID SCTG_SHIFL Reviewed; 142 AA.
AC P0A1X2; Q06083; Q9AFS1;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=Type 3 secretion system pilotin {ECO:0000305};
DE AltName: Full=Lipoprotein MxiM;
DE AltName: Full=MxiD pilot {ECO:0000303|PubMed:11717255};
DE AltName: Full=Secretin pilot protein {ECO:0000303|PubMed:15775974};
DE Flags: Precursor;
GN Name=mxiM {ECO:0000303|PubMed:1332940}; Synonyms=sctG {ECO:0000305};
GN OrderedLocusNames=CP0143;
OS Shigella flexneri.
OG Plasmid pWR100, Plasmid pINV_F6_M1382, and Plasmid pCP301.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBCELLULAR LOCATION.
RC STRAIN=M90T / Serotype 5a; PLASMID=pWR100;
RX PubMed=1332940; DOI=10.1128/jb.174.23.7661-7669.1992;
RA Allaoui A., Sansonetti P.J., Parsot C.;
RT "MxiJ, a lipoprotein involved in secretion of Shigella Ipa invasins, is
RT homologous to YscJ, a secretion factor of the Yersinia Yop proteins.";
RL J. Bacteriol. 174:7661-7669(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=M90T / Serotype 5a; PLASMID=pWR100;
RX PubMed=11115111; DOI=10.1046/j.1365-2958.2000.02179.x;
RA Buchrieser C., Glaser P., Rusniok C., Nedjari H., d'Hauteville H.,
RA Kunst F., Sansonetti P.J., Parsot C.;
RT "The virulence plasmid pWR100 and the repertoire of proteins secreted by
RT the type III secretion apparatus of Shigella flexneri.";
RL Mol. Microbiol. 38:760-771(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=M90T / Serotype 5a; PLASMID=pWR100;
RX PubMed=11292750; DOI=10.1128/iai.69.5.3271-3285.2001;
RA Venkatesan M.M., Goldberg M.B., Rose D.J., Grotbeck E.J., Burland V.,
RA Blattner F.R.;
RT "Complete DNA sequence and analysis of the large virulence plasmid of
RT Shigella flexneri.";
RL Infect. Immun. 69:3271-3285(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=M1382 / Serotype 6; PLASMID=pINV_F6_M1382;
RX PubMed=14573649; DOI=10.1128/iai.71.11.6298-6306.2003;
RA Lan R., Stevenson G., Reeves P.R.;
RT "Comparison of two major forms of the Shigella virulence plasmid pINV:
RT positive selection is a major force driving the divergence.";
RL Infect. Immun. 71:6298-6306(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a; PLASMID=pCP301;
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 [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=10085046; DOI=10.1128/iai.67.4.1982-1991.1999;
RA Schuch R., Maurelli A.T.;
RT "The mxi-Spa type III secretory pathway of Shigella flexneri requires an
RT outer membrane lipoprotein, MxiM, for invasin translocation.";
RL Infect. Immun. 67:1982-1991(1999).
RN [7]
RP FUNCTION, AND INTERACTION WITH MXID/SCTC.
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=11717255; DOI=10.1128/jb.183.24.6991-6998.2001;
RA Schuch R., Maurelli A.T.;
RT "MxiM and MxiJ, base elements of the Mxi-Spa type III secretion system of
RT Shigella, interact with and stabilize the MxiD secretin in the cell
RT envelope.";
RL J. Bacteriol. 183:6991-6998(2001).
RN [8] {ECO:0007744|PDB:1Y9L, ECO:0007744|PDB:1Y9T}
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 28-142, FUNCTION, SUBUNIT, AND
RP INTERACTION WITH MXID/SCTC.
RX PubMed=15775974; DOI=10.1038/sj.emboj.7600610;
RA Lario P.I., Pfuetzner R.A., Frey E.A., Creagh L., Haynes C., Maurelli A.T.,
RA Strynadka N.C.;
RT "Structure and biochemical analysis of a secretin pilot protein.";
RL EMBO J. 24:1111-1121(2005).
RN [9] {ECO:0007744|PDB:2JW1}
RP STRUCTURE BY NMR OF 28-142 IN COMPLEX WITH MXID/SCTC, AND SUBUNIT.
RX PubMed=18940609; DOI=10.1016/j.str.2008.08.006;
RA Okon M., Moraes T.F., Lario P.I., Creagh A.L., Haynes C.A., Strynadka N.C.,
RA McIntosh L.P.;
RT "Structural characterization of the type-III pilot-secretin complex from
RT Shigella flexneri.";
RL Structure 16:1544-1554(2008).
CC -!- FUNCTION: Involved in the synthesis of the type III secretion system
CC (T3SS), also called injectisome, which is used to inject bacterial
CC effector proteins into eukaryotic host cells (PubMed:10085046,
CC PubMed:11717255). Pilot protein that is required for the proper
CC localization of the secretin MxiD/SctC in the outer membrane
CC (PubMed:11717255). Also influences both MxiD/SctC multimerization and
CC stability (PubMed:11717255). Required for both Ipa translocation and
CC tissue culture cell invasion (PubMed:10085046). Binds lipids
CC (PubMed:15775974). {ECO:0000269|PubMed:10085046,
CC ECO:0000269|PubMed:11717255, ECO:0000269|PubMed:15775974}.
CC -!- SUBUNIT: Monomer (PubMed:15775974). Interacts with the secretin
CC MxiD/SctC (PubMed:11717255, PubMed:15775974, PubMed:18940609).
CC {ECO:0000269|PubMed:11717255, ECO:0000269|PubMed:15775974,
CC ECO:0000269|PubMed:18940609}.
CC -!- INTERACTION:
CC P0A1X2; Q04641: sctC; NbExp=3; IntAct=EBI-15735345, EBI-15735324;
CC -!- SUBCELLULAR LOCATION: Cell outer membrane
CC {ECO:0000269|PubMed:10085046}; Lipid-anchor
CC {ECO:0000269|PubMed:10085046, ECO:0000269|PubMed:1332940}; Periplasmic
CC side {ECO:0000269|PubMed:10085046}.
CC -!- DISRUPTION PHENOTYPE: Inactivation of the gene blocks the Ipa invasin
CC secretory pathway and severely attenuates virulence.
CC {ECO:0000269|PubMed:10085046}.
CC -!- SIMILARITY: Belongs to the MxiM family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK18462.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M98391; AAA26534.1; -; Genomic_DNA.
DR EMBL; AL391753; CAC05818.1; -; Genomic_DNA.
DR EMBL; AF348706; AAK18462.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY206439; AAP79006.1; -; Genomic_DNA.
DR EMBL; AF386526; AAL72325.2; -; Genomic_DNA.
DR PIR; E45271; E45271.
DR RefSeq; NP_858276.2; NC_004851.1.
DR RefSeq; WP_001346200.1; NZ_WPGS01000043.1.
DR RefSeq; YP_009062500.1; NC_024996.1.
DR PDB; 1Y9L; X-ray; 1.50 A; A=28-142.
DR PDB; 1Y9T; X-ray; 1.87 A; A=28-142.
DR PDB; 2JW1; NMR; -; A=28-142.
DR PDBsum; 1Y9L; -.
DR PDBsum; 1Y9T; -.
DR PDBsum; 2JW1; -.
DR AlphaFoldDB; P0A1X2; -.
DR BMRB; P0A1X2; -.
DR SMR; P0A1X2; -.
DR DIP; DIP-46243N; -.
DR IntAct; P0A1X2; 1.
DR STRING; 198214.CP0143; -.
DR DrugBank; DB04199; 1-Monohexanoyl-2-Hydroxy-Sn-Glycero-3-Phosphate.
DR EnsemblBacteria; AAL72325; AAL72325; SF_p0143.
DR GeneID; 1238028; -.
DR KEGG; sfl:CP0143; -.
DR PATRIC; fig|623.157.peg.5377; -.
DR HOGENOM; CLU_1814512_0_0_6; -.
DR OMA; GERQMIR; -.
DR EvolutionaryTrace; P0A1X2; -.
DR Proteomes; UP000001006; Plasmid pCP301.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR Gene3D; 2.40.128.230; -; 1.
DR InterPro; IPR021546; MxiM.
DR InterPro; IPR038517; MxiM_sf.
DR Pfam; PF11441; MxiM; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Lipoprotein; Membrane; Palmitate;
KW Plasmid; Reference proteome; Signal; Virulence.
FT SIGNAL 1..23
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 24..142
FT /note="Type 3 secretion system pilotin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT /id="PRO_0000018225"
FT LIPID 24
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 24
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT STRAND 34..40
FT /evidence="ECO:0007829|PDB:1Y9L"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:1Y9L"
FT STRAND 53..56
FT /evidence="ECO:0007829|PDB:1Y9L"
FT TURN 58..60
FT /evidence="ECO:0007829|PDB:1Y9L"
FT STRAND 63..66
FT /evidence="ECO:0007829|PDB:1Y9L"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:1Y9L"
FT STRAND 75..79
FT /evidence="ECO:0007829|PDB:1Y9L"
FT STRAND 82..86
FT /evidence="ECO:0007829|PDB:1Y9L"
FT HELIX 98..113
FT /evidence="ECO:0007829|PDB:1Y9L"
FT STRAND 115..118
FT /evidence="ECO:0007829|PDB:1Y9L"
FT STRAND 121..124
FT /evidence="ECO:0007829|PDB:1Y9L"
FT STRAND 126..130
FT /evidence="ECO:0007829|PDB:1Y9L"
FT STRAND 133..140
FT /evidence="ECO:0007829|PDB:1Y9L"
SQ SEQUENCE 142 AA; 15853 MW; 20D30F76A3EF9B16 CRC64;
MIRHGSNKLK IFILSILLLT LSGCALKSSS NSEKEWHIVP VSKDYFSIPN DLLWSFNTTN
KSINVYSKCI SGKAVYSFNA GKFMGNFNVK EVDGCFMDAQ KIAIDKLFSM LKDGVVLKGN
KINDTILIEK DGEVKLKLIR GI
