SCTC_SHIFL
ID SCTC_SHIFL Reviewed; 566 AA.
AC Q04641; Q8VSH0;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 25-MAY-2022, entry version 133.
DE RecName: Full=Type 3 secretion system secretin {ECO:0000255|HAMAP-Rule:MF_02219, ECO:0000305};
DE Short=T3SS secretin {ECO:0000255|HAMAP-Rule:MF_02219, ECO:0000305};
DE AltName: Full=Outer membrane protein MxiD {ECO:0000305};
DE Flags: Precursor;
GN Name=sctC {ECO:0000255|HAMAP-Rule:MF_02219, ECO:0000303|PubMed:9618447};
GN Synonyms=mxiD {ECO:0000303|PubMed:8437520}; OrderedLocusNames=CP0145;
OS Shigella flexneri.
OG Plasmid pWR100, and Plasmid pCP301.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=M90T / Serotype 5a; PLASMID=pWR100;
RX PubMed=8437520; DOI=10.1111/j.1365-2958.1993.tb01097.x;
RA Allaoui A., Sansonetti P.J., Parsot C.;
RT "MxiD, an outer membrane protein necessary for the secretion of the
RT Shigella flexneri lpa invasins.";
RL Mol. Microbiol. 7:59-68(1993).
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 [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 [5]
RP FUNCTION, INTERACTION WITH MXIM/SCTG AND MXIJ/SCTJ, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
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 [6]
RP REVIEW, AND NOMENCLATURE.
RX PubMed=9618447; DOI=10.1128/mmbr.62.2.379-433.1998;
RA Hueck C.J.;
RT "Type III protein secretion systems in bacterial pathogens of animals and
RT plants.";
RL Microbiol. Mol. Biol. Rev. 62:379-433(1998).
RN [7]
RP REVIEW, AND SUBUNIT.
RX PubMed=30107569; DOI=10.1093/femsle/fny201;
RA Wagner S., Grin I., Malmsheimer S., Singh N., Torres-Vargas C.E.,
RA Westerhausen S.;
RT "Bacterial type III secretion systems: a complex device for the delivery of
RT bacterial effector proteins into eukaryotic host cells.";
RL FEMS Microbiol. Lett. 365:0-0(2018).
RN [8] {ECO:0007744|PDB:2JW1}
RP STRUCTURE BY NMR OF 549-566 IN COMPLEX WITH MXIM/SCTG, 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: Component of the type III secretion system (T3SS), also
CC called injectisome, which is used to inject bacterial effector proteins
CC into eukaryotic host cells (PubMed:8437520). Forms a ring-shaped
CC multimeric structure with an apparent central pore in the outer
CC membrane (PubMed:11717255). Necessary for the secretion of Ipa invasins
CC (PubMed:8437520). {ECO:0000269|PubMed:11717255,
CC ECO:0000269|PubMed:8437520}.
CC -!- SUBUNIT: The core secretion machinery of the T3SS is composed of
CC approximately 20 different proteins, including cytoplasmic components,
CC a base, an export apparatus and a needle (PubMed:30107569). This
CC subunit is part of the base, which anchors the injectisome in the
CC bacterial cell envelope (PubMed:11717255). Forms a stable
CC homooligomeric complex (PubMed:11717255). Interacts with the pilotin
CC MxiM/SctG and the inner membrane ring outer protein MxiJ/SctJ
CC (PubMed:11717255, PubMed:18940609). {ECO:0000269|PubMed:11717255,
CC ECO:0000269|PubMed:18940609, ECO:0000305|PubMed:30107569}.
CC -!- INTERACTION:
CC Q04641; P0A1X2: mxiM; NbExp=3; IntAct=EBI-15735324, EBI-15735345;
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP-
CC Rule:MF_02219, ECO:0000269|PubMed:11717255,
CC ECO:0000305|PubMed:8437520}. Note=Localization to the outer membrane
CC requires MxiM/SctG. {ECO:0000269|PubMed:11717255}.
CC -!- DISRUPTION PHENOTYPE: Inactivated mutant strain is unable to invade
CC HeLa cells and to provoke keratoconjunctivitis in guinea-pigs.
CC {ECO:0000269|PubMed:8437520}.
CC -!- SIMILARITY: Belongs to the bacterial secretin family. T3SS SctC
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_02219, ECO:0000305}.
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DR EMBL; X67206; CAA47644.1; -; Genomic_DNA.
DR EMBL; AL391753; CAC05820.1; -; Genomic_DNA.
DR EMBL; AF348706; AAK18464.1; -; Genomic_DNA.
DR EMBL; AF386526; AAL72331.1; -; Genomic_DNA.
DR PIR; S28068; S28068.
DR RefSeq; NP_085308.1; NC_002698.1.
DR RefSeq; NP_858278.1; NC_004851.1.
DR RefSeq; WP_010921673.1; NZ_QWST01000007.1.
DR RefSeq; YP_009062502.1; NC_024996.1.
DR PDB; 2JW1; NMR; -; B=549-566.
DR PDB; 6RWK; EM; 3.86 A; 0/1/2/3/4/5/6/7/8/9/X/Y/Z/x/y/z=1-566.
DR PDBsum; 2JW1; -.
DR PDBsum; 6RWK; -.
DR AlphaFoldDB; Q04641; -.
DR BMRB; Q04641; -.
DR SMR; Q04641; -.
DR DIP; DIP-45187N; -.
DR IntAct; Q04641; 1.
DR STRING; 198214.CP0145; -.
DR PRIDE; Q04641; -.
DR EnsemblBacteria; AAL72331; AAL72331; SF_p0145.
DR GeneID; 1238034; -.
DR KEGG; sfl:CP0145; -.
DR PATRIC; fig|198214.7.peg.5392; -.
DR HOGENOM; CLU_022474_4_0_6; -.
DR EvolutionaryTrace; Q04641; -.
DR Proteomes; UP000001006; Plasmid pCP301.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030257; C:type III protein secretion system complex; IEA:UniProtKB-UniRule.
DR GO; GO:0030254; P:protein secretion by the type III secretion system; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.1370.120; -; 2.
DR HAMAP; MF_02219; Type_III_secretin; 1.
DR InterPro; IPR005644; NolW-like.
DR InterPro; IPR038591; NolW-like_sf.
DR InterPro; IPR004846; T2SS/T3SS.
DR InterPro; IPR004845; T2SS_GspD_CS.
DR InterPro; IPR003522; T3SS_OM_pore_YscC.
DR Pfam; PF00263; Secretin; 1.
DR Pfam; PF03958; Secretin_N; 1.
DR PRINTS; PR01337; TYPE3OMGPROT.
DR TIGRFAMs; TIGR02516; type_III_yscC; 1.
DR PROSITE; PS00875; T2SP_D; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Membrane; Plasmid; Protein transport;
KW Reference proteome; Signal; Translocation; Transport; Virulence.
FT SIGNAL 1..22
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02219"
FT CHAIN 23..566
FT /note="Type 3 secretion system secretin"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02219"
FT /id="PRO_0000013112"
FT VARIANT 296
FT /note="V -> I (in plasmid pCP301)"
FT HELIX 557..564
FT /evidence="ECO:0007829|PDB:2JW1"
SQ SEQUENCE 566 AA; 63173 MW; 56B0D80BB16C2431 CRC64;
MKKFNIKSLT LLIVLLPLIV NANNIDSHLL EQNDIAKYVA QSDTVGSFFE RFSALLNYPI
VVSKQAAKKR ISGEFDLSNP EEMLEKLTLL VGLIWYKDGN ALYIYDSGEL ISKVILLENI
SLNYLIQYLK DANLYDHRYP IRGNISDKTF YISGPPALVE LVANTATLLD KQVSSIGTDK
VNFGVIKLKN TFVSDRTYNM RGEDIVIPGV ATVVERLLNN GKALSNRQAQ NDPMPPFNIT
QKVSEDSNDF SFSSVTNSSI LEDVSLIAYP ETNSILVKGN DQQIQIIRDI ITQLDVAKRH
IELSLWIIDI DKSELNNLGV NWQGTASFGD SFGASFNMSS SASISTLDGN KFIASVMALN
QKKKANVVSR PVILTQENIP AIFDNNRTFY VSLVGERNSS LEHVTYGTLI NVIPRFSSRG
QIEMSLTIED GTGNSQSNYN YNNENTSVLP EVGRTKISTI ARVPQGKSLL IGGYTHETNS
NEIISIPFLS SIPVIGNVFK YKTSNISNIV RVFLIQPREI KESSYYNTAE YKSLISEREI
QKTTQIIPSE TTLLEDEKSL VSYLNY
