SCTC_YEREN
ID SCTC_YEREN Reviewed; 607 AA.
AC Q01244;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 25-MAY-2022, entry version 99.
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=YscC secretin {ECO:0000303|PubMed:15231798};
DE Flags: Precursor;
GN Name=sctC {ECO:0000255|HAMAP-Rule:MF_02219, ECO:0000303|PubMed:9618447};
GN Synonyms=yscC {ECO:0000303|PubMed:1860816};
OS Yersinia enterocolitica.
OG Plasmid pYV.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=630;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=439-80 / Serotype O:9;
RX PubMed=1860816; DOI=10.1128/jb.173.16.4994-5009.1991;
RA Michiels T., Vanooteghem J.-C., de Rouvroit C., China B., Gustin A.,
RA Boudry P., Cornelis G.R.;
RT "Analysis of virC, an operon involved in the secretion of Yop proteins by
RT Yersinia enterocolitica.";
RL J. Bacteriol. 173:4994-5009(1991).
RN [2]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, INDUCTION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=W22703 / Serotype O:9 / Biotype 2;
RX PubMed=9427408; DOI=10.1046/j.1365-2958.1997.6141981.x;
RA Koster M., Bitter W., de Cock H., Allaoui A., Cornelis G.R., Tommassen J.;
RT "The outer membrane component, YscC, of the Yop secretion machinery of
RT Yersinia enterocolitica forms a ring-shaped multimeric complex.";
RL Mol. Microbiol. 26:789-797(1997).
RN [3]
RP FUNCTION, AND SUBUNIT.
RC STRAIN=W22703 / Serotype O:9 / Biotype 2;
RX PubMed=15231798; DOI=10.1128/jb.186.14.4645-4654.2004;
RA Burghout P., van Boxtel R., Van Gelder P., Ringler P., Mueller S.A.,
RA Tommassen J., Koster M.;
RT "Structure and electrophysiological properties of the YscC secretin from
RT the type III secretion system of Yersinia enterocolitica.";
RL J. Bacteriol. 186:4645-4654(2004).
RN [4]
RP INTERACTION WITH YSCW/SCTG, AND SUBCELLULAR LOCATION.
RC STRAIN=W22703 / Serotype O:9 / Biotype 2;
RX PubMed=15292137; DOI=10.1128/jb.186.16.5366-5375.2004;
RA Burghout P., Beckers F., de Wit E., van Boxtel R., Cornelis G.R.,
RA Tommassen J., Koster M.;
RT "Role of the pilot protein YscW in the biogenesis of the YscC secretin in
RT Yersinia enterocolitica.";
RL J. Bacteriol. 186:5366-5375(2004).
RN [5]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=24207124; DOI=10.1016/j.str.2013.09.012;
RA Kowal J., Chami M., Ringler P., Mueller S.A., Kudryashev M.,
RA Castano-Diez D., Amstutz M., Cornelis G.R., Stahlberg H., Engel A.;
RT "Structure of the dodecameric Yersinia enterocolitica secretin YscC and its
RT trypsin-resistant core.";
RL Structure 21:2152-2161(2013).
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).
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:9427408, PubMed:15231798,
CC PubMed:24207124). Forms a ring-shaped multimeric structure with an
CC apparent central pore in the outer membrane (PubMed:9427408,
CC PubMed:15231798, PubMed:24207124). It may serve as an injectisome
CC assembly platform (PubMed:24207124). Essential for the export of Yop
CC proteins (PubMed:9427408). {ECO:0000269|PubMed:15231798,
CC ECO:0000269|PubMed:24207124, ECO:0000269|PubMed:9427408}.
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:15231798, PubMed:24207124). Forms a
CC stable homooligomeric complex (PubMed:9427408, PubMed:15231798,
CC PubMed:24207124). The complex is composed of 12 subunits
CC (PubMed:24207124). Interacts with the pilotin YscW/SctG, which is
CC important for localization and efficient oligomerization of SctC
CC (PubMed:15292137). Interacts with the inner membrane ring inner protein
CC YscD/SctD (PubMed:24207124). {ECO:0000269|PubMed:15231798,
CC ECO:0000269|PubMed:15292137, ECO:0000269|PubMed:24207124,
CC ECO:0000269|PubMed:9427408, ECO:0000305|PubMed:24207124,
CC ECO:0000305|PubMed:30107569}.
CC -!- INTERACTION:
CC Q01244; Q01244: sctC; NbExp=3; IntAct=EBI-16080711, EBI-16080711;
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP-
CC Rule:MF_02219, ECO:0000269|PubMed:15292137,
CC ECO:0000269|PubMed:24207124, ECO:0000269|PubMed:9427408}.
CC Note=Localization to the outer membrane requires YscW/SctG.
CC {ECO:0000269|PubMed:15292137}.
CC -!- INDUCTION: The SctC complex is found in cells grown at 37 degrees
CC Celsius, but not in cells grown at 23 degrees Celsius. Detectable in
CC cells grown in the presence of Ca(2+), although less abundantly than in
CC cells grown under Ca(2+) depletion. {ECO:0000269|PubMed:9427408}.
CC -!- DOMAIN: The oligomeric secretin consists of an outer membrane ring
CC connected via a thin cylindrical wall to a conical, periplasmic region
CC that exposes N-terminal petals connected by flexible linkers. These
CC petals harbor the binding site of YscD/SctD, a component of the inner
CC membrane ring. {ECO:0000269|PubMed:24207124}.
CC -!- DISRUPTION PHENOTYPE: Mutant does not secrete Yop proteins.
CC {ECO:0000269|PubMed:9427408}.
CC -!- MISCELLANEOUS: The secretion channel formed by SctC remains closed in
CC the absence of the other components of the T3SS.
CC {ECO:0000269|PubMed:15231798}.
CC -!- SIMILARITY: Belongs to the bacterial secretin family. T3SS SctC
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_02219, ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M74011; AAC37020.1; -; Genomic_DNA.
DR PIR; C40361; C40361.
DR RefSeq; WP_010891225.1; NZ_KN150737.1.
DR AlphaFoldDB; Q01244; -.
DR SMR; Q01244; -.
DR DIP; DIP-60586N; -.
DR TCDB; 1.B.22.3.3; the outer bacterial membrane secretin (secretin) family.
DR OMA; YLMARIS; -.
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:0042802; F:identical protein binding; IPI:IntAct.
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; 2.
DR PRINTS; PR01337; TYPE3OMGPROT.
DR TIGRFAMs; TIGR02516; type_III_yscC; 1.
DR PROSITE; PS00875; T2SP_D; 1.
PE 1: Evidence at protein level;
KW Cell outer membrane; Membrane; Plasmid; Protein transport; Signal;
KW Translocation; Transport; Virulence.
FT SIGNAL 1..26
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02219"
FT CHAIN 27..607
FT /note="Type 3 secretion system secretin"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02219"
FT /id="PRO_0000013120"
SQ SEQUENCE 607 AA; 67209 MW; CC5EA81348F3C687 CRC64;
MAFPLHSFFK RVLTGTLLLL SSYSWAQELD WLPIPYVYVA KGESLRDLLT DFGANYDATV
VVSDKINDKV SGQFEHDNPQ DFLQHIASLY NLVWYYDGNV LYIFKNSEVA SRLIRLQESE
AAELKQALQR SGIWEPRFGW RPDASNRLVY VSGPPRYLEL VEQTAAALEQ QTQIRSEKTG
ALAIEIFPLK YASASDRTIH YRDDEVAAPG VATILQRVLS DATIQQVTVD NQRIPQAATR
ASAQARVEAD PSLNAIIVRD SPERMPMYQR LIHALDKPSA RIEVALSIVD INADQLTELG
VDWRVGIRTG NNHQVVIKTT GDQSNIASNG ALGSLVDARG LDYLLARVNL LENEGSAQVV
SRPTLLTQEN AQAVIDHSET YYVKVTGKEV AELKGITYGT MLRMTPRVLT QGDKSEISLN
LHIEDGNQKP NSSGIEGIPT ISRTVVDTVA RVGHGQSLII GGIYRDELSV ALSKVPLLGD
IPYIGALFRR KSELTRRTVR LFIIEPRIID EGIAHHLALG NGQDLRTGIL TVDEISNQST
TLNKLLGGSQ CQPLNKAQEV QKWLSQNNKS SYLTQCKMDK SLGWRVVEGA CTPAQSWCVS
APKRGVL
