ID   GSPC2_ECOH1             Reviewed;         319 AA.
AC   E3PJ87;
DT   10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT   10-APR-2019, sequence version 2.
DT   03-AUG-2022, entry version 54.
DE   RecName: Full=Type II secretion system protein C 2;
DE            Short=T2SS protein C 2;
DE   AltName: Full=General secretion pathway protein C 2;
DE   AltName: Full=Type II secretion system protein C beta;
GN   Name=gspC2; OrderedLocusNames=ETEC_3238;
OS   Escherichia coli O78:H11 (strain H10407 / ETEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=316401;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H10407 / ETEC;
RX   PubMed=20802035; DOI=10.1128/jb.00710-10;
RA   Crossman L.C., Chaudhuri R.R., Beatson S.A., Wells T.J., Desvaux M.,
RA   Cunningham A.F., Petty N.K., Mahon V., Brinkley C., Hobman J.L.,
RA   Savarino S.J., Turner S.M., Pallen M.J., Penn C.W., Parkhill J.,
RA   Turner A.K., Johnson T.J., Thomson N.R., Smith S.G., Henderson I.R.;
RT   "A commensal gone bad: complete genome sequence of the prototypical
RT   enterotoxigenic Escherichia coli strain H10407.";
RL   J. Bacteriol. 192:5822-5831(2010).
RN   [2]
RP   DISCUSSION OF T2SS.
RC   STRAIN=H10407 / ETEC;
RX   PubMed=22585966; DOI=10.1128/iai.06394-11;
RA   Strozen T.G., Li G., Howard S.P.;
RT   "YghG (GspSbeta) is a novel pilot protein required for localization of the
RT   GspSbeta type II secretion system secretin of enterotoxigenic Escherichia
RT   coli.";
RL   Infect. Immun. 80:2608-2622(2012).
RN   [3] {ECO:0007744|PDB:3OSS}
RP   X-RAY CRYSTALLOGRAPHY (2.63 ANGSTROMS) OF 122-186, AND INTERACTION WITH
RP   GSPD2.
RC   STRAIN=H10407 / ETEC;
RX   PubMed=21931548; DOI=10.1371/journal.ppat.1002228;
RA   Korotkov K.V., Johnson T.L., Jobling M.G., Pruneda J., Pardon E.,
RA   Heroux A., Turley S., Steyaert J., Holmes R.K., Sandkvist M., Hol W.G.;
RT   "Structural and functional studies on the interaction of GspC and GspD in
RT   the type II secretion system.";
RL   PLoS Pathog. 7:E1002228-E1002228(2011).
CC   -!- FUNCTION: Involved in a type II secretion system (T2SS, formerly
CC       general secretion pathway, GSP) for the export of folded proteins
CC       across the outer membrane. {ECO:0000305|PubMed:22585966}.
CC   -!- SUBUNIT: Interacts with outer cell membrane protein GspD2 in the
CC       periplasm. {ECO:0000269|PubMed:21931548}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Single-pass
CC       membrane protein {ECO:0000305}.
CC   -!- MISCELLANEOUS: Encoded in a type II secretion system (T2SS-beta); this
CC       strain encodes 2 T2SS but only this one (beta) is expressed under
CC       standard laboratory conditions. {ECO:0000305|PubMed:22585966}.
CC   -!- SIMILARITY: Belongs to the GSP C family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CBJ02738.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; FN649414; CBJ02738.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_001549326.1; NC_017633.1.
DR   PDB; 3OSS; X-ray; 2.63 A; C=122-186.
DR   PDBsum; 3OSS; -.
DR   AlphaFoldDB; E3PJ87; -.
DR   SMR; E3PJ87; -.
DR   EnsemblBacteria; CBJ02738; CBJ02738; ETEC_3238.
DR   KEGG; elh:ETEC_3238; -.
DR   HOGENOM; CLU_068012_2_0_6; -.
DR   Proteomes; UP000006877; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015627; C:type II protein secretion system complex; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProt.
DR   GO; GO:0015628; P:protein secretion by the type II secretion system; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProt.
DR   Gene3D; 2.30.42.10; -; 1.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR024961; T2SS_GspC_N.
DR   InterPro; IPR001639; T2SS_protein-GspC.
DR   Pfam; PF11356; T2SSC; 1.
DR   SUPFAM; SSF50156; SSF50156; 1.
DR   TIGRFAMs; TIGR01713; typeII_sec_gspC; 1.
DR   PROSITE; PS01141; T2SP_C; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell inner membrane; Cell membrane; Membrane;
KW   Protein transport; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..319
FT                   /note="Type II secretion system protein C 2"
FT                   /id="PRO_0000446500"
FT   TOPO_DOM        1..42
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        43..65
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        66..319
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000305|PubMed:21931548"
FT   STRAND          128..137
FT                   /evidence="ECO:0007829|PDB:3OSS"
FT   STRAND          139..144
FT                   /evidence="ECO:0007829|PDB:3OSS"
FT   STRAND          147..151
FT                   /evidence="ECO:0007829|PDB:3OSS"
FT   STRAND          158..167
FT                   /evidence="ECO:0007829|PDB:3OSS"
FT   STRAND          169..176
FT                   /evidence="ECO:0007829|PDB:3OSS"
FT   STRAND          179..185
FT                   /evidence="ECO:0007829|PDB:3OSS"
SQ   SEQUENCE   319 AA;  35737 MW;  608DEAF577AE3B90 CRC64;
     MARVVFRDAR IYLIQWLTKI RHTLNQRQSL NTDKEHLRKI VRGMFWLMLL IISAKVAHSL
     WRYFSFSAEY TAVSPSANKP PRADAKTFDK NDVQLISQQN WFGKYQPVAT PVKQPEPASV
     AETRLNVVLR GIAFGARPGA VIEEGGKQQV YLQGERLDSH NAVIEEINRD HVMLRYQGKI
     ERLSLAEEGH STVAVTNKKA VSDEAKQAVA EPAASAPVEI PTAVRQALTK DPQKIFNYIQ
     LTPVRKEGIV GYAVKPGADR SLFDASGFKE GDIAIALNQQ DFTDPRAMIA LMRQLPSMDS
     IQLTVLRKGA RHDISIALR