ASPS2_ECOH1
ID ASPS2_ECOH1 Reviewed; 136 AA.
AC E3PJ88;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 1.
DT 25-MAY-2022, entry version 38.
DE RecName: Full=Pilotin AspS 2 {ECO:0000303|PubMed:29632366};
DE AltName: Full=Type II secretion system-beta protein GspS-beta {ECO:0000303|PubMed:22585966};
DE Flags: Precursor;
GN Name=gspS2 {ECO:0000305};
GN Synonyms=aspS {ECO:0000303|PubMed:29632366},
GN gspS-beta {ECO:0000303|PubMed:22585966},
GN yghG {ECO:0000303|PubMed:22585966}; OrderedLocusNames=ETEC_3239;
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 FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP CYS-25 AND 26-ALA-SER-27.
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:5ZDH}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.20 ANGSTROMS) OF 25-136 IN COMPLEX WITH
RP GSPD2, FUNCTION, SUBCELLULAR LOCATION, AND DISULFIDE BONDS.
RC STRAIN=H10407 / ETEC;
RX PubMed=29632366; DOI=10.1038/s41564-018-0148-0;
RA Yin M., Yan Z., Li X.;
RT "Structural insight into the assembly of the type II secretion system
RT pilotin-secretin complex from enterotoxigenic Escherichia coli.";
RL Nat. Microbiol. 3:581-587(2018).
CC -!- FUNCTION: Part of a type II secretion system (T2SS, formerly general
CC secretion pathway, GSP) for the export of folded proteins across the
CC outer membrane (Probable). Required for correct assembly of the type II
CC secretion system-beta (T2SS-beta), for localization of GspD-beta to the
CC cell outer membrane and for export of a labile enterotoxin by T2SS-beta
CC (PubMed:22585966). Each AspS2 binds to 2 GspD2 subunits and may clamp
CC the monomers together, stabilizing structure and accelerating its
CC assembly (PubMed:29632366). {ECO:0000269|PubMed:22585966,
CC ECO:0000269|PubMed:29632366, ECO:0000305|PubMed:22585966}.
CC -!- SUBUNIT: Cryo-electron microscopy shows the complex forms a cylindrical
CC channel with 15 GspD2 subunits, each of which interacts with its
CC surroundingy AspS2 (GspS-beta). {ECO:0000269|PubMed:29632366}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000305|PubMed:22585966,
CC ECO:0000305|PubMed:29632366}; Lipid-anchor
CC {ECO:0000305|PubMed:22585966, ECO:0000305|PubMed:29632366}; Periplasmic
CC side {ECO:0000305|PubMed:22585966, ECO:0000305|PubMed:29632366}.
CC Note=Protein can also be located in the cell inner membrane.
CC {ECO:0000305|PubMed:22585966}.
CC -!- DISRUPTION PHENOTYPE: Severely disrupts assembly and function of T2SS-
CC beta, mislocalization of GspD-beta to the cell inner membrane.
CC {ECO:0000269|PubMed:22585966}.
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:29632366}.
CC -!- SIMILARITY: Belongs to the GspS/AspS pilotin family. {ECO:0000305}.
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DR EMBL; FN649414; CBJ02739.1; -; Genomic_DNA.
DR RefSeq; WP_001389459.1; NC_017633.1.
DR PDB; 5ZDH; EM; 3.20 A; P/Q/R/S/T/U/V/W/X/Y/Z/a/b/c/d=25-136.
DR PDBsum; 5ZDH; -.
DR AlphaFoldDB; E3PJ88; -.
DR SMR; E3PJ88; -.
DR EnsemblBacteria; CBJ02739; CBJ02739; ETEC_3239.
DR KEGG; elh:ETEC_3239; -.
DR HOGENOM; CLU_156494_0_0_6; -.
DR OMA; HQANKIN; -.
DR Proteomes; UP000006877; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR InterPro; IPR016502; T2SSS_2.
DR Pfam; PF16549; T2SSS_2; 1.
DR PIRSF; PIRSF007010; UCP007010; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Disulfide bond; Lipoprotein; Membrane;
KW Palmitate; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 25..136
FT /note="Pilotin AspS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT /id="PRO_5003179701"
FT LIPID 25
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 25
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT DISULFID 94..131
FT /evidence="ECO:0007744|PDB:5ZDH"
FT MUTAGEN 25
FT /note="C->A: Precursor protein is not processed."
FT /evidence="ECO:0000269|PubMed:22585966"
FT MUTAGEN 26..27
FT /note="AS->DD: Protein is found almost exclusively in the
FT inner membrane, does not restore targeting of GspD-beta to
FT the outer membrane."
FT /evidence="ECO:0000269|PubMed:22585966"
SQ SEQUENCE 136 AA; 14670 MW; 8CF2819C427D869A CRC64;
MSIKQMPGRV LISLLLSVTG LLSGCASHNE NASLLAKKQA QNISQNLPIK SAGYTLVLAQ
SSGTTVKMTI ISEAGTQTTQ TPDAFLTSYQ RQMCADPTVK LMLTEGINYS ITINDTRTGN
QYQRKLDRTT CGIVKA
