GSPD2_ECOH1
ID GSPD2_ECOH1 Reviewed; 686 AA.
AC E3PJ86;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 1.
DT 25-MAY-2022, entry version 54.
DE RecName: Full=Secretin GspD 2 {ECO:0000305};
DE AltName: Full=General secretion pathway protein D 2;
DE Short=GspD;
DE AltName: Full=GspD-beta secretin {ECO:0000303|PubMed:22585966};
DE AltName: Full=Type II secretion system protein D 2;
DE Short=T2SS protein D;
DE Flags: Precursor;
GN Name=gspD2; Synonyms=gspD-beta {ECO:0000303|PubMed:22585966};
GN OrderedLocusNames=ETEC_3237;
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 SUBUNIT, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
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]
RP DISCUSSION OF SEQUENCE, AND DOMAIN.
RC STRAIN=H10407 / ETEC;
RX PubMed=28067918; DOI=10.1038/nsmb.3350;
RA Yan Z., Yin M., Xu D., Zhu Y., Li X.;
RT "Structural insights into the secretin translocation channel in the type II
RT secretion system.";
RL Nat. Struct. Mol. Biol. 24:177-183(2017).
RN [4] {ECO:0007744|PDB:3OSS}
RP X-RAY CRYSTALLOGRAPHY (2.63 ANGSTROMS) OF 40-110 AND 114-205 IN COMPLEX
RP WITH GSPC2, INTERACTION WITH GSPC2, AND DOMAIN.
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).
RN [5] {ECO:0007744|PDB:4JTM}
RP X-RAY CRYSTALLOGRAPHY (1.43 ANGSTROMS) OF 43-120, AND SUBUNIT.
RC STRAIN=H10407 / ETEC;
RX PubMed=23820381; DOI=10.1016/j.jsb.2013.06.013;
RA Korotkov K.V., Delarosa J.R., Hol W.G.;
RT "A dodecameric ring-like structure of the N0 domain of the type II secretin
RT from enterotoxigenic Escherichia coli.";
RL J. Struct. Biol. 183:354-362(2013).
RN [6] {ECO:0007744|PDB:5ZDH}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.20 ANGSTROMS) OF 41-686 IN COMPLEX WITH
RP ASPS2, SUBCELLULAR LOCATION, AND MUTAGENESIS OF 675-GLU--ASN-681;
RP 676-VAL--LEU-680; VAL-676; PHE-679; LEU-680 AND 684-ARG--ARG-686.
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). This subunit forms the outer membrane
CC channel (Probable). {ECO:0000305|PubMed:22585966,
CC ECO:0000305|PubMed:23820381, ECO:0000305|PubMed:29632366}.
CC -!- SUBUNIT: Forms a cylindrical channel with 15 subunits, each of which
CC interacts with the surrounding pilotin AspS2 proteins (also called
CC GspS-beta) (PubMed:29632366). Interacts with inner cell membrane
CC protein GspC2 in the periplasm (PubMed:21931548). Forms multimers in
CC the outer membrane (PubMed:22585966). The isolated N0 domain forms
CC dimers that self-assemble into rings (PubMed:23820381).
CC {ECO:0000269|PubMed:21931548, ECO:0000269|PubMed:22585966,
CC ECO:0000269|PubMed:23820381, ECO:0000269|PubMed:29632366}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000269|PubMed:22585966,
CC ECO:0000305|PubMed:29632366}. Note=Some protein is also found in the
CC cell inner membrane, the inner membrane protein does not form multimers
CC and is unstable (PubMed:22585966). Most of the protein is in the
CC periplasm which it traverses to contact proteins of the cell inner
CC membrane (Probable). {ECO:0000269|PubMed:22585966,
CC ECO:0000305|PubMed:29632366}.
CC -!- DOMAIN: The N0 region interacts in the periplasm with GspC
CC (PubMed:21931548). The S domain interacts with pilotin AspS2
CC (PubMed:29632366). The N0, N1, N2 and N3 domains are periplasmic, while
CC the secretin and S domains form a channel that is partially inserted in
CC the outer membrane. The cap gate extends out on the extracellular side
CC of the channel partially closing the channel. The secretin domain forms
CC a double beta-barrel structure; the outer barrel has an outer diameter
CC of about 110 Angstroms while the inner barrel forms the central gate
CC with a small pore in the closed state (By similarity).
CC {ECO:0000250|UniProtKB:P45779, ECO:0000269|PubMed:21931548,
CC ECO:0000269|PubMed:29632366}.
CC -!- DISRUPTION PHENOTYPE: Severely disrupts assembly and function of T2SS-
CC beta. {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:22585966,
CC ECO:0000305|PubMed:29632366}.
CC -!- SIMILARITY: Belongs to the bacterial secretin family. GSP D subfamily.
CC {ECO:0000305}.
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DR EMBL; FN649414; CBJ02737.1; -; Genomic_DNA.
DR RefSeq; WP_000498824.1; NC_017633.1.
DR PDB; 3OSS; X-ray; 2.63 A; D=40-110, D=114-205.
DR PDB; 4JTM; X-ray; 1.43 A; A/B=43-120.
DR PDB; 5ZDH; EM; 3.20 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O=41-686.
DR PDBsum; 3OSS; -.
DR PDBsum; 4JTM; -.
DR PDBsum; 5ZDH; -.
DR AlphaFoldDB; E3PJ86; -.
DR SMR; E3PJ86; -.
DR EnsemblBacteria; CBJ02737; CBJ02737; ETEC_3237.
DR KEGG; elh:ETEC_3237; -.
DR HOGENOM; CLU_006756_1_1_6; -.
DR OMA; YAVVEMD; -.
DR Proteomes; UP000006877; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015627; C:type II protein secretion system complex; IEA:InterPro.
DR GO; GO:0015628; P:protein secretion by the type II secretion system; IEA:InterPro.
DR Gene3D; 3.30.1370.120; -; 3.
DR InterPro; IPR001775; GspD/PilQ.
DR InterPro; IPR005644; NolW-like.
DR InterPro; IPR038591; NolW-like_sf.
DR InterPro; IPR004846; T2SS/T3SS.
DR InterPro; IPR013356; T2SS_GspD.
DR Pfam; PF00263; Secretin; 1.
DR Pfam; PF03958; Secretin_N; 3.
DR PRINTS; PR00811; BCTERIALGSPD.
DR TIGRFAMs; TIGR02517; type_II_gspD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Membrane; Protein transport; Signal;
KW Transmembrane; Transmembrane beta strand; Transport.
FT SIGNAL 1..40
FT /evidence="ECO:0000255"
FT CHAIN 41..686
FT /note="Secretin GspD 2"
FT /evidence="ECO:0000255"
FT /id="PRO_5003179632"
FT REGION 41..140
FT /note="N0, contacts GspC2"
FT /evidence="ECO:0000269|PubMed:21931548,
FT ECO:0000305|PubMed:28067918"
FT REGION 142..206
FT /note="N1"
FT /evidence="ECO:0000305|PubMed:28067918"
FT REGION 207..279
FT /note="N2"
FT /evidence="ECO:0000305|PubMed:28067918"
FT REGION 282..357
FT /note="N3"
FT /evidence="ECO:0000305|PubMed:28067918"
FT REGION 360..627
FT /note="Secretin"
FT /evidence="ECO:0000305|PubMed:28067918"
FT REGION 414..433
FT /note="Cap gate"
FT /evidence="ECO:0000305|PubMed:28067918"
FT REGION 629..686
FT /note="S domain, contacts AspS2"
FT /evidence="ECO:0000269|PubMed:29632366,
FT ECO:0000305|PubMed:28067918"
FT SITE 493
FT /note="May serve as a pivot that allows opening of the
FT central gate for substrate egress"
FT /evidence="ECO:0000250|UniProtKB:P45779"
FT MUTAGEN 675..681
FT /note="EVRAFLN->AVRAAFLA: Binds AspS2 normally."
FT /evidence="ECO:0000269|PubMed:29632366"
FT MUTAGEN 676..680
FT /note="VRAFL->ARAAA: No longer binds AspS2."
FT /evidence="ECO:0000269|PubMed:29632366"
FT MUTAGEN 676
FT /note="V->A: Binds AspS2 normally."
FT /evidence="ECO:0000269|PubMed:29632366"
FT MUTAGEN 679
FT /note="F->A: No longer binds AspS2, the AspS2-GspD2 complex
FT no longer forms in vivo."
FT /evidence="ECO:0000269|PubMed:29632366"
FT MUTAGEN 680
FT /note="L->A: Binds AspS2 normally."
FT /evidence="ECO:0000269|PubMed:29632366"
FT MUTAGEN 684..686
FT /note="RTR->AAA: Binds AspS2 normally."
FT /evidence="ECO:0000269|PubMed:29632366"
FT STRAND 48..53
FT /evidence="ECO:0007829|PDB:4JTM"
FT HELIX 54..65
FT /evidence="ECO:0007829|PDB:4JTM"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:4JTM"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:4JTM"
FT HELIX 89..103
FT /evidence="ECO:0007829|PDB:4JTM"
FT STRAND 105..110
FT /evidence="ECO:0007829|PDB:4JTM"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:4JTM"
FT STRAND 114..119
FT /evidence="ECO:0007829|PDB:4JTM"
FT STRAND 143..149
FT /evidence="ECO:0007829|PDB:3OSS"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:3OSS"
FT HELIX 155..158
FT /evidence="ECO:0007829|PDB:3OSS"
FT HELIX 159..169
FT /evidence="ECO:0007829|PDB:3OSS"
FT STRAND 174..178
FT /evidence="ECO:0007829|PDB:3OSS"
FT TURN 179..181
FT /evidence="ECO:0007829|PDB:3OSS"
FT STRAND 182..188
FT /evidence="ECO:0007829|PDB:3OSS"
FT HELIX 189..204
FT /evidence="ECO:0007829|PDB:3OSS"
SQ SEQUENCE 686 AA; 74202 MW; 213BE2A98A043B4F CRC64;
MFWRDITLSV WRKKTTGLKT KKRLLPLVLA AALCSSPVWA EEATFTANFK DTDLKSFIET
VGANLNKTII MGPGVQGKVS IRTMTPLNER QYYQLFLNLL EAQGYAVVPM ENDVLKVVKS
SAAKVEPLPL VGEGSDNYAG DEMVTKVVPV RNVSVRELAP ILRQMIDSAG SGNVVNYDPS
NVIMLTGRAS VVERLTEVIQ RVDHAGNRTE EVIPLDNASA SEIARVLESL TKNSGENQPA
TLKSQIVADE RTNSVIVSGD PATRDKMRRL IRRLDSEMER SGNSQVFYLK YSKAEDLVDV
LKQVSGTLTA AKEEAEGTVG SGREIVSIAA SKHSNALIVT APQDIMQSLQ SVIEQLDIRR
AQVHVEALIV EVAEGSNINF GVQWASKDAG LMQFANGTQI PIGTLGAAIS QAKPQKGSTV
ISENGATTIN PDTNGDLSTL AQLLSGFSGT AVGVVKGDWM ALVQAVKNDS SSNVLSTPSI
TTLDNQEAFF MVGQDVPVLT GSTVGSNNSN PFNTVERKKV GIMLKVTPQI NEGNAVQMVI
EQEVSKVEGQ TSLDVVFGER KLKTTVLAND GELIVLGGLM DDQAGESVAK VPLLGDIPLI
GNLFKSTADK KEKRNLMVFI RPTILRDGMA ADGVSQRKYN YMRAEQIYRD EQGLSLMPHT
AQPVLPAQNQ ALPPEVRAFL NAGRTR
