GSPD_VIBCH
ID GSPD_VIBCH Reviewed; 674 AA.
AC P45779;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=Secretin GspD {ECO:0000303|PubMed:28067918};
DE AltName: Full=Cholera toxin secretion protein EpsD;
DE AltName: Full=General secretion pathway protein D;
DE Short=GspD;
DE AltName: Full=Type II secretion system protein D;
DE Short=T2SS protein D;
DE Flags: Precursor;
GN Name=epsD; OrderedLocusNames=VC_2733;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=El Tor TRH7000;
RA Overbye L.J.;
RT "Organization of the general secretion pathway genes in Vibrio cholerae.";
RL Thesis (1994), Michigan State University, United States.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
RN [3] {ECO:0007744|PDB:5WQ8, ECO:0007744|PDB:5WQ9}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.26 ANGSTROMS) OF 25-674, FUNCTION,
RP SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF 395-ASP--THR-417; GLY-477;
RP GLY-505; LEU-508; VAL-510; LEU-522; ILE-524 AND ILE-605.
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).
CC -!- FUNCTION: Involved in a type II secretion system (T2SS, formerly
CC general secretion pathway, GSP) for the export of proteins. Required
CC for secretion of cholera toxin through the outer membrane. This subunit
CC forms the outer membrane channel. {ECO:0000305|PubMed:28067918}.
CC -!- SUBUNIT: Forms a cylindrical channel with 15 subunits; unlike E.coli no
CC 16-subunit channels are seen. The closed pentadeacameric channels are
CC 195 Angstroms long and 145 Angstroms in diameter. Each subunit turns in
CC a clock-wise manner around the channel. {ECO:0000269|PubMed:28067918}.
CC -!- INTERACTION:
CC P45779; P45779: epsD; NbExp=17; IntAct=EBI-6449570, EBI-6449570;
CC -!- SUBCELLULAR LOCATION: Cell outer membrane
CC {ECO:0000305|PubMed:28067918}. Note=Most of the protein is in the
CC periplasm which it traverses to contact proteins of the cell inner
CC membrane. {ECO:0000305|PubMed:28067918}.
CC -!- DOMAIN: The N0, N1, N2 and N3 domains are periplasmic, while the
CC secretin and S domains form a channel that is partially inserted in the
CC outer membrane. The cap gate extends out on the extracellular side of
CC the channel partially closing the channel. The secretin domain forms a
CC double beta-barrel structure; the outer barrel has an outer diameter of
CC about 110 Angstroms while the inner barrel forms the central gate with
CC a small pore in the closed state. {ECO:0000305|PubMed:28067918}.
CC -!- SIMILARITY: Belongs to the bacterial secretin family. GSP D subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AE003852; Type=Frameshift; Note=This may be a natural frameshift.; Evidence={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; L33796; AAA58785.1; -; Genomic_DNA.
DR EMBL; AE003852; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; WP_000878557.1; NZ_LT906614.1.
DR PDB; 5WQ8; EM; 3.26 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O=25-674.
DR PDB; 5WQ9; EM; 4.22 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O=25-674.
DR PDBsum; 5WQ8; -.
DR PDBsum; 5WQ9; -.
DR AlphaFoldDB; P45779; -.
DR SMR; P45779; -.
DR DIP; DIP-59035N; -.
DR GeneID; 57741325; -.
DR OMA; YAVVEMD; -.
DR Proteomes; UP000000584; Chromosome 1.
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; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0009306; P:protein secretion; IBA:GO_Central.
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 InterPro; IPR004845; T2SS_GspD_CS.
DR Pfam; PF00263; Secretin; 1.
DR Pfam; PF03958; Secretin_N; 3.
DR PRINTS; PR00811; BCTERIALGSPD.
DR TIGRFAMs; TIGR02517; type_II_gspD; 1.
DR PROSITE; PS00875; T2SP_D; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Membrane; Protein transport;
KW Reference proteome; Signal; Transmembrane; Transmembrane beta strand;
KW Transport.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..674
FT /note="Secretin GspD"
FT /id="PRO_0000013105"
FT REGION 25..121
FT /note="N0"
FT /evidence="ECO:0000305|PubMed:28067918"
FT REGION 123..187
FT /note="N1"
FT /evidence="ECO:0000305|PubMed:28067918"
FT REGION 188..261
FT /note="N2"
FT /evidence="ECO:0000305|PubMed:28067918"
FT REGION 264..338
FT /note="N3"
FT /evidence="ECO:0000305|PubMed:28067918"
FT REGION 343..612
FT /note="Secretin"
FT /evidence="ECO:0000305|PubMed:28067918"
FT REGION 395..417
FT /note="Cap gate"
FT /evidence="ECO:0000305|PubMed:28067918"
FT REGION 614..674
FT /note="S domain"
FT /evidence="ECO:0000305|PubMed:28067918"
FT SITE 477
FT /note="May serve as a pivot that allows opening of the
FT central gate for substrate egress"
FT /evidence="ECO:0000305|PubMed:28067918"
FT MUTAGEN 395..417
FT /note="Missing: Complex resembles E.coli."
FT /evidence="ECO:0000269|PubMed:28067918"
FT MUTAGEN 477
FT /note="G->A: Decreased complex assembly; complex is
FT partially open."
FT /evidence="ECO:0000269|PubMed:28067918"
FT MUTAGEN 505
FT /note="G->A: No complex assembly."
FT /evidence="ECO:0000269|PubMed:28067918"
FT MUTAGEN 508
FT /note="L->D: No complex assembly."
FT /evidence="ECO:0000269|PubMed:28067918"
FT MUTAGEN 510
FT /note="V->D: No complex assembly."
FT /evidence="ECO:0000269|PubMed:28067918"
FT MUTAGEN 522
FT /note="L->D: No complex assembly."
FT /evidence="ECO:0000269|PubMed:28067918"
FT MUTAGEN 524
FT /note="I->E: No complex assembly."
FT /evidence="ECO:0000269|PubMed:28067918"
FT MUTAGEN 605
FT /note="I->E: No complex assembly."
FT /evidence="ECO:0000269|PubMed:28067918"
FT CONFLICT 89
FT /note="V -> A (in Ref. 1; AAA58785)"
FT /evidence="ECO:0000305"
FT CONFLICT 144
FT /note="R -> P (in Ref. 1; AAA58785)"
FT /evidence="ECO:0000305"
FT STRAND 124..128
FT /evidence="ECO:0007829|PDB:5WQ8"
FT HELIX 136..139
FT /evidence="ECO:0007829|PDB:5WQ8"
FT HELIX 140..149
FT /evidence="ECO:0007829|PDB:5WQ8"
FT STRAND 155..159
FT /evidence="ECO:0007829|PDB:5WQ8"
FT TURN 160..162
FT /evidence="ECO:0007829|PDB:5WQ8"
FT STRAND 163..169
FT /evidence="ECO:0007829|PDB:5WQ8"
FT HELIX 170..184
FT /evidence="ECO:0007829|PDB:5WQ8"
FT TURN 185..187
FT /evidence="ECO:0007829|PDB:5WQ8"
FT STRAND 190..195
FT /evidence="ECO:0007829|PDB:5WQ8"
FT STRAND 197..199
FT /evidence="ECO:0007829|PDB:5WQ8"
FT HELIX 201..209
FT /evidence="ECO:0007829|PDB:5WQ8"
FT STRAND 228..231
FT /evidence="ECO:0007829|PDB:5WQ8"
FT TURN 232..235
FT /evidence="ECO:0007829|PDB:5WQ8"
FT STRAND 236..241
FT /evidence="ECO:0007829|PDB:5WQ8"
FT HELIX 243..255
FT /evidence="ECO:0007829|PDB:5WQ8"
FT STRAND 266..270
FT /evidence="ECO:0007829|PDB:5WQ8"
FT STRAND 272..274
FT /evidence="ECO:0007829|PDB:5WQ8"
FT HELIX 276..287
FT /evidence="ECO:0007829|PDB:5WQ8"
FT STRAND 308..312
FT /evidence="ECO:0007829|PDB:5WQ8"
FT TURN 313..316
FT /evidence="ECO:0007829|PDB:5WQ8"
FT STRAND 317..321
FT /evidence="ECO:0007829|PDB:5WQ8"
FT HELIX 324..337
FT /evidence="ECO:0007829|PDB:5WQ8"
FT STRAND 343..367
FT /evidence="ECO:0007829|PDB:5WQ8"
FT TURN 368..371
FT /evidence="ECO:0007829|PDB:5WQ8"
FT STRAND 372..375
FT /evidence="ECO:0007829|PDB:5WQ8"
FT STRAND 377..381
FT /evidence="ECO:0007829|PDB:5WQ8"
FT HELIX 383..393
FT /evidence="ECO:0007829|PDB:5WQ8"
FT STRAND 396..401
FT /evidence="ECO:0007829|PDB:5WQ8"
FT STRAND 413..417
FT /evidence="ECO:0007829|PDB:5WQ8"
FT HELIX 422..428
FT /evidence="ECO:0007829|PDB:5WQ8"
FT STRAND 433..440
FT /evidence="ECO:0007829|PDB:5WQ8"
FT STRAND 443..467
FT /evidence="ECO:0007829|PDB:5WQ8"
FT STRAND 472..482
FT /evidence="ECO:0007829|PDB:5WQ8"
FT STRAND 500..514
FT /evidence="ECO:0007829|PDB:5WQ8"
FT STRAND 516..518
FT /evidence="ECO:0007829|PDB:5WQ8"
FT STRAND 520..532
FT /evidence="ECO:0007829|PDB:5WQ8"
FT STRAND 541..553
FT /evidence="ECO:0007829|PDB:5WQ8"
FT STRAND 559..575
FT /evidence="ECO:0007829|PDB:5WQ8"
FT HELIX 578..581
FT /evidence="ECO:0007829|PDB:5WQ8"
FT TURN 583..585
FT /evidence="ECO:0007829|PDB:5WQ8"
FT HELIX 586..589
FT /evidence="ECO:0007829|PDB:5WQ8"
FT STRAND 591..606
FT /evidence="ECO:0007829|PDB:5WQ8"
FT HELIX 613..636
FT /evidence="ECO:0007829|PDB:5WQ8"
FT STRAND 640..642
FT /evidence="ECO:0007829|PDB:5WQ8"
FT HELIX 644..646
FT /evidence="ECO:0007829|PDB:5WQ8"
FT HELIX 661..669
FT /evidence="ECO:0007829|PDB:5WQ8"
SQ SEQUENCE 674 AA; 73470 MW; 3D77B891A59E6223 CRC64;
MKYWLKKSSW LLAGSLLSTP LAMANEFSAS FKGTDIQEFI NIVGRNLEKT IIVDPSVRGK
VDVRSFDTLN EEQYYSFFLS VLEVYGFAVV EMDNGVLKVI KSKDAKTSAI PVLSGEERAN
GDEVITQVVA VKNVSVRELS PLLRQLIDNA GAGNVVHYDP ANIILITGRA AVVNRLAEII
RRVDQAGDKE IEVVELNNAS AAEMVRIVEA LNKTTDAQNT PEFLKPKFVA DERTNSILIS
GDPKVRERLK RLIKQLDVEM AAKGNNRVVY LKYAKAEDLV EVLKGVSENL QAEKGTGQPT
TSKRNEVMIA AHADTNSLVL TAPQDIMNAM LEVIGQLDIR RAQVLIEALI VEMAEGDGIN
LGVQWGSLES GSVIQYGNTG ASIGNVMIGL EEAKDTTQTK AVYDTNNNFL RNETTTTKGD
YTKLASALSS IQGAAVSIAM GDWTALINAV SNDSSSNILS SPSITVMDNG EASFIVGEEV
PVITGSTAGS NNDNPFQTVD RKEVGIKLKV VPQINEGNSV QLNIEQEVSN VLGANGAVDV
RFAKRQLNTS VMVQDGQMLV LGGLIDERAL ESESKVPLLG DIPLLGQLFR STSSQVEKKN
LMVFIKPTII RDGVTADGIT QRKYNYIRAE QLFRAEKGLR LLDDASVPVL PKFGDDRRHS
PEIQAFIEQM EAKQ
