GSPD2_DICD3
ID GSPD2_DICD3 Reviewed; 710 AA.
AC Q01565; E0SM41;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Secretin OutD;
DE AltName: Full=General secretion pathway protein D;
DE AltName: Full=Pectic enzymes secretion protein OutD;
DE AltName: Full=Type II secretion system protein D;
DE Short=T2SS protein D;
DE Flags: Precursor;
GN Name=outD; OrderedLocusNames=Dda3937_02415;
OS Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937)).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Dickeya.
OX NCBI_TaxID=198628;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=3937;
RX PubMed=1453958; DOI=10.1111/j.1365-2958.1992.tb01775.x;
RA Condemine G., Dorel C., Hugouvieux-Cotte-Pattat N., Robert-Baudouy J.;
RT "Some of the out genes involved in the secretion of pectate lyases in
RT Erwinia chrysanthemi are regulated by kdgR.";
RL Mol. Microbiol. 6:3199-3211(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3937;
RX PubMed=21217001; DOI=10.1128/jb.01513-10;
RA Glasner J.D., Yang C.H., Reverchon S., Hugouvieux-Cotte-Pattat N.,
RA Condemine G., Bohin J.P., Van Gijsegem F., Yang S., Franza T., Expert D.,
RA Plunkett G. III, San Francisco M.J., Charkowski A.O., Py B., Bell K.,
RA Rauscher L., Rodriguez-Palenzuela P., Toussaint A., Holeva M.C., He S.Y.,
RA Douet V., Boccara M., Blanco C., Toth I., Anderson B.D., Biehl B.S.,
RA Mau B., Flynn S.M., Barras F., Lindeberg M., Birch P.R., Tsuyumu S.,
RA Shi X., Hibbing M., Yap M.N., Carpentier M., Dassa E., Umehara M.,
RA Kim J.F., Rusch M., Soni P., Mayhew G.F., Fouts D.E., Gill S.R.,
RA Blattner F.R., Keen N.T., Perna N.T.;
RT "Genome sequence of the plant-pathogenic bacterium Dickeya dadantii 3937.";
RL J. Bacteriol. 193:2076-2077(2011).
RN [3] {ECO:0007744|PDB:4K0U}
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 693-705, SUBUNIT, AND DOMAIN.
RX PubMed=23897461; DOI=10.1107/s0907444913007658;
RA Rehman S., Gu S., Shevchik V.E., Pickersgill R.W.;
RT "Anatomy of secretin binding to the Dickeya dadantii type II secretion
RT system pilotin.";
RL Acta Crystallogr. D 69:1381-1386(2013).
CC -!- FUNCTION: Involved in a type II secretion system (T2SS, formerly
CC general secretion pathway, GSP) for the export of proteins (By
CC similarity). Required for the translocation of the multiple pectic
CC enzymes (Probable). This subunit forms the outer membrane channel (By
CC similarity). {ECO:0000250|UniProtKB:E3PJ86,
CC ECO:0000250|UniProtKB:P45779, ECO:0000305|PubMed:1453958}.
CC -!- SUBUNIT: Forms a cylindrical channel with 15 subunits (By similarity).
CC Interacts with pilotin OutS (PubMed:23897461).
CC {ECO:0000250|UniProtKB:P45779, ECO:0000269|PubMed:23897461}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane
CC {ECO:0000250|UniProtKB:E3PJ86}. Note=Most of the protein is in the
CC periplasm which it traverses to contact proteins of the cell inner
CC membrane. {ECO:0000250|UniProtKB:P45779}.
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 N1, N2 and N3 domains each form a periplasmic ring.
CC The secretin domain forms a double beta-barrel structure; the outer
CC barrel has a diameter of about 110 Angstroms while the inner barrel
CC forms the central gate with a small pore in the closed state (By
CC similarity). The S domain interacts with pilotin OutS
CC (PubMed:23897461). {ECO:0000250|UniProtKB:P45779,
CC ECO:0000269|PubMed:23897461}.
CC -!- SIMILARITY: Belongs to the bacterial secretin family. GSP D subfamily.
CC {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; X65265; CAA46370.1; -; Genomic_DNA.
DR EMBL; CP002038; ADM99376.1; -; Genomic_DNA.
DR PIR; S28014; S28014.
DR RefSeq; WP_013318810.1; NC_014500.1.
DR PDB; 4K0U; X-ray; 2.15 A; B=693-705.
DR PDBsum; 4K0U; -.
DR AlphaFoldDB; Q01565; -.
DR SMR; Q01565; -.
DR STRING; 198628.Dda3937_02415; -.
DR PRIDE; Q01565; -.
DR EnsemblBacteria; ADM99376; ADM99376; Dda3937_02415.
DR GeneID; 9734624; -.
DR KEGG; ddd:Dda3937_02415; -.
DR PATRIC; fig|198628.6.peg.3137; -.
DR eggNOG; COG1450; Bacteria.
DR HOGENOM; CLU_006756_1_1_6; -.
DR OMA; TFNVGQE; -.
DR OrthoDB; 881521at2; -.
DR BioCyc; DDAD198628:DDA3937_RS14800-MON; -.
DR Proteomes; UP000006859; 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:0016485; P:protein processing; IMP:ASAP.
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..27
FT /evidence="ECO:0000255"
FT CHAIN 28..710
FT /note="Secretin OutD"
FT /id="PRO_0000013101"
FT REGION 28..105
FT /note="N0"
FT /evidence="ECO:0000305|PubMed:23897461"
FT REGION 123..190
FT /note="N1"
FT /evidence="ECO:0000305|PubMed:23897461"
FT REGION 192..262
FT /note="N2"
FT /evidence="ECO:0000305|PubMed:23897461"
FT REGION 288..399
FT /note="N3"
FT /evidence="ECO:0000305|PubMed:23897461"
FT REGION 289..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..648
FT /note="Secretin"
FT /evidence="ECO:0000305|PubMed:23897461"
FT REGION 691..710
FT /note="S domain"
FT /evidence="ECO:0000305|PubMed:23897461"
FT SITE 511
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 HELIX 693..704
FT /evidence="ECO:0007829|PDB:4K0U"
SQ SEQUENCE 710 AA; 76214 MW; 156E84CC50CD54FA CRC64;
MLGKGIKKSW GWLGLTVLLL GSPCGWAAEF SASFKGTDIQ EFINTVSKNL NKTVIIDPTV
RGTISVRSYD MMNEGQYYQF FLSVLDVYGF SVVPMDNGVL KVIRSKDAKS SSIPLANNEQ
PGIGDELVTR VVPLNNVAAR DLAPLLRQLN DNAGAGTVVH YEPSNVLLMT GRAAVIKRLV
DIVNTVDKTG DREMVTVPLT YASAEDVAKL VNDLNKSDEK NALPSTMLAN VVADGRTNSV
VVSGEENARQ RAVEMIRQLD RKQVVQGGTK VIYLKYAKAL DLIEVLAGNG TSGNRNSSSS
NASRPSSPRS GSSSNSNSSS GSSGSSSGSS SSSSSSSSMG FGSAFGSTSS SGGRTITIQG
KEVTVRAHDQ TNSLIITAPP DIMRDLEQVI NQLDIRRPQV LVEAIIAEIQ DADGLNLGIQ
WANKRAGMTQ FTNTGIPIST AVIGTDQFRS NGTLTTAYAS ALSSFNGVTA GFYRGNWSML
LTALSSDSKN DVLATPSIVT LDNMEATFNV GQEVPVLTGS QTTSADNIFN TVERKTVGIK
LRVKPQINEG DSVLLQIEQE VSSVADSNSS TNSSLGVTFN TRTVNNAVMV TNGETVVVGG
LLDKTSVESN DKVPLLGDIP WLGSLFRSKS QEVRKRNLML FLRPTIIRDP GQFQEASINK
YRSFNNEQQQ QRGEGNGVLD NNTLRLSGGN TYTFRQVQSS ISDFYKPEGR
