ID   GSPD1_DICCH             Reviewed;         712 AA.
AC   P31700;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   25-MAY-2022, entry version 81.
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;
OS   Dickeya chrysanthemi (Pectobacterium chrysanthemi) (Erwinia chrysanthemi).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Dickeya.
OX   NCBI_TaxID=556;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=EC16;
RX   PubMed=1429461; DOI=10.1128/jb.174.22.7385-7397.1992;
RA   Lindeberg M., Collmer A.;
RT   "Analysis of eight out genes in a cluster required for pectic enzyme
RT   secretion by Erwinia chrysanthemi: sequence comparison with secretion genes
RT   from other Gram-negative bacteria.";
RL   J. Bacteriol. 174:7385-7397(1992).
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:1429461}.
CC   -!- SUBUNIT: Forms a cylindrical channel with 15 subunits.
CC       {ECO:0000250|UniProtKB:P45779}.
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.
CC       {ECO:0000250|UniProtKB:P45779}.
CC   -!- SIMILARITY: Belongs to the bacterial secretin family. GSP D subfamily.
CC       {ECO:0000305}.
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DR   EMBL; L02214; AAA24831.1; -; Genomic_DNA.
DR   PIR; B47021; B47021.
DR   AlphaFoldDB; P31700; -.
DR   SMR; P31700; -.
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   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   3: Inferred from homology;
KW   Cell outer membrane; Membrane; Protein transport; Signal; Transmembrane;
KW   Transmembrane beta strand; Transport.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..712
FT                   /note="Secretin OutD"
FT                   /id="PRO_0000013100"
FT   REGION          28..124
FT                   /note="N0"
FT                   /evidence="ECO:0000250|UniProtKB:P45779"
FT   REGION          126..190
FT                   /note="N1"
FT                   /evidence="ECO:0000250|UniProtKB:P45779"
FT   REGION          191..264
FT                   /note="N2"
FT                   /evidence="ECO:0000250|UniProtKB:P45779"
FT   REGION          267..394
FT                   /note="N3"
FT                   /evidence="ECO:0000250|UniProtKB:P45779"
FT   REGION          288..342
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          399..651
FT                   /note="Secretin"
FT                   /evidence="ECO:0000250|UniProtKB:P45779"
FT   REGION          653..712
FT                   /note="S domain"
FT                   /evidence="ECO:0000250|UniProtKB:P45779"
FT   COMPBIAS        289..342
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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"
SQ   SEQUENCE   712 AA;  76479 MW;  8A065D9ADAE24888 CRC64;
     MLGKGIKKSW GWLGLTVLLL GSPCGWAAEF SASFKGTDIQ EFINTVSKNL NKTVIIDPTV
     RGTISVRSYD MMDEGQYYQF FLSVLDVYGF SVVPMDNGVL KVIRSKDAKS SSIPLANNEQ
     PGVGDELVTR VVPLNNVAAR DLAPLLRQLN DNAGAGTVVH YEPSNVLLMT GRAAVIKRLV
     DIVNTVDKTG DREMITVSLN YASAEDVAKL VNDLNKTDEK NALPSTMLAN VVADGRTNSV
     VVSGEENTSP CAVEMIRQLD RKQVAQGGTK VIYLKYAKAL DLIEVLAGNG TSGNRNSSST
     NSSRPSSTRS SSTLNNSNSS SSGSSSGSGS SSSSSSSSMG FGSAFGSANS SGGRTIVIQG
     KEVTVRAHDQ TNSLIITRPP DIMRDLEQVI NQLDIRRPQV LVEAIIAEIQ DADGLNLGIQ
     WANKRAGMTQ FTNTGIPIST AMIGTDQFRS DGTLTTAYAS ALSNFNGITA GFYRGNWSML
     LTALSSDGKN DVLATPSIVT LDNMEATFNV GQEVPVLTGS QTTVGSGDNI FNTVERKTVG
     IKLRVKPQIN EGDSVLLQIE QEVSSVAEGN GSSNSSLGVT FNTRTVNNAV MVTNRETVVV
     GGLLDKTAIE TNNKVPLLGD IPWLGSLFRS KTQTMSKRNL MLFLRPTIIR DPQQYQQASI
     SKYNSFNNEQ QQQRGQGNSV LDNNTLRLSG GNTYTFRQVQ SSISAFYQPE GR