ID   GSPD_AERHY              Reviewed;         678 AA.
AC   P31780;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Secretin ExeD;
DE   AltName: Full=General secretion pathway protein D;
DE   AltName: Full=Type II secretion system protein D;
DE            Short=T2SS protein D;
DE   Flags: Precursor;
GN   Name=exeD;
OS   Aeromonas hydrophila.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=644;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Ah65;
RA   Howard S.P.;
RL   Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 408-678.
RC   STRAIN=Ah65;
RX   PubMed=1640836; DOI=10.1111/j.1365-2958.1992.tb00856.x;
RA   Jiang B., Howard S.P.;
RT   "The Aeromonas hydrophila exeE gene, required both for protein secretion
RT   and normal outer membrane biogenesis, is a member of a general secretion
RT   pathway.";
RL   Mol. Microbiol. 6:1351-1361(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). This subunit forms the outer membrane channel (By
CC       similarity). {ECO:0000250|UniProtKB:E3PJ86,
CC       ECO:0000250|UniProtKB:P45779}.
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; X66504; CAA47124.1; -; Genomic_DNA.
DR   PIR; S22668; S22668.
DR   PDB; 6I1X; EM; 3.70 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O=122-645.
DR   PDBsum; 6I1X; -.
DR   AlphaFoldDB; P31780; -.
DR   SMR; P31780; -.
DR   STRING; 1448139.AI20_16530; -.
DR   PRIDE; P31780; -.
DR   eggNOG; COG1450; Bacteria.
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   1: Evidence at protein level;
KW   3D-structure; Cell outer membrane; Membrane; Protein transport; Signal;
KW   Transmembrane; Transmembrane beta strand; Transport.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..678
FT                   /note="Secretin ExeD"
FT                   /id="PRO_0000013097"
FT   REGION          26..122
FT                   /note="N0"
FT                   /evidence="ECO:0000250|UniProtKB:P45779"
FT   REGION          124..188
FT                   /note="N1"
FT                   /evidence="ECO:0000250|UniProtKB:P45779"
FT   REGION          189..264
FT                   /note="N2"
FT                   /evidence="ECO:0000250|UniProtKB:P45779"
FT   REGION          267..348
FT                   /note="N3"
FT                   /evidence="ECO:0000250|UniProtKB:P45779"
FT   REGION          353..602
FT                   /note="Secretin"
FT                   /evidence="ECO:0000250|UniProtKB:P45779"
FT   REGION          604..678
FT                   /note="S domain"
FT                   /evidence="ECO:0000250|UniProtKB:P45779"
FT   SITE            464
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   678 AA;  72451 MW;  43B33A28861B0238 CRC64;
     MINKGKGWRL ATVAAALMMA GSAWATEYSA SFKNADIEEF INTVGKNLSK TIIIEPSVRG
     KINVRSYDLL NEEQYYQFFL SVLDVYGFAV VPMDNGVLKV VRSKDAKTSA IPVVDETNPG
     IGDEMVTRVV PVRNVSVREL APLLRQLNDN AGGGNVVHYD PSNVLLITGR AAVVNRLVEV
     VRRVDKAGDQ EVDIIKLKYA SAGEMVRLVT NLNKDGNSQG GNTSLLLAPK VVADERTNSV
     VVSGEPKARA RIIQMVRQLD RDLQSQGNTR VFYLKYGKAK DMVEVLKGVS SSIEADKKGG
     GTATTAGGGA SIGGGKLAIS ADETTNALVI TAQPDVMAEL EQVVAKLDIR RAQVLVEAII
     VEIADGDGLN LGVQWANTNG GGTQFTNAGP GIGSVAIAAK DYKDNGTTTG LAKLAENFNG
     MAAGFYQGNW AMLVTALSTN TKSDILSTPS IVTMDNKEAS FNVGQEVPVQ TGTQNSTSGD
     TTFSTIERKT VGTKLVVTPQ INEGDSVLLT IEQEVSSVGK QATGTDGLGP TFDTRTVKNA
     VLVKSGETVV LGGLMDEQTK EEVSKVPLLG DIPVLGYLFR STSNNTSKRN LMVFIRPTIL
     RDANVYSGIS SNKYTLFRAQ QLDAVAQEGY ATSPDRQVLP EYGQDVTMSP EAQKQIELMK
     THQQATADGV QPFVQGNK