ID   GSPD_AERSA              Reviewed;         678 AA.
AC   P45778;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 87.
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 salmonicida.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=645;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 33658 / DSM 19634 / JCM 7874 / NCIMB 1102 / NCTC 12959;
RX   PubMed=7789814; DOI=10.1016/0378-1119(95)00139-w;
RA   Karlyshev A.V., Macintyre S.;
RT   "Cloning and study of the genetic organization of the exe gene cluster of
RT   Aeromonas salmonicida.";
RL   Gene 158:77-82(1995).
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; X80505; CAA56668.1; -; Genomic_DNA.
DR   PIR; I39678; S46963.
DR   RefSeq; WP_005315865.1; NZ_UFSF01000001.1.
DR   AlphaFoldDB; P45778; -.
DR   SMR; P45778; -.
DR   STRING; 1233098.GCA_000315855_00772; -.
DR   PRIDE; P45778; -.
DR   OMA; TFNVGQE; -.
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..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..678
FT                   /note="Secretin ExeD"
FT                   /id="PRO_0000013098"
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..347
FT                   /note="N3"
FT                   /evidence="ECO:0000250|UniProtKB:P45779"
FT   REGION          352..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            463
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;  72768 MW;  CB4921C9BAA8438E CRC64;
     MINKGKSWRL ATVAAALMMA GSAWATEYSA SFKNADIEEF INTVGKNLSK TIIIEPSVRG
     KINVRSYDLL NEEQYYQFFL SVLDVYGFAV VPMDNGVLKV VRSKDAKTSA IPVVDETNPG
     IGDEMVTRVV PVRNVSVREL APLLRQLNDN AGGGNVVHYD PSNVLLITGR AAVVNRLVEV
     VRRVDKAGDQ EVDIIKLRYA SAGEMVRLVT NLNKDGNTQG GNTSLLLAPK VVADERTNSV
     VVSGEPKARA RIIQMVRQLD RDLQSQGNTR VFYLKYGKAK DMVEVLKGVS TSIEADKKGG
     GTTAGGGNAS IGGGKLAISA DETTNALVIT AQPDVMAELE QVVAKLDIRR AQVLVEAIIV
     EIADGDGLNL GVQWANTNGG GTQFTDTNLP IGSVAIAAKD YNENGTTTGL ADLAKGFNGM
     AAGFYHGNWA ALVTALSTST KSDILSTPSI VTMDNKEASF NVGQEVPVQS GSQSSTTSDQ
     VFNTIERKTV GTKLTVTPQI NEGDSVLLNI EQEVSSVAQK QATGTADLGP TFDTRTIKNA
     VLVKSGETVV LGGLMDEQTQ EKVSKVPLLG DIPVLGYLFR STNNTTSKRN LMVFIRPTIL
     RDAHVYSGIS SNKYTMFRAE QLDAAAQESY LTSPKRQVLP EYGQDVAQSP EVQKQIELMK
     ARQQATADGA QPFVQGNK