GSPD_PECCC
ID GSPD_PECCC Reviewed; 650 AA.
AC P31701;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 25-MAY-2022, entry version 88.
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 Pectobacterium carotovorum subsp. carotovorum (Erwinia carotovora subsp.
OS carotovora).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Pectobacterium.
OX NCBI_TaxID=555;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SCRI 193;
RX PubMed=8326859; DOI=10.1111/j.1365-2958.1993.tb01589.x;
RA Reeves P.J., Whitcombe D., Wharam S., Gibson M., Allison G., Bunce N.,
RA Barallon R., Douglas P., Mulholland V., Stevens S., Walker S.,
RA Salmond G.P.C.;
RT "Molecular cloning and characterization of 13 out genes from Erwinia
RT carotovora subspecies carotovora: genes encoding members of a general
RT secretion pathway (GSP) widespread in Gram-negative bacteria.";
RL Mol. Microbiol. 8:443-456(1993).
RN [2]
RP IDENTIFICATION OF PROBABLE FRAMESHIFT.
RA Bairoch A.;
RL Unpublished observations (FEB-1997).
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:8326859}.
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; X70049; CAA49645.1; -; Genomic_DNA.
DR PIR; S32858; S32858.
DR AlphaFoldDB; P31701; -.
DR SMR; P31701; -.
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; 2.
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..18
FT /evidence="ECO:0000255"
FT CHAIN 19..650
FT /note="Secretin OutD"
FT /id="PRO_0000013102"
FT REGION 20..115
FT /note="N0"
FT /evidence="ECO:0000250|UniProtKB:P45779"
FT REGION 117..181
FT /note="N1"
FT /evidence="ECO:0000250|UniProtKB:P45779"
FT REGION 182..255
FT /note="N2"
FT /evidence="ECO:0000250|UniProtKB:P45779"
FT REGION 258..330
FT /note="N3"
FT /evidence="ECO:0000250|UniProtKB:P45779"
FT REGION 335..585
FT /note="Secretin"
FT /evidence="ECO:0000250|UniProtKB:P45779"
FT REGION 587..650
FT /note="S domain"
FT /evidence="ECO:0000250|UniProtKB:P45779"
FT SITE 447
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 CONFLICT 139..164
FT /note="ELNDNAWRGTCGDYEPANVVVMTGRA -> VERQRVAWDVWRLRTCERRRDD
FT WPR (in Ref. 1; CAA49645)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 650 AA; 70144 MW; 9A228C369B0E2AFC CRC64;
MLLLSGSVLL MASSLAWSAE FSASFKGTDI QEFINTVSKN LNKTVIIDPS VSGTITVRSY
DMMNEEQYYQ FFLSVLDVYG FTVIPMDNNV LKIIRSKDAK STSMPLATDR QPGIGDEVVT
RVVPVNNVAA RDFGRSSREL NDNAWRGTCG DYEPANVVVM TGRAGVIHAV MTIVERVDQT
GDRNVTTIPL SYASSTEVVK MVNELNKMDE KSALPGMLTA NVVADERTNS AAGFGEPNSR
QRVIDMVKQL DRQQAVQGNT KVIYLKYAKA ADLVEVLTGV GDSIQTDQQN ALPALRKDIS
IKAHEQTNSL IVNAAPDIMR DLEQVIAQLD IRRPQVLVEA IIAEVQDADG MNLGVQWANK
NAGVTQFTNT GLPITTMMAG ADQFRRDGTL GTAATTALGG FNGIAAGFYQ GNWGMLMTAL
SSNSKNDILA TPSIVTLDNM EATFNVGQEV PVLAGSQTTS GDNVFQTVER KTVGIKLKVK
PQINEGDSVL LEIEQEVSSV ADAASSSSTN LGATFNTRTV NNAVLVSSGD TVVVGGLLDK
STNESANKVP LLGDIPVLGY LFRSNSTETK KRNLMLFIRP SIIRDRSQFQ SASASKYHSF
SAEENKQRNV SNGEGGLLDN DLLRLPEGGN AYTFRQVQSS IVAFYPAGGK
