GSPD_KLEPN
ID GSPD_KLEPN Reviewed; 660 AA.
AC P15644;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=Secretin PulD;
DE AltName: Full=General secretion pathway protein D;
DE AltName: Full=Pullulanase secretion envelope PulD;
DE AltName: Full=Type II secretion system protein D;
DE Short=T2SS protein D;
DE Flags: Precursor;
GN Name=pulD;
OS Klebsiella pneumoniae.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=573;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 28-42, FUNCTION, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=UNF5023;
RX PubMed=2677007; DOI=10.1016/s0021-9258(18)71517-2;
RA D'Enfert C., Reyss I., Wandersman C., Pugsley A.P.;
RT "Protein secretion by Gram-negative bacteria. Characterization of two
RT membrane proteins required for pullulanase secretion by Escherichia coli K-
RT 12.";
RL J. Biol. Chem. 264:17462-17468(1989).
CC -!- FUNCTION: Involved in a type II secretion system (T2SS, formerly
CC general secretion pathway, GSP) for the export of proteins. Required
CC for the translocation of pullulanase (PubMed:2677007). This subunit
CC forms the outer membrane channel (By similarity).
CC {ECO:0000250|UniProtKB:P45779, ECO:0000269|PubMed:2677007}.
CC -!- SUBUNIT: Forms a cylindrical channel with 15 subunits.
CC {ECO:0000250|UniProtKB:P45779}.
CC -!- INTERACTION:
CC P15644; P15644: pulD; NbExp=2; IntAct=EBI-7074093, EBI-7074093;
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000269|PubMed:2677007}.
CC Note=Most of the protein is in the periplasm which it traverses to
CC contact proteins of the cell inner membrane.
CC {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}.
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; M32613; AAA25126.2; -; Genomic_DNA.
DR PIR; B34469; B34469.
DR AlphaFoldDB; P15644; -.
DR SMR; P15644; -.
DR MINT; P15644; -.
DR TCDB; 1.B.22.1.1; the outer bacterial membrane secretin (secretin) family.
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:0042802; F:identical protein binding; IPI:IntAct.
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 Cell outer membrane; Direct protein sequencing; Membrane;
KW Protein transport; Signal; Transmembrane; Transmembrane beta strand;
KW Transport.
FT SIGNAL 1..27
FT /evidence="ECO:0000269|PubMed:2677007"
FT CHAIN 28..660
FT /note="Secretin PulD"
FT /id="PRO_0000013103"
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..341
FT /note="N3"
FT /evidence="ECO:0000250|UniProtKB:P45779"
FT REGION 346..596
FT /note="Secretin"
FT /evidence="ECO:0000250|UniProtKB:P45779"
FT REGION 598..660
FT /note="S domain"
FT /evidence="ECO:0000250|UniProtKB:P45779"
FT SITE 458
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 660 AA; 70658 MW; DE25D7C924B85F00 CRC64;
MIIANVIRSF SLTLLIFAAL LFRPAAAEEF SASFKGTDIQ EFINTVSKNL NKTVIIDPSV
RGTITVRSYD MLNEEQYYQF FLSVLDVYGF AVINMNNGVL KVVRSKDAKT AAVPVASDAA
PGIGDEVVTR VVPLTNVAAR DLAPLLRQLN DNAGVGSVVH YEPSNVLLMT GRAAVIKRLL
TIVERVDNAG DRSVVTVPLS WASAADVVKL VTELNKDTSK SALPGSMVAN VVADERTNAV
LVSGEPNSRQ RIIAMIKQLD RQQATQGNTK VIYLKYAKAS DLVEVLTGIS STMQSEKQAA
KPVAALDKNI IIKAHGQTNA LIVTAAPDVM NDLERVIAQL DIRRPQVLVE AIIAEVQDAD
GLNLGIQWAN KNAGMTQFTN SGLPISTAIA GANQYNKDGT VSSSLASALS SFNGIAAGFY
QGNWAMLLTA LSSSTKNDIL ATPSIVTLDN MEATFNVGQE VPVLTGSQTT SGDNIFNTVE
RKTVGIKLKV KPQINEGDSV LLEIEQEVSS VADAASSTSS DLGATFNTRT VNNAVLVGSG
ETVVVGGLLD KSVSDTADKV PLLGDIPVIG ALFRSTSKKV SKRNLMLFIR PTVIRDRDEY
RQASSGQYTA FNDAQSKQRG KENNDAMLNQ DLLEIYPRQD TAAFRQVSAA IDAFNLGGNL
