GSPD_ECOLI
ID GSPD_ECOLI Reviewed; 650 AA.
AC P45758; Q2M6Z0;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2001, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Putative secretin GspD {ECO:0000303|PubMed:28067918};
DE AltName: Full=Putative general secretion pathway protein D;
DE AltName: Full=Putative type II secretion system protein D;
DE Short=T2SS protein D;
DE Flags: Precursor;
GN Name=gspD; Synonyms=yheF; OrderedLocusNames=b3325, JW5707;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [3]
RP LACK OF EXPRESSION.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=8655552; DOI=10.1128/jb.178.12.3544-3549.1996;
RA Francetic O., Pugsley A.P.;
RT "The cryptic general secretory pathway (gsp) operon of Escherichia coli K-
RT 12 encodes functional proteins.";
RL J. Bacteriol. 178:3544-3549(1996).
RN [4]
RP LACK OF EXPRESSION, AND TRANSCRIPTIONAL REGULATION.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=11118204; DOI=10.1093/emboj/19.24.6697;
RA Francetic O., Belin D., Badaut C., Pugsley A.P.;
RT "Expression of the endogenous type II secretion pathway in Escherichia coli
RT leads to chitinase secretion.";
RL EMBO J. 19:6697-6703(2000).
RN [5] {ECO:0007744|PDB:5WQ7}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.04 ANGSTROMS) OF 24-650, SUBCELLULAR
RP LOCATION, AND DOMAIN.
RC STRAIN=K12 / DH5-alpha;
RX PubMed=28067918; DOI=10.1038/nsmb.3350;
RA Yan Z., Yin M., Xu D., Zhu Y., Li X.;
RT "Structural insights into the secretin translocation channel in the type II
RT secretion system.";
RL Nat. Struct. Mol. Biol. 24:177-183(2017).
CC -!- FUNCTION: Involved in a type II secretion system (T2SS, formerly
CC general secretion pathway, GSP) for the export of folded proteins
CC across the outer membrane. This subunit would form the outer membrane
CC channel. {ECO:0000250|UniProtKB:E3PJ86}.
CC -!- SUBUNIT: Forms a cylindrical channel with 15 subunits; approximately
CC 25% of the particles have 16-subunit channels. Closed pentadeacameric
CC channels are 180 Angstroms long and 145 Angstroms in diameter. Each
CC subunit turns in a clock-wise manner around the channel.
CC {ECO:0000269|PubMed:28067918}.
CC -!- INTERACTION:
CC P45758; P45758: gspD; NbExp=3; IntAct=EBI-21225187, EBI-21225187;
CC -!- SUBCELLULAR LOCATION: Cell outer membrane
CC {ECO:0000305|PubMed:28067918}. Note=Most of the protein is in the
CC periplasm which it traverses to contact proteins of the cell inner
CC membrane. {ECO:0000305|PubMed:28067918}.
CC -!- INDUCTION: Silenced by the DNA-binding protein H-NS under standard
CC growth conditions. {ECO:0000269|PubMed:11118204}.
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 N0 domain was present but not resolved by electron microscopy. The
CC secretin domain forms a double beta-barrel structure; the outer barrel
CC has a diameter of about 110 Angstroms while the inner barrel forms the
CC central gate with a small pore in the closed state.
CC {ECO:0000269|PubMed:28067918}.
CC -!- MISCELLANEOUS: Part of a cryptic operon that encodes proteins involved
CC in type II secretion machinery in other organisms, but is not expressed
CC in strain K12.
CC -!- SIMILARITY: Belongs to the bacterial secretin family. GSP D subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA58122.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U18997; AAA58122.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC76350.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE77966.1; -; Genomic_DNA.
DR PIR; H65125; H65125.
DR RefSeq; NP_417784.4; NC_000913.3.
DR RefSeq; WP_001326512.1; NZ_SSZK01000040.1.
DR PDB; 5WQ7; EM; 3.04 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O=24-650.
DR PDBsum; 5WQ7; -.
DR AlphaFoldDB; P45758; -.
DR SMR; P45758; -.
DR BioGRID; 4261297; 269.
DR STRING; 511145.b3325; -.
DR TCDB; 1.B.22.1.3; the outer bacterial membrane secretin (secretin) family.
DR PaxDb; P45758; -.
DR PRIDE; P45758; -.
DR EnsemblBacteria; AAC76350; AAC76350; b3325.
DR EnsemblBacteria; BAE77966; BAE77966; BAE77966.
DR GeneID; 947822; -.
DR KEGG; ecj:JW5707; -.
DR KEGG; eco:b3325; -.
DR PATRIC; fig|1411691.4.peg.3406; -.
DR EchoBASE; EB2727; -.
DR eggNOG; COG1450; Bacteria.
DR HOGENOM; CLU_006756_1_1_6; -.
DR InParanoid; P45758; -.
DR OMA; TFNVGQE; -.
DR PhylomeDB; P45758; -.
DR BioCyc; EcoCyc:G7703-MON; -.
DR BioCyc; MetaCyc:G7703-MON; -.
DR PRO; PR:P45758; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
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; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0009306; P:protein secretion; IBA:GO_Central.
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;
KW Reference proteome; Signal; Transmembrane; Transmembrane beta strand;
KW Transport.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..650
FT /note="Putative secretin GspD"
FT /id="PRO_0000013099"
FT REGION 24..122
FT /note="N0"
FT /evidence="ECO:0000305|PubMed:28067918"
FT REGION 124..188
FT /note="N1"
FT /evidence="ECO:0000305|PubMed:28067918"
FT REGION 189..263
FT /note="N2"
FT /evidence="ECO:0000305|PubMed:28067918"
FT REGION 266..342
FT /note="N3"
FT /evidence="ECO:0000305|PubMed:28067918"
FT REGION 345..596
FT /note="Secretin"
FT /evidence="ECO:0000305|PubMed:28067918"
FT REGION 598..650
FT /note="S domain"
FT /evidence="ECO:0000305|PubMed:28067918"
FT SITE 461
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 STRAND 126..131
FT /evidence="ECO:0007829|PDB:5WQ7"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:5WQ7"
FT HELIX 137..140
FT /evidence="ECO:0007829|PDB:5WQ7"
FT HELIX 141..148
FT /evidence="ECO:0007829|PDB:5WQ7"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:5WQ7"
FT STRAND 156..159
FT /evidence="ECO:0007829|PDB:5WQ7"
FT STRAND 164..169
FT /evidence="ECO:0007829|PDB:5WQ7"
FT HELIX 171..186
FT /evidence="ECO:0007829|PDB:5WQ7"
FT STRAND 193..196
FT /evidence="ECO:0007829|PDB:5WQ7"
FT HELIX 202..210
FT /evidence="ECO:0007829|PDB:5WQ7"
FT STRAND 230..232
FT /evidence="ECO:0007829|PDB:5WQ7"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:5WQ7"
FT STRAND 238..241
FT /evidence="ECO:0007829|PDB:5WQ7"
FT HELIX 245..257
FT /evidence="ECO:0007829|PDB:5WQ7"
FT STRAND 267..272
FT /evidence="ECO:0007829|PDB:5WQ7"
FT STRAND 274..276
FT /evidence="ECO:0007829|PDB:5WQ7"
FT HELIX 278..289
FT /evidence="ECO:0007829|PDB:5WQ7"
FT STRAND 312..316
FT /evidence="ECO:0007829|PDB:5WQ7"
FT TURN 317..320
FT /evidence="ECO:0007829|PDB:5WQ7"
FT STRAND 321..325
FT /evidence="ECO:0007829|PDB:5WQ7"
FT HELIX 328..341
FT /evidence="ECO:0007829|PDB:5WQ7"
FT STRAND 347..371
FT /evidence="ECO:0007829|PDB:5WQ7"
FT TURN 372..374
FT /evidence="ECO:0007829|PDB:5WQ7"
FT STRAND 375..378
FT /evidence="ECO:0007829|PDB:5WQ7"
FT STRAND 382..384
FT /evidence="ECO:0007829|PDB:5WQ7"
FT HELIX 386..399
FT /evidence="ECO:0007829|PDB:5WQ7"
FT HELIX 409..413
FT /evidence="ECO:0007829|PDB:5WQ7"
FT STRAND 417..424
FT /evidence="ECO:0007829|PDB:5WQ7"
FT STRAND 427..451
FT /evidence="ECO:0007829|PDB:5WQ7"
FT STRAND 456..467
FT /evidence="ECO:0007829|PDB:5WQ7"
FT STRAND 482..496
FT /evidence="ECO:0007829|PDB:5WQ7"
FT STRAND 499..501
FT /evidence="ECO:0007829|PDB:5WQ7"
FT STRAND 504..514
FT /evidence="ECO:0007829|PDB:5WQ7"
FT STRAND 516..518
FT /evidence="ECO:0007829|PDB:5WQ7"
FT STRAND 526..536
FT /evidence="ECO:0007829|PDB:5WQ7"
FT STRAND 543..559
FT /evidence="ECO:0007829|PDB:5WQ7"
FT HELIX 563..565
FT /evidence="ECO:0007829|PDB:5WQ7"
FT HELIX 569..572
FT /evidence="ECO:0007829|PDB:5WQ7"
FT STRAND 575..594
FT /evidence="ECO:0007829|PDB:5WQ7"
FT HELIX 597..621
FT /evidence="ECO:0007829|PDB:5WQ7"
SQ SEQUENCE 650 AA; 70698 MW; 973259A12A7237B2 CRC64;
MKGLNKITCC LLAALLMPCA GHAENEQYGA NFNNADIRQF VEIVGQHLGK TILIDPSVQG
TISVRSNDTF SQQEYYQFFL SILDLYGYSV ITLDNGFLKV VRSANVKTSP GMIADSSRPG
VGDELVTRIV PLENVPARDL APLLRQMMDA GSVGNVVHYE PSNVLILTGR ASTINKLIEV
IKRVDVIGTE KQQIIHLEYA SAEDLAEILN QLISESHGKS QMPALLSAKI VADKRTNSLI
ISGPEKARQR ITSLLKSLDV EESEEGNTRV YYLKYAKATN LVEVLTGVSE KLKDEKGNAR
KPSSSGAMDN VAITADEQTN SLVITADQSV QEKLATVIAR LDIRRAQVLV EAIIVEVQDG
NGLNLGVQWA NKNVGAQQFT NTGLPIFNAA QGVADYKKNG GITSANPAWD MFSAYNGMAA
GFFNGDWGVL LTALASNNKN DILATPSIVT LDNKLASFNV GQDVPVLSGS QTTSGDNVFN
TVERKTVGTK LKVTPQVNEG DAVLLEIEQE VSSVDSSSNS TLGPTFNTRT IQNAVLVKTG
ETVVLGGLLD DFSKEQVSKV PLLGDIPLVG QLFRYTSTER AKRNLMVFIR PTIIRDDDVY
RSLSKEKYTR YRQEQQQRID GKSKALVGSE DLPVLDENTF NSHAPAPSSR
