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Escherichia coli K-12 substr. MG1655 Polypeptide: putative protein secretion protein for export



Gene: gspD Accession Numbers: G7703 (EcoCyc), b3325, ECK3312

Synonyms: yheF

Regulation Summary Diagram: ?

Component of: GspC-O secreton complex (extended summary available)

Summary:
In Escherichia coli, gspD is a member of an operon of genes (gspC-O) which are not normally expressed [Francetic00] but are homologous to those encoding the secreton, or type II secretion machinery in Klebsiella oxytoca and Aeromonase hydrophila, among others [Francetic96]. GspD belongs to a large family of homologous proteins called secretins, some of which are also involved in type III, type IV and filamentous phage extrusion [Genin94]. 12-14 subunits of GspD are thought to form an oligomeric pore in the outer membrane [Bitter98, Kazmierczak94, Hardie96]. The C-terminal outer membrane domain is conserved among secretins while the N-terminus is variable and may interact with other secretion apparatus components in the periplasm [Sandkvist01].

gspD is not required for spontaneous plasmid transformation on nutrient plates with high agar concentration [Sun09a].

Locations: outer membrane

Map Position: [3,454,399 -> 3,456,351] (74.45 centisomes)
Length: 1953 bp / 650 aa

Molecular Weight of Polypeptide: 70.698 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0010879 , EchoBASE:EB2727 , EcoGene:EG12890 , EcoliWiki:b3325 , OU-Microarray:b3325 , PortEco:gspD , Protein Model Portal:P45758 , RefSeq:NP_417784 , RegulonDB:G7703 , SMR:P45758 , String:511145.b3325 , UniProt:P45758

Relationship Links: EcoO157Cyc:Homolog:ESCC , EcoO157Cyc:Homolog:ESCC-MONOMER , EcoO157Cyc:Homolog:Z4197 , EcoO157Cyc:Homolog:Z4197-MONOMER , InterPro:IN-FAMILY:IPR001775 , InterPro:IN-FAMILY:IPR004845 , InterPro:IN-FAMILY:IPR004846 , InterPro:IN-FAMILY:IPR005644 , InterPro:IN-FAMILY:IPR013356 , Pfam:IN-FAMILY:PF00263 , Pfam:IN-FAMILY:PF03958 , Prints:IN-FAMILY:PR00811 , Prosite:IN-FAMILY:PS00875

In Paralogous Gene Group: 517 (2 members)

Gene-Reaction Schematic: ?

Genetic Regulation Schematic: ?

GO Terms:

Biological Process: GO:0006810 - transport Inferred by computational analysis [UniProtGOA11]
GO:0009306 - protein secretion Inferred by computational analysis [GOA01]
GO:0015031 - protein transport Inferred by computational analysis [UniProtGOA11]
GO:0015628 - protein secretion by the type II secretion system Inferred by computational analysis [GOA01]
Molecular Function: GO:0008565 - protein transporter activity Inferred by computational analysis [GOA01]
Cellular Component: GO:0009279 - cell outer membrane Inferred by computational analysis [UniProtGOA11a, UniProtGOA11, DiazMejia09]
GO:0015627 - type II protein secretion system complex Inferred by computational analysis [GOA01]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11]
GO:0019867 - outer membrane Inferred by computational analysis [GOA01]

MultiFun Terms: All-Genes Pseudo-Genes Cryptic-Genes
MultiFun transport Putative uncharacterized transport protein

Essentiality data for gspD knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 1]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 2]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 1]

Subunit of: GspC-O secreton complex

Subunit composition of GspC-O secreton complex = [GspC][GspD][GspE][GspF][GspG][GspH][GspI][GspJ][GspK][GspL][GspM][GspO]
         putative protein secretion protein for export = GspC (summary available)
         putative protein secretion protein for export = GspD (summary available)
         putative protein secretion protein for export = GspE (extended summary available)
         putative protein secretion protein for export = GspF (summary available)
         putative protein secretion protein for export = GspG (summary available)
         putative protein secretion protein for export = GspH (summary available)
         putative protein secretion protein for export = GspI (summary available)
         putative protein secretion protein for export = GspJ (summary available)
         putative protein secretion protein for export = GspK (summary available)
         putative protein secretion protein for export = GspL (summary available)
         putative protein secretion protein = GspM (summary available)
         leader peptidase, integral membrane protein = GspO (extended summary available)

Summary:
GspC-O, the type II secretion or secreton complex in Escherichia coli has also been known as the general secretory pathway (GSP) for the export of proteins across the outer membranes of gram-negative bacteria [Pugsley93]. Translocation across the cytoplasmic membrane prior to secreton-dependent secretion can take place via the signal peptide-dependent Sec pathway or the twin-arginine translocation (TAT) system [Voulhoux01]. After transport across the outer membrane, the translocated proteins may be either released into the medium or stay attached to the outer membrane and assembled into surface organelles [Pugsley93, Pugsley98]. The secreton facilitates the extrusion of folded proteins through a putative large gated pore in the outer membrane [Pugsley93]. Although Escherichia coli K-12 does not secrete endogenous proteins, the gsp genes of E. coli are orthologs of those in other secretons [Francetic96], including those of the pullulanase (pul) secretion pathway of Klebsiella oxytoca. The pulO gene product has been shown to be an enzyme required for processing of PulG as well as PulH, PulI and PulJ [Pugsley93a, Strom94]. Complementation studies have shown that the pulO homolog, gspO, is capable of complementing the processing function in a pulO deletion mutant [Francetic96]. The pulG homolog, gspG, has been shown to be capable of complementing a pulG mutation when expressed under the control of a lac promoter [Francetic96]. Transcription of the gspC-O operon was shown to be silenced in wild-type E. coli K-12 by the nucleoid structuring protein H-NS. Deletion mutants lacking H-NS and with the gsp genes present on a multiple-copy-number plasmid have been shown to express the secreton genes and promote the efficient secretion of the co-regulated endochitinase ChiA [Francetic00]. Expression of gspC-O also resulted in formation of pili composed of the GspG pseudopilin when extra copies of gspG were supplied on a second plasmid [Vignon03].


Sequence Features

Feature Class Location Citations Comment
Signal-Sequence 1 -> 23
[UniProt10a]
UniProt: Non-Experimental Qualifier: potential;
Chain 24 -> 650
[UniProt09]
UniProt: Probable general secretion pathway protein D;


Gene Local Context (not to scale): ?

Transcription Units:

Notes:

History:
Peter D. Karp on Wed Jan 18, 2006:
Gene left-end position adjusted based on analysis performed in the 2005 E. coli annotation update [Riley06 ].
Markus Krummenacker on Tue Oct 14, 1997:
Gene object created from Blattner lab Genbank (v. M52) entry.


References

Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

Bitter98: Bitter W, Koster M, Latijnhouwers M, de Cock H, Tommassen J (1998). "Formation of oligomeric rings by XcpQ and PilQ, which are involved in protein transport across the outer membrane of Pseudomonas aeruginosa." Mol Microbiol 27(1);209-19. PMID: 9466268

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

Francetic00: Francetic O, Belin D, Badaut C, Pugsley AP (2000). "Expression of the endogenous type II secretion pathway in Escherichia coli leads to chitinase secretion." EMBO J 19(24);6697-703. PMID: 11118204

Francetic96: Francetic O, Pugsley AP (1996). "The cryptic general secretory pathway (gsp) operon of Escherichia coli K-12 encodes functional proteins." J Bacteriol 178(12);3544-9. PMID: 8655552

Genin94: Genin S, Boucher CA (1994). "A superfamily of proteins involved in different secretion pathways in gram-negative bacteria: modular structure and specificity of the N-terminal domain." Mol Gen Genet 243(1);112-8. PMID: 8190064

GOA01: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

Hardie96: Hardie KR, Lory S, Pugsley AP (1996). "Insertion of an outer membrane protein in Escherichia coli requires a chaperone-like protein." EMBO J 15(5);978-88. PMID: 8605893

Joyce06: Joyce AR, Reed JL, White A, Edwards R, Osterman A, Baba T, Mori H, Lesely SA, Palsson BO, Agarwalla S (2006). "Experimental and computational assessment of conditionally essential genes in Escherichia coli." J Bacteriol 188(23);8259-71. PMID: 17012394

Kazmierczak94: Kazmierczak BI, Mielke DL, Russel M, Model P (1994). "pIV, a filamentous phage protein that mediates phage export across the bacterial cell envelope, forms a multimer." J Mol Biol 238(2);187-98. PMID: 8158648

Pugsley93: Pugsley AP (1993). "The complete general secretory pathway in gram-negative bacteria." Microbiol Rev 57(1);50-108. PMID: 8096622

Pugsley93a: Pugsley AP (1993). "Processing and methylation of PuIG, a pilin-like component of the general secretory pathway of Klebsiella oxytoca." Mol Microbiol 9(2);295-308. PMID: 8412682

Pugsley98: Pugsley AP, Francetic O (1998). "Protein secretion in Escherichia coli K-12: dead or alive?." Cell Mol Life Sci 54(4);347-52. PMID: 9614971

Riley06: Riley M, Abe T, Arnaud MB, Berlyn MK, Blattner FR, Chaudhuri RR, Glasner JD, Horiuchi T, Keseler IM, Kosuge T, Mori H, Perna NT, Plunkett G, Rudd KE, Serres MH, Thomas GH, Thomson NR, Wishart D, Wanner BL (2006). "Escherichia coli K-12: a cooperatively developed annotation snapshot--2005." Nucleic Acids Res 34(1);1-9. PMID: 16397293

Sandkvist01: Sandkvist M (2001). "Biology of type II secretion." Mol Microbiol 40(2);271-83. PMID: 11309111

Strom94: Strom MS, Nunn DN, Lory S (1994). "Posttranslational processing of type IV prepilin and homologs by PilD of Pseudomonas aeruginosa." Methods Enzymol 235;527-40. PMID: 8057924

Sun09a: Sun D, Zhang X, Wang L, Prudhomme M, Xie Z, Martin B, Claverys JP (2009). "Transforming DNA uptake gene orthologs do not mediate spontaneous plasmid transformation in Escherichia coli." J Bacteriol 191(3):713-9. PMID: 19011021

UniProt09: UniProt Consortium (2009). "UniProt version 15.8 released on 2009-10-01 00:00:00." Database.

UniProt10a: UniProt Consortium (2010). "UniProt version 2010-07 released on 2010-06-15 00:00:00." Database.

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on the manual assignment of UniProtKB Subcellular Location terms in UniProtKB/Swiss-Prot entries."

Vignon03: Vignon G, Kohler R, Larquet E, Giroux S, Prevost MC, Roux P, Pugsley AP (2003). "Type IV-like pili formed by the type II secreton: specificity, composition, bundling, polar localization, and surface presentation of peptides." J Bacteriol 185(11);3416-28. PMID: 12754241

Voulhoux01: Voulhoux R, Ball G, Ize B, Vasil ML, Lazdunski A, Wu LF, Filloux A (2001). "Involvement of the twin-arginine translocation system in protein secretion via the type II pathway." EMBO J 20(23);6735-41. PMID: 11726509

Other References Related to Gene Regulation

Chen07: Chen Z, Lewis KA, Shultzaberger RK, Lyakhov IG, Zheng M, Doan B, Storz G, Schneider TD (2007). "Discovery of Fur binding site clusters in Escherichia coli by information theory models." Nucleic Acids Res 35(20);6762-77. PMID: 17921503


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 18.5 on Thu Nov 20, 2014, BIOCYC14A.