Type 4 prepilin-like proteins leader peptide-processing enzyme

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P25960 (LEP4_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 110. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Type 4 prepilin-like proteins leader peptide-processing enzyme

Including the following 2 domains:

Leader peptidase
EC=3.4.23.43
Alternative name(s):
Prepilin peptidase
N-methyltransferase
EC=2.1.1.-

Gene names

Name:	gspO
Synonyms:	hofD, hopD, hopO, yheC
Ordered Locus Names:	b3335, JW3297

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	225 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Cleaves type-4 fimbrial leader sequence and methylates the N-terminal (generally Phe) residue By similarity.
Catalytic activity	Typically cleaves a -Gly-\|-Phe- bond to release an N-terminal, basic peptide of 5-8 residues from type IV prepilin, and then N-methylates the new N-terminal amino group, the methyl donor being S-adenosyl-L-methionine.
Subcellular location	Cell inner membrane; Multi-pass membrane protein.
Induction	Silenced by the DNA-binding protein H-NS under standard growth conditions. Ref.7
Miscellaneous	Part of a cryptic operon that encodes proteins involved in type II secretion machinery in other organisms, but is not expressed in strain K12. However, GspO is functional when expressed from a stronger promoter (Ref.6).
Sequence similarities	Belongs to the peptidase A24 family.

Ontologies

Keywords
Biological process	Transport
Cellular component	Cell inner membrane Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Molecular function	Hydrolase Protease Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	aspartic-type endopeptidase activity Inferred from electronic annotation. Source: InterPro transferase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 225

225

Type 4 prepilin-like proteins leader peptide-processing enzyme

PRO_0000192632

Regions

Topological domain

1 – 2

Periplasmic Potential

Transmembrane

3 – 23

Helical; Potential

Topological domain

24 – 67

Cytoplasmic Potential

Transmembrane

68 – 88

Helical; Potential

Topological domain

89 – 103

Periplasmic Potential

Transmembrane

104 – 124

Helical; Potential

Topological domain

125 – 127

Cytoplasmic Potential

Transmembrane

128 – 148

Helical; Potential

Topological domain

149 – 174

Periplasmic Potential

Transmembrane

175 – 195

Helical; Potential

Topological domain

196 – 202

Cytoplasmic Potential

Transmembrane

203 – 223

Helical; Potential

Topological domain

224 – 225

Periplasmic Potential

Experimental info

Sequence conflict

131

A → P in AAC13988. Ref.4

Sequence conflict

208 – 209

WL → CV in AAA58132. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

P25960 [UniParc].

Last modified June 1, 1994. Version 2.
Checksum: 90297BB7E6592EDD
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FASTA

225

24,957

        10         20         30         40         50         60 
MTMLLPLFIL VGFIADYFVN AIAYHLSPLE DKTALTFRQV LVHFRQKKYA WHDTVPLILC 

        70         80         90        100        110        120 
VAAAIACALA PFTPIVTGAL FLYFCFVLTL SVIDFRTQLL PDKLTLPLLW LGLVFNAQYG 

       130        140        150        160        170        180 
LIDLHDAVYG AVAGYGVLWC VYWGVWLVCH KEGLGYGDFK LLAAAGAWCG WQTLPMILLI 

       190        200        210        220 
ASLGGIGYAI VSQLLQRRTI TTIAFGPWLA LGSMINLGYL AWISY

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Escherichia coli contains a set of genes homologous to those involved in protein secretion, DNA uptake and the assembly of type-4 fimbriae in other bacteria." Whitchurch C.B., Mattick J.S. Gene 150:9-15(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"Cloning, sequencing, and mapping of the bacterioferritin gene (bfr) of Escherichia coli K-12." Andrews S.C., Harrison P.M., Guest J.R. J. Bacteriol. 171:3940-3947(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 116-225. Strain: K12.
[5]	"Characterisation of a Pseudomonas aeruginosa twitching motility gene and evidence for a specialised protein export system widespread in eubacteria." Whitchurch C.B., Hobbs M., Livingston S.P., Krishnapillai V., Mattick J.S. Gene 101:33-44(1991) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION.
[6]	"The cryptic general secretory pathway (gsp) operon of Escherichia coli K-12 encodes functional proteins." Francetic O., Pugsley A.P. J. Bacteriol. 178:3544-3549(1996) [PubMed] [Europe PMC] [Abstract] Cited for: LACK OF EXPRESSION, GENE NAME. Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
[7]	"Expression of the endogenous type II secretion pathway in Escherichia coli leads to chitinase secretion." Francetic O., Belin D., Badaut C., Pugsley A.P. EMBO J. 19:6697-6703(2000) [PubMed] [Europe PMC] [Abstract] Cited for: LACK OF EXPRESSION, TRANSCRIPTIONAL REGULATION. Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
[8]	"Global topology analysis of the Escherichia coli inner membrane proteome." Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G. Science 308:1321-1323(2005) [PubMed] [Europe PMC] [Abstract] Cited for: TOPOLOGY [LARGE SCALE ANALYSIS]. Strain: K12 / MG1655 / ATCC 47076.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L28106 Genomic DNA. Translation: AAC36928.1. U18997 Genomic DNA. Translation: AAA58132.1. U00096 Genomic DNA. Translation: AAC76360.1. AP009048 Genomic DNA. Translation: BAE77956.1. M27176 mRNA. Translation: AAC13988.1.
PIR	B65127.
RefSeq	NP_417794.1. NC_000913.2. YP_492097.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P25960.
ModBase	Search...
Protein-protein interaction databases
STRING	511145.b3335.
Protein family/group databases
MEROPS	A24.A10.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC76360; AAC76360; b3335. BAE77956; BAE77956; BAE77956.
GeneID	12933471. 947840.
KEGG	ecj:Y75_p3841. eco:b3335.
PATRIC	32122102. VBIEscCol129921_3428.
Organism-specific databases
EchoBASE	EB1334.
EcoGene	EG11359. gspO.
Phylogenomic databases
eggNOG	COG1989.
HOGENOM	HOG000248584.
KO	K02464.
OMA	ACWISPL.
ProtClustDB	CLSK891809.
Enzyme and pathway databases
BioCyc	EcoCyc:EG11359-MONOMER. ECOL316407:JW3297-MONOMER. MetaCyc:EG11359-MONOMER.
Gene expression databases
Genevestigator	P25960.
Family and domain databases
InterPro	IPR014032. Peptidase_A24A_bac. IPR000045. Prepilin_IV_endopep_pep. [Graphical view]
Pfam	PF01478. Peptidase_A24. 1 hit. [Graphical view]
PRINTS	PR00864. PREPILNPTASE.
ProtoNet	Search...

Entry information

Entry name

LEP4_ECOLI

Accession

Primary (citable) accession number: P25960
Secondary accession number(s): Q2M700

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	June 1, 1994
Last modified:	May 1, 2013
This is version 110 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Including the following 2 domains:

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents