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P09169 (OMPT_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protease 7

EC=3.4.23.49
Alternative name(s):
Omptin
Outer membrane protein 3B
Protease A
Protease VII
Gene names
Name:ompT
Ordered Locus Names:b0565, JW0554
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length317 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Protease that can cleave T7 RNA polymerase, ferric enterobactin receptor protein (FEP), antimicrobial peptide protamine and other proteins. This protease has a specificity for paired basic residues. Ref.8

Catalytic activity

Has a virtual requirement for Arg in the P1 position and a slightly less stringent preference for this residue in the P1' position, which can also contain Lys, Gly or Val.

Enzyme regulation

Inhibited by zinc.

Subunit structure

Homopentamer Potential.

Subcellular location

Cell outer membrane; Multi-pass membrane protein.

Miscellaneous

Was originally classified as a serine protease, but it seems that OmpT could have a novel catalytic mechanism involving an Asp/His dyad and a pair of Asp.

Encoded by the cryptic lambdoid prophage DLP12.

Sequence similarities

Belongs to the peptidase A26 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Ref.1 Ref.2 Ref.7 Ref.9
Chain21 – 317297Protease 7
PRO_0000025815

Regions

Topological domain21 – 3111Periplasmic Potential
Transmembrane32 – 4110Beta stranded; Potential
Topological domain42 – 6928Extracellular Potential
Transmembrane70 – 789Beta stranded; Potential
Topological domain79 – 835Periplasmic Potential
Transmembrane84 – 929Beta stranded; Potential
Topological domain93 – 13038Extracellular Potential
Transmembrane131 – 14010Beta stranded; Potential
Topological domain141 – 1455Periplasmic Potential
Transmembrane146 – 15611Beta stranded; Potential
Topological domain157 – 19741Extracellular Potential
Transmembrane198 – 20912Beta stranded; Potential
Topological domain210 – 2112Periplasmic Potential
Transmembrane212 – 22110Beta stranded; Potential
Topological domain222 – 25029Extracellular Potential
Transmembrane251 – 26111Beta stranded; Potential
Topological domain262 – 2643Periplasmic Potential
Transmembrane265 – 27410Beta stranded; Potential
Topological domain275 – 30632Extracellular Potential
Transmembrane307 – 31610Beta stranded; Potential
Topological domain3171Periplasmic Potential

Sites

Active site1031 Probable
Active site1051 Probable
Active site2301 Probable
Active site2321 Probable

Experimental info

Mutagenesis1031D → A: Loss of activity. Ref.10
Mutagenesis1051D → A: Loss of activity. Ref.10
Mutagenesis2301D → A: Loss of activity. Ref.10
Mutagenesis236 – 2372GK → KG: 70% of wild-type enzymatic activity. Ref.9
Mutagenesis2371K → T: 40% of wild-type enzymatic activity. Ref.9
Mutagenesis2381R → L: Loss of activity.

Secondary structure

........................... 317
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P09169 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: CA112FE7F6336F61

FASTA31735,562
        10         20         30         40         50         60 
MRAKLLGIVL TTPIAISSFA STETLSFTPD NINADISLGT LSGKTKERVY LAEEGGRKVS 

        70         80         90        100        110        120 
QLDWKFNNAA IIKGAINWDL MPQISIGAAG WTTLGSRGGN MVDQDWMDSS NPGTWTDESR 

       130        140        150        160        170        180 
HPDTQLNYAN EFDLNIKGWL LNEPNYRLGL MAGYQESRYS FTARGGSYIY SSEEGFRDDI 

       190        200        210        220        230        240 
GSFPNGERAI GYKQRFKMPY IGLTGSYRYE DFELGGTFKY SGWVESSDND EHYDPGKRIT 

       250        260        270        280        290        300 
YRSKVKDQNY YSVAVNAGYY VTPNAKVYVE GAWNRVTNKK GNTSLYDHNN NTSDYSKNGA 

       310 
GIENYNFITT AGLKYTF 

« Hide

References

« Hide 'large scale' references
[1]"Complete nucleotide sequence and deduced amino acid sequence of the ompT gene of Escherichia coli K-12."
Grodberg J., Lundrigan M.D., Toledo D.L., Mangel W.F., Dunn J.J.
Nucleic Acids Res. 16:1209-1209(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 21-36.
Strain: K12.
[2]"Purification, characterization, and primary structure of Escherichia coli protease VII with specificity for paired basic residues: identity of protease VII and OmpT."
Sugimura K., Nisihihara T.
J. Bacteriol. 170:5625-5632(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 21-40, CHARACTERIZATION.
[3]"Sequence of minutes 4-25 of Escherichia coli."
Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"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 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[5]"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.
[6]"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map."
Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. expand/collapse author list , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T.
DNA Res. 3:137-155(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-16.
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[7]"Extraction of membrane proteins by differential solubilization for separation using two-dimensional gel electrophoresis."
Molloy M.P., Herbert B.R., Walsh B.J., Tyler M.I., Traini M., Sanchez J.-C., Hochstrasser D.F., Williams K.L., Gooley A.A.
Electrophoresis 19:837-844(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 21-24.
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[8]"Identification of OmpT as the protease that hydrolyzes the antimicrobial peptide protamine before it enters growing cells of Escherichia coli."
Stumpe S., Schmid R., Stephens D.L., Georgiou G., Bakker E.P.
J. Bacteriol. 180:4002-4006(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"In vitro folding, purification and characterization of Escherichia coli outer membrane protease ompT."
Kramer R.A., Zandwijken D., Egmond M.R., Dekker N.
Eur. J. Biochem. 267:885-893(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION, PROTEIN SEQUENCE OF 21-25, MUTAGENESIS OF GLY-236 AND LYS-237.
Strain: BL21-DE3 and K12 / DH5-alpha.
[10]"Identification of essential acidic residues of outer membrane protease OmpT supports a novel active site."
Kramer R.A., Vandeputte-Rutten L., de Roon G.J., Gros P., Dekker N., Egmond M.R.
FEBS Lett. 505:426-430(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: ACTIVE SITE, MUTAGENESIS OF ASP-103; ASP-105 AND ASP-230.
Strain: BL21-DE3 and K12 / DH5-alpha.
[11]"Crystal structure of the outer membrane protease OmpT from Escherichia coli suggests a novel catalytic site."
Vandeputte-Rutten L., Kramer R.A., Kroon J., Dekker N., Egmond M.R., Gros P.
EMBO J. 20:5033-5039(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X06903 Genomic DNA. Translation: CAA30008.1.
M23630 Genomic DNA. Translation: AAA24430.1.
U82598 Genomic DNA. Translation: AAB40761.1.
U00096 Genomic DNA. Translation: AAC73666.1.
AP009048 Genomic DNA. Translation: BAA35199.2.
PIRA31387.
RefSeqNP_415097.1. NC_000913.3.
YP_488852.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1I78X-ray2.60A/B21-317[»]
ProteinModelPortalP09169.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING511145.b0565.

Protein family/group databases

MEROPSA26.001.
TCDB9.B.50.1.1. the outer membrane beta-barrel endoprotease, omptin (omptin) family.

2D gel databases

SWISS-2DPAGEP09169.

Proteomic databases

PaxDbP09169.
PRIDEP09169.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73666; AAC73666; b0565.
BAA35199; BAA35199; BAA35199.
GeneID12934526.
945185.
KEGGecj:Y75_p0552.
eco:b0565.
PATRIC32116296. VBIEscCol129921_0588.

Organism-specific databases

EchoBASEEB0667.
EcoGeneEG10673. ompT.

Phylogenomic databases

eggNOGCOG4571.
HOGENOMHOG000117799.
KOK01355.
OMAKERVYHP.
OrthoDBEOG6Q8HZT.

Enzyme and pathway databases

BioCycEcoCyc:EG10673-MONOMER.
ECOL316407:JW0554-MONOMER.
MetaCyc:EG10673-MONOMER.
BRENDA3.4.23.49. 2026.

Gene expression databases

GenevestigatorP09169.

Family and domain databases

Gene3D2.40.128.90. 1 hit.
InterProIPR020080. OM_adhesin/peptidase_omptin.
IPR023619. Peptidase_A26.
IPR020079. Peptidase_A26_CS.
IPR000036. Peptidase_A26_omptin.
[Graphical view]
PfamPF01278. Omptin. 1 hit.
[Graphical view]
PIRSFPIRSF001522. Peptidase_A26. 1 hit.
PRINTSPR00482. OMPTIN.
SUPFAMSSF69917. SSF69917. 1 hit.
PROSITEPS00834. OMPTIN_1. 1 hit.
PS00835. OMPTIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP09169.
PROP09169.

Entry information

Entry nameOMPT_ECOLI
AccessionPrimary (citable) accession number: P09169
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: June 11, 2014
This is version 133 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

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