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P09169

- OMPT_ECOLI

UniProt

P09169 - OMPT_ECOLI

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Protein

Protease 7

Gene

ompT

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

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 regulationi

Inhibited by zinc.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei103 – 10311 Publication
Active sitei105 – 10511 Publication
Active sitei230 – 23011 Publication
Active sitei232 – 23211 Publication

GO - Molecular functioni

  1. aspartic-type endopeptidase activity Source: UniProtKB-KW
  2. endopeptidase activity Source: EcoliWiki
  3. serine-type endopeptidase activity Source: EcoliWiki

GO - Biological processi

  1. proteolysis Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Aspartyl protease, Hydrolase, Protease

Enzyme and pathway databases

BioCyciEcoCyc:EG10673-MONOMER.
ECOL316407:JW0554-MONOMER.
MetaCyc:EG10673-MONOMER.
BRENDAi3.4.23.49. 2026.

Protein family/group databases

MEROPSiA26.001.
TCDBi9.B.50.1.1. the outer membrane beta-barrel endoprotease, omptin (omptin) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Protease 7 (EC:3.4.23.49)
Alternative name(s):
Omptin
Outer membrane protein 3B
Protease A
Protease VII
Gene namesi
Name:ompT
Ordered Locus Names:b0565, JW0554
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10673. ompT.

Subcellular locationi

GO - Cellular componenti

  1. cell outer membrane Source: EcoCyc
  2. integral component of membrane Source: UniProtKB-KW
  3. intrinsic component of cell outer membrane Source: EcoliWiki
Complete GO annotation...

Keywords - Cellular componenti

Cell outer membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi103 – 1031D → A: Loss of activity. 1 Publication
Mutagenesisi105 – 1051D → A: Loss of activity. 1 Publication
Mutagenesisi230 – 2301D → A: Loss of activity. 1 Publication
Mutagenesisi236 – 2372GK → KG: 70% of wild-type enzymatic activity.
Mutagenesisi237 – 2371K → T: 40% of wild-type enzymatic activity. 1 Publication
Mutagenesisi238 – 2381R → L: Loss of activity.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 20204 PublicationsAdd
BLAST
Chaini21 – 317297Protease 7PRO_0000025815Add
BLAST

Proteomic databases

PaxDbiP09169.
PRIDEiP09169.

2D gel databases

SWISS-2DPAGEP09169.

Expressioni

Gene expression databases

GenevestigatoriP09169.

Interactioni

Subunit structurei

Homopentamer.Curated

Protein-protein interaction databases

STRINGi511145.b0565.

Structurei

Secondary structure

1
317
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi32 – 5120
Turni52 – 565
Beta strandi57 – 7822
Beta strandi81 – 9515
Beta strandi97 – 1059
Beta strandi116 – 14227
Beta strandi144 – 16421
Beta strandi167 – 1704
Beta strandi188 – 20922
Beta strandi212 – 23322
Beta strandi235 – 2373
Beta strandi239 – 26224
Beta strandi265 – 28723
Turni288 – 2914
Beta strandi292 – 31625

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1I78X-ray2.60A/B21-317[»]
ProteinModelPortaliP09169.
SMRiP09169. Positions 21-317.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09169.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini21 – 3111PeriplasmicSequence AnalysisAdd
BLAST
Topological domaini42 – 6928ExtracellularSequence AnalysisAdd
BLAST
Topological domaini79 – 835PeriplasmicSequence Analysis
Topological domaini93 – 13038ExtracellularSequence AnalysisAdd
BLAST
Topological domaini141 – 1455PeriplasmicSequence Analysis
Topological domaini157 – 19741ExtracellularSequence AnalysisAdd
BLAST
Topological domaini210 – 2112PeriplasmicSequence Analysis
Topological domaini222 – 25029ExtracellularSequence AnalysisAdd
BLAST
Topological domaini262 – 2643PeriplasmicSequence Analysis
Topological domaini275 – 30632ExtracellularSequence AnalysisAdd
BLAST
Topological domaini317 – 3171PeriplasmicSequence Analysis

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei32 – 4110Beta strandedSequence Analysis
Transmembranei70 – 789Beta strandedSequence Analysis
Transmembranei84 – 929Beta strandedSequence Analysis
Transmembranei131 – 14010Beta strandedSequence Analysis
Transmembranei146 – 15611Beta strandedSequence AnalysisAdd
BLAST
Transmembranei198 – 20912Beta strandedSequence AnalysisAdd
BLAST
Transmembranei212 – 22110Beta strandedSequence Analysis
Transmembranei251 – 26111Beta strandedSequence AnalysisAdd
BLAST
Transmembranei265 – 27410Beta strandedSequence Analysis
Transmembranei307 – 31610Beta strandedSequence Analysis

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase A26 family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane beta strand

Phylogenomic databases

eggNOGiCOG4571.
HOGENOMiHOG000117799.
KOiK01355.
OMAiKERVYHP.
OrthoDBiEOG6Q8HZT.

Family and domain databases

Gene3Di2.40.128.90. 1 hit.
InterProiIPR020080. OM_adhesin/peptidase_omptin.
IPR023619. Peptidase_A26.
IPR020079. Peptidase_A26_CS.
IPR000036. Peptidase_A26_omptin.
[Graphical view]
PfamiPF01278. Omptin. 1 hit.
[Graphical view]
PIRSFiPIRSF001522. Peptidase_A26. 1 hit.
PRINTSiPR00482. OMPTIN.
SUPFAMiSSF69917. SSF69917. 1 hit.
PROSITEiPS00834. OMPTIN_1. 1 hit.
PS00835. OMPTIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P09169 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRAKLLGIVL TTPIAISSFA STETLSFTPD NINADISLGT LSGKTKERVY
60 70 80 90 100
LAEEGGRKVS QLDWKFNNAA IIKGAINWDL MPQISIGAAG WTTLGSRGGN
110 120 130 140 150
MVDQDWMDSS NPGTWTDESR HPDTQLNYAN EFDLNIKGWL LNEPNYRLGL
160 170 180 190 200
MAGYQESRYS FTARGGSYIY SSEEGFRDDI GSFPNGERAI GYKQRFKMPY
210 220 230 240 250
IGLTGSYRYE DFELGGTFKY SGWVESSDND EHYDPGKRIT YRSKVKDQNY
260 270 280 290 300
YSVAVNAGYY VTPNAKVYVE GAWNRVTNKK GNTSLYDHNN NTSDYSKNGA
310
GIENYNFITT AGLKYTF
Length:317
Mass (Da):35,562
Last modified:July 1, 1989 - v1
Checksum:iCA112FE7F6336F61
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiA31387.
RefSeqiNP_415097.1. NC_000913.3.
YP_488852.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC73666; AAC73666; b0565.
BAA35199; BAA35199; BAA35199.
GeneIDi12934526.
945185.
KEGGiecj:Y75_p0552.
eco:b0565.
PATRICi32116296. VBIEscCol129921_0588.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
PIRi A31387.
RefSeqi NP_415097.1. NC_000913.3.
YP_488852.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1I78 X-ray 2.60 A/B 21-317 [» ]
ProteinModelPortali P09169.
SMRi P09169. Positions 21-317.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 511145.b0565.

Protein family/group databases

MEROPSi A26.001.
TCDBi 9.B.50.1.1. the outer membrane beta-barrel endoprotease, omptin (omptin) family.

2D gel databases

SWISS-2DPAGE P09169.

Proteomic databases

PaxDbi P09169.
PRIDEi P09169.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC73666 ; AAC73666 ; b0565 .
BAA35199 ; BAA35199 ; BAA35199 .
GeneIDi 12934526.
945185.
KEGGi ecj:Y75_p0552.
eco:b0565.
PATRICi 32116296. VBIEscCol129921_0588.

Organism-specific databases

EchoBASEi EB0667.
EcoGenei EG10673. ompT.

Phylogenomic databases

eggNOGi COG4571.
HOGENOMi HOG000117799.
KOi K01355.
OMAi KERVYHP.
OrthoDBi EOG6Q8HZT.

Enzyme and pathway databases

BioCyci EcoCyc:EG10673-MONOMER.
ECOL316407:JW0554-MONOMER.
MetaCyc:EG10673-MONOMER.
BRENDAi 3.4.23.49. 2026.

Miscellaneous databases

EvolutionaryTracei P09169.
PROi P09169.

Gene expression databases

Genevestigatori P09169.

Family and domain databases

Gene3Di 2.40.128.90. 1 hit.
InterProi IPR020080. OM_adhesin/peptidase_omptin.
IPR023619. Peptidase_A26.
IPR020079. Peptidase_A26_CS.
IPR000036. Peptidase_A26_omptin.
[Graphical view ]
Pfami PF01278. Omptin. 1 hit.
[Graphical view ]
PIRSFi PIRSF001522. Peptidase_A26. 1 hit.
PRINTSi PR00482. OMPTIN.
SUPFAMi SSF69917. SSF69917. 1 hit.
PROSITEi PS00834. OMPTIN_1. 1 hit.
PS00835. OMPTIN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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).

Entry informationi

Entry nameiOMPT_ECOLI
AccessioniPrimary (citable) accession number: P09169
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: October 29, 2014
This is version 135 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3