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P09169

- OMPT_ECOLI

UniProt

P09169 - OMPT_ECOLI

Protein

Protease 7

Gene

ompT

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 1 (01 Jul 1989)
      Previous versions | rss
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    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

    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

    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. 1 Publication
    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.
    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.

    P09169-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRAKLLGIVL TTPIAISSFA STETLSFTPD NINADISLGT LSGKTKERVY    50
    LAEEGGRKVS QLDWKFNNAA IIKGAINWDL MPQISIGAAG WTTLGSRGGN 100
    MVDQDWMDSS NPGTWTDESR HPDTQLNYAN EFDLNIKGWL LNEPNYRLGL 150
    MAGYQESRYS FTARGGSYIY SSEEGFRDDI GSFPNGERAI GYKQRFKMPY 200
    IGLTGSYRYE DFELGGTFKY SGWVESSDND EHYDPGKRIT YRSKVKDQNY 250
    YSVAVNAGYY VTPNAKVYVE GAWNRVTNKK GNTSLYDHNN NTSDYSKNGA 300
    GIENYNFITT AGLKYTF 317
    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.
    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

    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 1, 2014
    This is version 134 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