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Protein

Protease 7

Gene

ompT

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Active sitei1031 Publication1
Active sitei1051 Publication1
Active sitei2301 Publication1
Active sitei2321 Publication1

GO - Molecular functioni

  • aspartic-type endopeptidase activity Source: UniProtKB-KW
  • endopeptidase activity Source: EcoliWiki
  • serine-type endopeptidase activity Source: EcoliWiki

GO - Biological processi

  • 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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10673. ompT.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini21 – 31PeriplasmicSequence analysisAdd BLAST11
Transmembranei32 – 41Beta strandedSequence analysis10
Topological domaini42 – 69ExtracellularSequence analysisAdd BLAST28
Transmembranei70 – 78Beta strandedSequence analysis9
Topological domaini79 – 83PeriplasmicSequence analysis5
Transmembranei84 – 92Beta strandedSequence analysis9
Topological domaini93 – 130ExtracellularSequence analysisAdd BLAST38
Transmembranei131 – 140Beta strandedSequence analysis10
Topological domaini141 – 145PeriplasmicSequence analysis5
Transmembranei146 – 156Beta strandedSequence analysisAdd BLAST11
Topological domaini157 – 197ExtracellularSequence analysisAdd BLAST41
Transmembranei198 – 209Beta strandedSequence analysisAdd BLAST12
Topological domaini210 – 211PeriplasmicSequence analysis2
Transmembranei212 – 221Beta strandedSequence analysis10
Topological domaini222 – 250ExtracellularSequence analysisAdd BLAST29
Transmembranei251 – 261Beta strandedSequence analysisAdd BLAST11
Topological domaini262 – 264PeriplasmicSequence analysis3
Transmembranei265 – 274Beta strandedSequence analysis10
Topological domaini275 – 306ExtracellularSequence analysisAdd BLAST32
Transmembranei307 – 316Beta strandedSequence analysis10
Topological domaini317PeriplasmicSequence analysis1

GO - Cellular componenti

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

Keywords - Cellular componenti

Cell outer membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi103D → A: Loss of activity. 1 Publication1
Mutagenesisi105D → A: Loss of activity. 1 Publication1
Mutagenesisi230D → A: Loss of activity. 1 Publication1
Mutagenesisi236 – 237GK → KG: 70% of wild-type enzymatic activity. 2
Mutagenesisi237K → T: 40% of wild-type enzymatic activity. 1 Publication1
Mutagenesisi238R → L: Loss of activity. 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 204 PublicationsAdd BLAST20
ChainiPRO_000002581521 – 317Protease 7Add BLAST297

Proteomic databases

PaxDbiP09169.
PRIDEiP09169.

2D gel databases

SWISS-2DPAGEP09169.

Interactioni

Subunit structurei

Homopentamer.Curated

Protein-protein interaction databases

BioGridi4263520. 151 interactors.
STRINGi511145.b0565.

Structurei

Secondary structure

1317
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi32 – 51Combined sources20
Turni52 – 56Combined sources5
Beta strandi57 – 78Combined sources22
Beta strandi81 – 95Combined sources15
Beta strandi97 – 105Combined sources9
Beta strandi116 – 142Combined sources27
Beta strandi144 – 164Combined sources21
Beta strandi167 – 170Combined sources4
Beta strandi188 – 209Combined sources22
Beta strandi212 – 233Combined sources22
Beta strandi235 – 237Combined sources3
Beta strandi239 – 262Combined sources24
Beta strandi265 – 287Combined sources23
Turni288 – 291Combined sources4
Beta strandi292 – 316Combined sources25

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1I78X-ray2.60A/B21-317[»]
ProteinModelPortaliP09169.
SMRiP09169.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09169.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase A26 family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane beta strand

Phylogenomic databases

eggNOGiENOG4108NC2. Bacteria.
COG4571. LUCA.
HOGENOMiHOG000117799.
KOiK01355.
OMAiHYQTETI.

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

        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:
EMBLi
GenBanki
DDBJi
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.
WP_001201845.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73666; AAC73666; b0565.
BAA35199; BAA35199; BAA35199.
GeneIDi945185.
KEGGiecj:JW0554.
eco:b0565.
PATRICi32116296. VBIEscCol129921_0588.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
WP_001201845.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1I78X-ray2.60A/B21-317[»]
ProteinModelPortaliP09169.
SMRiP09169.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263520. 151 interactors.
STRINGi511145.b0565.

Protein family/group databases

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

2D gel databases

SWISS-2DPAGEP09169.

Proteomic databases

PaxDbiP09169.
PRIDEiP09169.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73666; AAC73666; b0565.
BAA35199; BAA35199; BAA35199.
GeneIDi945185.
KEGGiecj:JW0554.
eco:b0565.
PATRICi32116296. VBIEscCol129921_0588.

Organism-specific databases

EchoBASEiEB0667.
EcoGeneiEG10673. ompT.

Phylogenomic databases

eggNOGiENOG4108NC2. Bacteria.
COG4571. LUCA.
HOGENOMiHOG000117799.
KOiK01355.
OMAiHYQTETI.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP09169.
PROiP09169.

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]
ProtoNetiSearch...

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: November 2, 2016
This is version 145 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.