P09169 (OMPT_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	317 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.
Sequence similarities	Belongs to the peptidase A26 family.

Ontologies

Keywords
Cellular component	Cell membrane Cell outer membrane Membrane
Domain	Signal Transmembrane Transmembrane beta strand
Molecular function	Aspartyl protease Hydrolase Protease
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cell outer membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	aspartic-type endopeptidase 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

Signal peptide

1 – 20

20

Ref.1 Ref.2 Ref.7 Ref.9

Chain

21 – 317

297

Protease 7

PRO_0000025815

Regions

Topological domain

21 – 31

11

Periplasmic Potential

Transmembrane

32 – 41

10

Beta stranded; Potential

Topological domain

42 – 69

28

Extracellular Potential

Transmembrane

70 – 78

9

Beta stranded; Potential

Topological domain

79 – 83

5

Periplasmic Potential

Transmembrane

84 – 92

9

Beta stranded; Potential

Topological domain

93 – 130

38

Extracellular Potential

Transmembrane

131 – 140

10

Beta stranded; Potential

Topological domain

141 – 145

5

Periplasmic Potential

Transmembrane

146 – 156

11

Beta stranded; Potential

Topological domain

157 – 197

41

Extracellular Potential

Transmembrane

198 – 209

12

Beta stranded; Potential

Topological domain

210 – 211

2

Periplasmic Potential

Transmembrane

212 – 221

10

Beta stranded; Potential

Topological domain

222 – 250

29

Extracellular Potential

Transmembrane

251 – 261

11

Beta stranded; Potential

Topological domain

262 – 264

3

Periplasmic Potential

Transmembrane

265 – 274

10

Beta stranded; Potential

Topological domain

275 – 306

32

Extracellular Potential

Transmembrane

307 – 316

10

Beta stranded; Potential

Topological domain

317

1

Periplasmic Potential

Sites

Active site

103

1

Probable

Active site

105

1

Probable

Active site

230

1

Probable

Active site

232

1

Probable

Experimental info

Mutagenesis

103

1

D → A: Loss of activity. Ref.10

Mutagenesis

105

1

D → A: Loss of activity. Ref.10

Mutagenesis

230

1

D → A: Loss of activity. Ref.10

Mutagenesis

236 – 237

2

GK → KG: 70% of wild-type enzymatic activity. Ref.9

Mutagenesis

237

1

K → T: 40% of wild-type enzymatic activity. Ref.9

Mutagenesis

238

1

R → L: Loss of activity.

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

317

Helix Strand Turn

Details...

Beta strand

32 – 51

20

Turn

52 – 56

5

Beta strand

57 – 78

22

Beta strand

81 – 95

15

Beta strand

97 – 105

9

Beta strand

116 – 142

27

Beta strand

144 – 164

21

Beta strand

167 – 170

4

Beta strand

188 – 209

22

Beta strand

212 – 233

22

Beta strand

235 – 237

3

Beta strand

239 – 262

24

Beta strand

265 – 287

23

Turn

288 – 291

4

Beta strand

292 – 316

25

Sequences

	Sequence		Length	Mass (Da)
	P09169 [UniParc]. Last modified July 1, 1989. Version 1. Checksum: CA112FE7F6336F61	FASTA	317	35,562
	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

References

	« Hide 'large scale' referencesShow '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: 3278297] [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: 3056908] [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 277:1453-1474(1997) [PubMed: 9278503] [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: 16738553] [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. , 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: 8905232] [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: 9629924] [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: 9683502] [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: 10651827] [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: 11576541] [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: 11566868] [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.

PIR

A31387.

RefSeq

NP_415097.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1I78	X-ray	2.60	A/B	21-317	[»]

ProteinModelPortal

P09169.

SMR

P09169. Positions 21-317.

ModBase

Search...

Protein family/group databases

MEROPS

A26.001.

2D gel databases

SWISS-2DPAGE

P09169.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000003678; EBESCP00000003678; EBESCG00000003007.
EBESCT00000018388; EBESCP00000017679; EBESCG00000017442.

GeneID

945185.

GenomeReviews

Gene locus JW0554 in contig AP009048_GR.
Gene locus b0565 in contig U00096_GR.

KEGG

ecj:JW0554.
eco:b0565.

PATRIC

32116296. VBIEscCol129921_0588.

Organism-specific databases

EchoBASE

EB0667.

EcoGene

EG10673. ompT.

Phylogenomic databases

eggNOG

COG4571.

GeneTree

EBGT00050000011956.

HOGENOM

HBG468061.

OMA

RDWMDSS.

ProtClustDB

PRK10993.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10673-MONOMER.
MetaCyc:EG10673-MONOMER.

BRENDA

3.4.23.49. 2026.

Gene expression databases

Genevestigator

P09169.

Family and domain databases

InterPro

IPR020080. OM_adhesin/peptidase_omptin.
IPR023619. Peptidase_A26.
IPR020079. Peptidase_A26_CS.
IPR000036. Peptidase_A26_omptin.
[Graphical view]

Gene3D

G3DSA:2.40.128.90. Peptidase_A26. 1 hit.

KO

K01355.

Pfam

PF01278. Omptin. 1 hit.
[Graphical view]

PIRSF

PIRSF001522. Peptidase_A26. 1 hit.

PRINTS

PR00482. OMPTIN.

SUPFAM

SSF69917. OM_adhesin/protease_omptin. 1 hit.

PROSITE

PS00834. OMPTIN_1. 1 hit.
PS00835. OMPTIN_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

OMPT_ECOLI

Accession

Primary (citable) accession number: P09169

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	January 25, 2012
This is version 114 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program