P23827 (ECOT_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ecotin

Gene names

Name:	eco
Synonyms:	eti
Ordered Locus Names:	b2209, JW2197

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	162 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	General inhibitor of pancreatic serine proteases: inhibits chymotrypsin, trypsin, elastases, factor X, kallikrein as well as a variety of other proteases. The strength of inhibition does not appear to be correlated with a particular protease specificity. HAMAP MF_00706
Subunit structure	Homodimer.
Subcellular location	Periplasm HAMAP MF_00706.
Sequence similarities	Belongs to the protease inhibitor I11 (ecotin) family. [View classification]
Sequence caution	The sequence AAA16410.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Periplasm
Domain	Signal
Molecular function	Protease inhibitor Serine protease inhibitor
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Cellular component	periplasmic space Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	protein binding Inferred from physical interaction Ref.11. Source: IntAct serine-type endopeptidase inhibitor activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
F11	P03951	3	EBI-1029159,EBI-1041019	From a different organism.
Prss2	P00763	2	EBI-1029159,EBI-1029166	From a different organism.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 20

20

Ref.1 Ref.7

Chain

21 – 162

142

Ecotin HAMAP MF_00706

PRO_0000007423

Sites

Site

104 – 105

2

Reactive bond

Amino acid modifications

Disulfide bond

70 ↔ 107

HAMAP MF_00706

Secondary structure

1

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162

Helix Strand Turn

Details...

Helix

27 – 29

3

Beta strand

40 – 45

6

Beta strand

56 – 68

13

Beta strand

73 – 76

4

Beta strand

78 – 83

6

Turn

85 – 87

3

Beta strand

90 – 95

6

Beta strand

101 – 103

3

Beta strand

113 – 120

8

Beta strand

126 – 128

3

Beta strand

135 – 140

6

Beta strand

144 – 152

9

Sequences

	Sequence		Length	Mass (Da)
	P23827 [UniParc]. Last modified November 1, 1991. Version 1. Checksum: E965383177B92ECD	FASTA	162	18,192
	10 20 30 40 50 60 MKTILPAVLF AAFATTSAWA AESVQPLEKI APYPQAEKGM KRQVIQLTPQ EDESTLKVEL 70 80 90 100 110 120 LIGQTLEVDC NLHRLGGKLE NKTLEGWGYD YYVFDKVSSP VSTMMACPDG KKEKKFVTAY 130 140 150 160 LGDAGMLRYN SKLPIVVYTP DNVDVKYRVW KAEEKIDNAV VR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The sequence and reactive site of ecotin. A general inhibitor of pancreatic serine proteases from Escherichia coli." McGrath M.E., Hines W.M., Sakanari J.A., Fletterick R.J., Craik C.S. J. Biol. Chem. 266:6620-6625(1991) [PubMed: 2007606] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 21-25 AND 105-109.
[2]	"Molecular cloning of the ecotin gene in Escherichia coli." Lee H.R., Seol J.H., Kim O.M., Lee C.S., Suh S.W., Hong Y.M., Tanaka K., Ichihara A., Ha D.B., Chung C.H. FEBS Lett. 287:53-56(1991) [PubMed: 1879537] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Automated multiplex sequencing of the E.coli genome." Richterich P., Lakey N., Gryan G., Jaehn L., Mintz L., Robison K., Church G.M. Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / BHB2600.
[4]	"A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map." Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S. , Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y., Horiuchi T. DNA Res. 3:379-392(1996) [PubMed: 9097040] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"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.
[6]	"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.
[7]	"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Link A.J., Robison K., Church G.M. Electrophoresis 18:1259-1313(1997) [PubMed: 9298646] [Abstract] Cited for: PROTEIN SEQUENCE OF 21-32. Strain: K12 / EMG2.
[8]	"Macromolecular chelation as an improved mechanism of protease inhibition: structure of the ecotin-trypsin complex." McGrath M.E., Erpel T., Bystroff C., Fletterick R.J. EMBO J. 13:1502-1507(1994) [PubMed: 8156987] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
[9]	"Crystal structure analyses of uncomplexed ecotin in two crystal forms: implications for its function and stability." Shin D.H.A., Song H.K., Seong I.S., Lee C.S., Chung C.H., Suh S.W. Protein Sci. 5:2236-2247(1996) [PubMed: 8931142] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.68 ANGSTROMS).
[10]	"Crystal structure of an ecotin-collagenase complex suggests a model for recognition and cleavage of the collagen triple helix." Perona J.J., Tsu C.A., Craik C.S., Fletterick R.J. Biochemistry 36:5381-5392(1997) [PubMed: 9154920] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF COMPLEX WITH UCA COLLAGENASE.
[11]	"Compromise and accommodation in ecotin, a dimeric macromolecular inhibitor of serine proteases." Gillmor S.A., Takeuchi T., Yang S.Q., Craik C.S., Fletterick R.J. J. Mol. Biol. 299:993-1003(2000) [PubMed: 10843853] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
[12]	"Crystal structure of thrombin-ecotin reveals conformational changes and extended interactions." Wang S.X., Esmon C.T., Fletterick R.J. Biochemistry 40:10038-10046(2001) [PubMed: 11513582] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF MUTANT ARG-104.
[13]	"Ecotin: lessons on survival in a protease-filled world." McGrath M.E., Gillmor S.A., Fletterick R.J. Protein Sci. 4:141-148(1995) [PubMed: 7757004] [Abstract] Cited for: REVIEW.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M60876 Genomic DNA. Translation: AAA23719.1.
X61951 Genomic DNA. Translation: CAA43954.1.
U00008 Genomic DNA. Translation: AAA16410.1. Different initiation.
U00096 Genomic DNA. Translation: AAC75269.1.
AP009048 Genomic DNA. Translation: BAA15992.1.

PIR

A38742.

RefSeq

NP_416713.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AZZ	X-ray	2.30	C/D	21-162	[»]
1ECY	X-ray	2.19	A	21-162	[»]
1ECZ	X-ray	2.68	A/B	21-162	[»]
1EZS	X-ray	2.30	A/B	21-162	[»]
1EZU	X-ray	2.40	A/B	21-162	[»]
1FI8	X-ray	2.20	C/E	21-100	[»]
			D/F	105-162	[»]
1ID5	X-ray	2.50	I	21-162	[»]
1IFG	X-ray	2.00	A	26-162	[»]
1N8O	X-ray	2.00	E	21-162	[»]
1P0S	X-ray	2.80	E	21-162	[»]
1SLU	X-ray	1.80	A	21-162	[»]
1SLV	X-ray	2.30	A	21-162	[»]
1SLW	X-ray	2.00	A	21-162	[»]
1SLX	X-ray	2.20	A	21-162	[»]
1XX9	X-ray	2.20	C/D	21-162	[»]
1XXD	X-ray	2.91	C/D	21-162	[»]
1XXF	X-ray	2.60	C/D	21-162	[»]

ProteinModelPortal

P23827.

SMR

P23827. Positions 21-162.

ModBase

Search...

Protein-protein interaction databases

IntAct

P23827. 8 interactions.

MINT

MINT-276115.

Protein family/group databases

MEROPS

I11.001.

2D gel databases

ECO2DBASE

G016.3. 6TH EDITION.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000003682; EBESCP00000003682; EBESCG00000003011.
EBESCT00000014637; EBESCP00000013928; EBESCG00000013698.

GeneID

946700.

GenomeReviews

Gene locus JW2197 in contig AP009048_GR.
Gene locus b2209 in contig U00096_GR.

KEGG

ecj:JW2197.
eco:b2209.

PATRIC

32119777. VBIEscCol129921_2298.

Organism-specific databases

EchoBASE

EB0251.

EcoGene

EG10255. eco.

Phylogenomic databases

eggNOG

COG4574.

GeneTree

EBGT00050000011046.

HOGENOM

HBG710412.

OMA

RYDSRLP.

ProtClustDB

PRK03719.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10255-MONOMER.

Gene expression databases

Genevestigator

P23827.

Family and domain databases

HAMAP

MF_00706. Ecotin.
[Tree]

InterPro

IPR005658. Prot_inh_ecotin.
IPR023189. Prot_inh_ecotin_dom.
IPR023084. Prot_inh_ecotin_gammaproteobac.
[Graphical view]

Gene3D

G3DSA:2.60.40.550. Prot_inh_ecotin. 1 hit.

KO

K08276.

Pfam

PF03974. Ecotin. 1 hit.
[Graphical view]

PIRSF

PIRSF006865. Prot_inh_ecotin. 1 hit.

SUPFAM

SSF49772. Prot_inh_ecotin. 1 hit.

ProtoNet

Search...

Entry information

Entry name

ECOT_ECOLI

Accession

Primary (citable) accession number: P23827

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	November 1, 1991
Last modified:	January 25, 2012
This is version 104 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program