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Protein

Metalloprotease StcE

Gene

stcE

Organism
Escherichia coli O157:H7
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Virulence factor that contributes to intimate adherence of enterohemorrhagic E.coli (EHEC) O157:H7 to host cells. Is able to cleave the secreted human mucin 7 (MUC7) and the glycoprotein 340 (DMBT1/GP340). Also cleaves human C1 inhibitor (SERPING1), a regulator of multiple inflammatory pathways, and binds and localizes it to bacterial and host cell surfaces, protecting them from complement-mediated lysis. Therefore, the current model proposes two roles for StcE during infection: it acts first as a mucinase, allowing passage of EHEC through the oral cavity by cleaving the salivary glycoproteins that are responsible for bacterial aggregation. Similarly, in the colon, StcE cleaves the glycoproteins that protect the intestinal epithelial surface, allowing EHEC to come into close contact with host cell membranes. Secondly, it acts as an anti-inflammatory agent by localizing SERPING1 to cell membranes.4 Publications

Cofactori

Zn2+2 PublicationsNote: Binds 1 zinc ion per subunit. Does not contain structural calcium, which is often associated with other metalloproteases.2 Publications

Enzyme regulationi

Inhibited by divalent cation chelators such as BPS and EDTA.

Kineticsi

Proteolytic activity is 2.5-fold more efficient with the secreted mucin MUC7 than with SERPING1.

  1. KM=0.13 µM for MUC71 Publication
  2. KM=0.27 µM for SERPING11 Publication
  1. Vmax=70.2 nM/min/µg enzyme for MUC7 cleavage1 Publication
  2. Vmax=66.8 nM/min/µg enzyme for SERPING1 cleavage1 Publication

pH dependencei

Optimum pH is 6.5-7.0. Active from pH 6.1 to 9.0.1 Publication

Temperature dependencei

Optimum temperature is 37-42 degrees Celsius. Active from 4 to 55 degrees Celsius. Inactive above 60 degrees Celsius.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi446 – 4461Zinc; catalyticBy similarity
Active sitei447 – 4471
Metal bindingi450 – 4501Zinc; catalyticBy similarity
Metal bindingi456 – 4561Zinc; catalyticBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Virulence

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiM66.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Metalloprotease StcE (EC:3.4.24.-)
Alternative name(s):
Mucinase
Neutral zinc metalloprotease StcE
Secreted protease of C1 esterase inhibitor from EHEC
Gene namesi
Name:stcE
Synonyms:tagA
Ordered Locus Names:L7031, ECO57PM83
Encoded oniPlasmid pO1570 Publication
OrganismiEscherichia coli O157:H7
Taxonomic identifieri83334 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000558 Componenti: Plasmid pO157
  • UP000002519 Componenti: Plasmid pO157

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi447 – 4471E → D: Prevents both cleavage and binding to SERPING1. Unable to aggregate T-cells. Still able to bind zinc. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3535Sequence analysisAdd
BLAST
Chaini36 – 898863Metalloprotease StcEPRO_0000248145Add
BLAST

Proteomic databases

PRIDEiO82882.

Expressioni

Inductioni

Up-regulated by the LEE (locus of enterocyte effacement)-encoded regulator ler.2 Publications

Interactioni

Protein-protein interaction databases

DIPiDIP-59647N.
STRINGi155864.L7031.

Structurei

Secondary structure

1
898
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi42 – 443Combined sources
Beta strandi54 – 563Combined sources
Beta strandi59 – 7214Combined sources
Beta strandi82 – 865Combined sources
Beta strandi88 – 969Combined sources
Beta strandi99 – 1013Combined sources
Beta strandi103 – 1086Combined sources
Beta strandi114 – 1196Combined sources
Helixi123 – 1253Combined sources
Beta strandi146 – 1483Combined sources
Beta strandi150 – 1534Combined sources
Helixi156 – 1605Combined sources
Helixi161 – 1633Combined sources
Helixi168 – 1747Combined sources
Beta strandi178 – 1858Combined sources
Beta strandi191 – 1944Combined sources
Helixi199 – 2013Combined sources
Beta strandi205 – 2117Combined sources
Beta strandi216 – 2205Combined sources
Beta strandi223 – 2275Combined sources
Beta strandi232 – 2387Combined sources
Beta strandi241 – 2444Combined sources
Helixi249 – 2524Combined sources
Beta strandi253 – 2553Combined sources
Beta strandi260 – 2645Combined sources
Helixi266 – 2683Combined sources
Beta strandi274 – 2796Combined sources
Beta strandi282 – 2865Combined sources
Beta strandi296 – 30813Combined sources
Helixi315 – 3184Combined sources
Helixi320 – 3278Combined sources
Beta strandi333 – 3408Combined sources
Beta strandi343 – 3497Combined sources
Beta strandi355 – 3584Combined sources
Helixi370 – 3745Combined sources
Helixi375 – 3806Combined sources
Helixi381 – 3899Combined sources
Beta strandi393 – 3975Combined sources
Beta strandi408 – 41811Combined sources
Beta strandi421 – 4244Combined sources
Beta strandi427 – 4304Combined sources
Beta strandi433 – 4353Combined sources
Helixi441 – 45010Combined sources
Turni451 – 4533Combined sources
Helixi460 – 4645Combined sources
Beta strandi471 – 4733Combined sources
Beta strandi477 – 4793Combined sources
Turni480 – 4834Combined sources
Beta strandi484 – 4863Combined sources
Beta strandi488 – 4936Combined sources
Beta strandi498 – 5003Combined sources
Beta strandi503 – 5053Combined sources
Beta strandi511 – 5133Combined sources
Turni517 – 5204Combined sources
Helixi535 – 54612Combined sources
Beta strandi548 – 5514Combined sources
Beta strandi558 – 5636Combined sources
Turni564 – 5674Combined sources
Beta strandi568 – 5714Combined sources
Beta strandi682 – 69514Combined sources
Beta strandi709 – 7168Combined sources
Beta strandi755 – 7628Combined sources
Helixi763 – 7653Combined sources
Beta strandi793 – 7986Combined sources
Beta strandi806 – 8116Combined sources
Turni812 – 8143Combined sources
Beta strandi817 – 8215Combined sources
Turni832 – 8365Combined sources
Beta strandi839 – 8435Combined sources
Beta strandi847 – 85711Combined sources
Beta strandi862 – 8654Combined sources
Beta strandi867 – 8693Combined sources
Helixi871 – 8733Combined sources
Beta strandi874 – 8785Combined sources
Beta strandi880 – 8856Combined sources
Beta strandi891 – 8977Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3UJZX-ray2.50A36-898[»]
4DNYX-ray1.61A132-251[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini296 – 551256Peptidase M66Add
BLAST

Sequence similaritiesi

Contains 1 peptidase M66 domain.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4108MA4. Bacteria.
ENOG410XSA0. LUCA.
HOGENOMiHOG000272937.
OMAiSVMNKFH.
OrthoDBiEOG66F033.

Family and domain databases

InterProiIPR019503. Peptidase_M66_dom.
[Graphical view]
PfamiPF10462. Peptidase_M66. 1 hit.
[Graphical view]
PROSITEiPS51694. PEPTIDASE_M66. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

O82882-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNTKMNERWR TPMKLKYLSC TILAPLAIGV FSATAADNNS AIYFNTSQPI
60 70 80 90 100
NDLQGSLAAE VKFAQSQILP AHPKEGDSQP HLTSLRKSLL LVRPVKADDK
110 120 130 140 150
TPVQVEARDD NNKILGTLTL YPPSSLPDTI YHLDGVPEGG IDFTPHNGTK
160 170 180 190 200
KIINTVAEVN KLSDASGSSI HSHLTNNALV EIHTANGRWV RDIYLPQGPD
210 220 230 240 250
LEGKMVRFVS SAGYSSTVFY GDRKVTLSVG NTLLFKYVNG QWFRSGELEN
260 270 280 290 300
NRITYAQHIW SAELPAHWIV PGLNLVIKQG NLSGRLNDIK IGAPGELLLH
310 320 330 340 350
TIDIGMLTTP RDRFDFAKDK EAHREYFQTI PVSRMIVNNY APLHLKEVML
360 370 380 390 400
PTGELLTDMD PGNGGWHSGT MRQRIGKELV SHGIDNANYG LNSTAGLGEN
410 420 430 440 450
SHPYVVAQLA AHNSRGNYAN GIQVHGGSGG GGIVTLDSTL GNEFSHEVGH
460 470 480 490 500
NYGLGHYVDG FKGSVHRSAE NNNSTWGWDG DKKRFIPNFY PSQTNEKSCL
510 520 530 540 550
NNQCQEPFDG HKFGFDAMAG GSPFSAANRF TMYTPNSSAI IQRFFENKAV
560 570 580 590 600
FDSRSSTGFS KWNADTQEME PYEHTIDRAE QITASVNELS ESKMAELMAE
610 620 630 640 650
YAVVKVHMWN GNWTRNIYIP TASADNRGSI LTINHEAGYN SYLFINGDEK
660 670 680 690 700
VVSQGYKKSF VSDGQFWKER DVVDTREARK PEQFGVPVTT LVGYYDPEGT
710 720 730 740 750
LSSYIYPAMY GAYGFTYSDD SQNLSDNDCQ LQVDTKEGQL RFRLANHRAN
760 770 780 790 800
NTVMNKFHIN VPTESQPTQA TLVCNNKILD TKSLTPAPEG LTYTVNGQAL
810 820 830 840 850
PAKENEGCIV SVNSGKRYCL PVGQRSGYSL PDWIVGQEVY VDSGAKAKVL
860 870 880 890
LSDWDNLSYN RIGEFVGNVN PADMKKVKAW NGQYLDFSKP RSMRVVYK
Length:898
Mass (Da):99,548
Last modified:November 1, 1999 - v2
Checksum:i3C1AE23E3EAE1FAB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y11831 Genomic DNA. Translation: CAA72517.1.
Y11275 Genomic DNA. Translation: CAA72142.1.
AF074613 Genomic DNA. Translation: AAC70099.1.
AB011549 Genomic DNA. Translation: BAA31757.3.
AY714880 Genomic DNA. Translation: AAU25886.1.
PIRiT42131.
RefSeqiNP_052607.1. NC_002128.1.
YP_001294684.1. NC_009602.1.

Genome annotation databases

EnsemblBacteriaiAAC70099; AAC70099; Z_L7031.
BAA31757; BAA31757; BAA31757.
GeneIDi1789672.
5290916.
KEGGiece:Z_L7031.
ecs:pO157p01.
pg:5290916.
PATRICi18360435. VBIEscCol44059_5619.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y11831 Genomic DNA. Translation: CAA72517.1.
Y11275 Genomic DNA. Translation: CAA72142.1.
AF074613 Genomic DNA. Translation: AAC70099.1.
AB011549 Genomic DNA. Translation: BAA31757.3.
AY714880 Genomic DNA. Translation: AAU25886.1.
PIRiT42131.
RefSeqiNP_052607.1. NC_002128.1.
YP_001294684.1. NC_009602.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3UJZX-ray2.50A36-898[»]
4DNYX-ray1.61A132-251[»]
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-59647N.
STRINGi155864.L7031.

Protein family/group databases

MEROPSiM66.001.

Proteomic databases

PRIDEiO82882.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC70099; AAC70099; Z_L7031.
BAA31757; BAA31757; BAA31757.
GeneIDi1789672.
5290916.
KEGGiece:Z_L7031.
ecs:pO157p01.
pg:5290916.
PATRICi18360435. VBIEscCol44059_5619.

Phylogenomic databases

eggNOGiENOG4108MA4. Bacteria.
ENOG410XSA0. LUCA.
HOGENOMiHOG000272937.
OMAiSVMNKFH.
OrthoDBiEOG66F033.

Family and domain databases

InterProiIPR019503. Peptidase_M66_dom.
[Graphical view]
PfamiPF10462. Peptidase_M66. 1 hit.
[Graphical view]
PROSITEiPS51694. PEPTIDASE_M66. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Brunder W.
    Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
  2. "The complete DNA sequence and analysis of the large virulence plasmid of Escherichia coli O157:H7."
    Burland V., Shao Y., Perna N.T., Plunkett G. III, Sofia H.J., Blattner F.R.
    Nucleic Acids Res. 26:4196-4204(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
  3. "Complete nucleotide sequences of 93-kb and 3.3-kb plasmids of an enterohemorrhagic Escherichia coli O157:H7 derived from Sakai outbreak."
    Makino K., Ishii K., Yasunaga T., Hattori M., Yokoyama K., Yatsudo H.C., Kubota Y., Yamaichi Y., Iida T., Yamamoto K., Honda T., Han C.G., Ohtsubo A., Kasamatsu M., Hayashi T., Kuhara S., Shinagawa H.
    DNA Res. 5:1-9(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.
  4. "The StcE protease contributes to intimate adherence of enterohemorrhagic Escherichia coli O157:H7 to host cells."
    Grys T.E., Siegel M.B., Lathem W.W., Welch R.A.
    Infect. Immun. 73:1295-1303(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 36-898, FUNCTION.
    Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
  5. "The locus of enterocyte effacement (LEE)-encoded regulator controls expression of both LEE- and non-LEE-encoded virulence factors in enteropathogenic and enterohemorrhagic Escherichia coli."
    Elliott S.J., Sperandio V., Giron J.A., Shin S., Mellies J.L., Wainwright L., Hutcheson S.W., McDaniel T.K., Kaper J.B.
    Infect. Immun. 68:6115-6126(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  6. "StcE, a metalloprotease secreted by Escherichia coli O157:H7, specifically cleaves C1 esterase inhibitor."
    Lathem W.W., Grys T.E., Witowski S.E., Torres A.G., Kaper J.B., Tarr P.I., Welch R.A.
    Mol. Microbiol. 45:277-288(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, COFACTOR, SUBCELLULAR LOCATION, INDUCTION, MUTAGENESIS OF GLU-447.
    Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
  7. "Potentiation of C1 esterase inhibitor by StcE, a metalloprotease secreted by Escherichia coli O157:H7."
    Lathem W.W., Bergsbaken T., Welch R.A.
    J. Exp. Med. 199:1077-1087(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
    Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
  8. "Characterization of the StcE protease activity of Escherichia coli O157:H7."
    Grys T.E., Walters L.L., Welch R.A.
    J. Bacteriol. 188:4646-4653(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CHARACTERIZATION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES.
    Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.

Entry informationi

Entry nameiSTCE_ECO57
AccessioniPrimary (citable) accession number: O82882
Secondary accession number(s): Q647K0
, Q799Q8, Q7BSW2, Q9ZAL1, Q9ZGU1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: November 1, 1999
Last modified: January 20, 2016
This is version 81 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Is resistant to proteolytic degradation by trypsin, chymotrypsin, human and bacterial elastase, but not by the fungal protease proteinase K.
Cleavage of SERPING1 occurs within its heavily glycosylated N-terminal region and is different to that of elastase.

Keywords - Technical termi

3D-structure, Complete proteome, Plasmid

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. 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.