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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)DescriptionActionsGraphical viewLength
Metal bindingi446Zinc; catalyticBy similarity1
Active sitei4471
Metal bindingi450Zinc; catalyticBy similarity1
Metal bindingi456Zinc; catalyticBy similarity1

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
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)DescriptionActionsGraphical viewLength
Mutagenesisi447E → D: Prevents both cleavage and binding to SERPING1. Unable to aggregate T-cells. Still able to bind zinc. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 35Sequence analysisAdd BLAST35
ChainiPRO_000024814536 – 898Metalloprotease StcEAdd BLAST863

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

1898
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi42 – 44Combined sources3
Beta strandi54 – 56Combined sources3
Beta strandi59 – 72Combined sources14
Beta strandi82 – 86Combined sources5
Beta strandi88 – 96Combined sources9
Beta strandi99 – 101Combined sources3
Beta strandi103 – 108Combined sources6
Beta strandi114 – 119Combined sources6
Helixi123 – 125Combined sources3
Beta strandi146 – 148Combined sources3
Beta strandi150 – 153Combined sources4
Helixi156 – 160Combined sources5
Helixi161 – 163Combined sources3
Helixi168 – 174Combined sources7
Beta strandi178 – 185Combined sources8
Beta strandi191 – 194Combined sources4
Helixi199 – 201Combined sources3
Beta strandi205 – 211Combined sources7
Beta strandi216 – 220Combined sources5
Beta strandi223 – 227Combined sources5
Beta strandi232 – 238Combined sources7
Beta strandi241 – 244Combined sources4
Helixi249 – 252Combined sources4
Beta strandi253 – 255Combined sources3
Beta strandi260 – 264Combined sources5
Helixi266 – 268Combined sources3
Beta strandi274 – 279Combined sources6
Beta strandi282 – 286Combined sources5
Beta strandi296 – 308Combined sources13
Helixi315 – 318Combined sources4
Helixi320 – 327Combined sources8
Beta strandi333 – 340Combined sources8
Beta strandi343 – 349Combined sources7
Beta strandi355 – 358Combined sources4
Helixi370 – 374Combined sources5
Helixi375 – 380Combined sources6
Helixi381 – 389Combined sources9
Beta strandi393 – 397Combined sources5
Beta strandi408 – 418Combined sources11
Beta strandi421 – 424Combined sources4
Beta strandi427 – 430Combined sources4
Beta strandi433 – 435Combined sources3
Helixi441 – 450Combined sources10
Turni451 – 453Combined sources3
Helixi460 – 464Combined sources5
Beta strandi471 – 473Combined sources3
Beta strandi477 – 479Combined sources3
Turni480 – 483Combined sources4
Beta strandi484 – 486Combined sources3
Beta strandi488 – 493Combined sources6
Beta strandi498 – 500Combined sources3
Beta strandi503 – 505Combined sources3
Beta strandi511 – 513Combined sources3
Turni517 – 520Combined sources4
Helixi535 – 546Combined sources12
Beta strandi548 – 551Combined sources4
Beta strandi558 – 563Combined sources6
Turni564 – 567Combined sources4
Beta strandi568 – 571Combined sources4
Beta strandi682 – 695Combined sources14
Beta strandi709 – 716Combined sources8
Beta strandi755 – 762Combined sources8
Helixi763 – 765Combined sources3
Beta strandi793 – 798Combined sources6
Beta strandi806 – 811Combined sources6
Turni812 – 814Combined sources3
Beta strandi817 – 821Combined sources5
Turni832 – 836Combined sources5
Beta strandi839 – 843Combined sources5
Beta strandi847 – 857Combined sources11
Beta strandi862 – 865Combined sources4
Beta strandi867 – 869Combined sources3
Helixi871 – 873Combined sources3
Beta strandi874 – 878Combined sources5
Beta strandi880 – 885Combined sources6
Beta strandi891 – 897Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3UJZX-ray2.50A36-898[»]
4DNYX-ray1.61A132-251[»]
SMRiO82882.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini296 – 551Peptidase M66Add BLAST256

Sequence similaritiesi

Contains 1 peptidase M66 domain.Curated

Keywords - Domaini

Signal

Phylogenomic databases

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

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.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3UJZX-ray2.50A36-898[»]
4DNYX-ray1.61A132-251[»]
SMRiO82882.
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.
PATRICi18360435. VBIEscCol44059_5619.

Phylogenomic databases

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

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...

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: November 30, 2016
This is version 85 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.