STCE_ECO57
ID STCE_ECO57 Reviewed; 898 AA.
AC O82882; Q647K0; Q799Q8; Q7BSW2; Q9ZAL1; Q9ZGU1;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Metalloprotease StcE;
DE EC=3.4.24.-;
DE AltName: Full=Mucinase;
DE AltName: Full=Neutral zinc metalloprotease StcE;
DE AltName: Full=Secreted protease of C1 esterase inhibitor from EHEC;
DE Flags: Precursor;
GN Name=stcE; Synonyms=tagA; OrderedLocusNames=L7031, ECO57PM83;
OS Escherichia coli O157:H7.
OG Plasmid pO157.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RA Brunder W.;
RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=9722640; DOI=10.1093/nar/26.18.4196;
RA Burland V., Shao Y., Perna N.T., Plunkett G. III, Sofia H.J.,
RA Blattner F.R.;
RT "The complete DNA sequence and analysis of the large virulence plasmid of
RT Escherichia coli O157:H7.";
RL Nucleic Acids Res. 26:4196-4204(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=9628576; DOI=10.1093/dnares/5.1.1;
RA Makino K., Ishii K., Yasunaga T., Hattori M., Yokoyama K., Yatsudo H.C.,
RA Kubota Y., Yamaichi Y., Iida T., Yamamoto K., Honda T., Han C.G.,
RA Ohtsubo A., Kasamatsu M., Hayashi T., Kuhara S., Shinagawa H.;
RT "Complete nucleotide sequences of 93-kb and 3.3-kb plasmids of an
RT enterohemorrhagic Escherichia coli O157:H7 derived from Sakai outbreak.";
RL DNA Res. 5:1-9(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 36-898, AND FUNCTION.
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=15731026; DOI=10.1128/iai.73.3.1295-1303.2005;
RA Grys T.E., Siegel M.B., Lathem W.W., Welch R.A.;
RT "The StcE protease contributes to intimate adherence of enterohemorrhagic
RT Escherichia coli O157:H7 to host cells.";
RL Infect. Immun. 73:1295-1303(2005).
RN [5]
RP INDUCTION.
RX PubMed=11035714; DOI=10.1128/iai.68.11.6115-6126.2000;
RA Elliott S.J., Sperandio V., Giron J.A., Shin S., Mellies J.L.,
RA Wainwright L., Hutcheson S.W., McDaniel T.K., Kaper J.B.;
RT "The locus of enterocyte effacement (LEE)-encoded regulator controls
RT expression of both LEE- and non-LEE-encoded virulence factors in
RT enteropathogenic and enterohemorrhagic Escherichia coli.";
RL Infect. Immun. 68:6115-6126(2000).
RN [6]
RP FUNCTION, COFACTOR, SUBCELLULAR LOCATION, INDUCTION, AND MUTAGENESIS OF
RP GLU-447.
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=12123444; DOI=10.1046/j.1365-2958.2002.02997.x;
RA Lathem W.W., Grys T.E., Witowski S.E., Torres A.G., Kaper J.B., Tarr P.I.,
RA Welch R.A.;
RT "StcE, a metalloprotease secreted by Escherichia coli O157:H7, specifically
RT cleaves C1 esterase inhibitor.";
RL Mol. Microbiol. 45:277-288(2002).
RN [7]
RP FUNCTION.
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=15096536; DOI=10.1084/jem.20030255;
RA Lathem W.W., Bergsbaken T., Welch R.A.;
RT "Potentiation of C1 esterase inhibitor by StcE, a metalloprotease secreted
RT by Escherichia coli O157:H7.";
RL J. Exp. Med. 199:1077-1087(2004).
RN [8]
RP FUNCTION, CHARACTERIZATION, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=16788173; DOI=10.1128/jb.01806-05;
RA Grys T.E., Walters L.L., Welch R.A.;
RT "Characterization of the StcE protease activity of Escherichia coli
RT O157:H7.";
RL J. Bacteriol. 188:4646-4653(2006).
CC -!- FUNCTION: Virulence factor that contributes to intimate adherence of
CC enterohemorrhagic E.coli (EHEC) O157:H7 to host cells. Is able to
CC cleave the secreted human mucin 7 (MUC7) and the glycoprotein 340
CC (DMBT1/GP340). Also cleaves human C1 inhibitor (SERPING1), a regulator
CC of multiple inflammatory pathways, and binds and localizes it to
CC bacterial and host cell surfaces, protecting them from complement-
CC mediated lysis. Therefore, the current model proposes two roles for
CC StcE during infection: it acts first as a mucinase, allowing passage of
CC EHEC through the oral cavity by cleaving the salivary glycoproteins
CC that are responsible for bacterial aggregation. Similarly, in the
CC colon, StcE cleaves the glycoproteins that protect the intestinal
CC epithelial surface, allowing EHEC to come into close contact with host
CC cell membranes. Secondly, it acts as an anti-inflammatory agent by
CC localizing SERPING1 to cell membranes. {ECO:0000269|PubMed:12123444,
CC ECO:0000269|PubMed:15096536, ECO:0000269|PubMed:15731026,
CC ECO:0000269|PubMed:16788173}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:12123444, ECO:0000269|PubMed:16788173};
CC Note=Binds 1 zinc ion per subunit. Does not contain structural calcium,
CC which is often associated with other metalloproteases.
CC {ECO:0000269|PubMed:12123444, ECO:0000269|PubMed:16788173};
CC -!- ACTIVITY REGULATION: Inhibited by divalent cation chelators such as BPS
CC and EDTA.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.13 uM for MUC7 {ECO:0000269|PubMed:16788173};
CC KM=0.27 uM for SERPING1 {ECO:0000269|PubMed:16788173};
CC Vmax=70.2 nM/min/ug enzyme for MUC7 cleavage
CC {ECO:0000269|PubMed:16788173};
CC Vmax=66.8 nM/min/ug enzyme for SERPING1 cleavage
CC {ECO:0000269|PubMed:16788173};
CC Note=Proteolytic activity is 2.5-fold more efficient with the
CC secreted mucin MUC7 than with SERPING1.;
CC pH dependence:
CC Optimum pH is 6.5-7.0. Active from pH 6.1 to 9.0.
CC {ECO:0000269|PubMed:16788173};
CC Temperature dependence:
CC Optimum temperature is 37-42 degrees Celsius. Active from 4 to 55
CC degrees Celsius. Inactive above 60 degrees Celsius.
CC {ECO:0000269|PubMed:16788173};
CC -!- INTERACTION:
CC O82882; P05155: SERPING1; Xeno; NbExp=3; IntAct=EBI-15979286, EBI-1223454;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12123444}.
CC Note=Secreted via the etp type II secretion pathway.
CC -!- INDUCTION: Up-regulated by the LEE (locus of enterocyte effacement)-
CC encoded regulator ler. {ECO:0000269|PubMed:11035714,
CC ECO:0000269|PubMed:12123444}.
CC -!- MISCELLANEOUS: Is resistant to proteolytic degradation by trypsin,
CC chymotrypsin, human and bacterial elastase, but not by the fungal
CC protease proteinase K.
CC -!- MISCELLANEOUS: Cleavage of SERPING1 occurs within its heavily
CC glycosylated N-terminal region and is different to that of elastase.
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DR EMBL; Y11831; CAA72517.1; -; Genomic_DNA.
DR EMBL; Y11275; CAA72142.1; -; Genomic_DNA.
DR EMBL; AF074613; AAC70099.1; -; Genomic_DNA.
DR EMBL; AB011549; BAA31757.3; -; Genomic_DNA.
DR EMBL; AY714880; AAU25886.1; -; Genomic_DNA.
DR PIR; T42131; T42131.
DR RefSeq; NP_052607.1; NC_002128.1.
DR RefSeq; WP_001358886.1; NZ_SWKA01000002.1.
DR RefSeq; YP_001294684.1; NC_009602.1.
DR PDB; 3UJZ; X-ray; 2.50 A; A=36-898.
DR PDB; 4DNY; X-ray; 1.61 A; A=132-251.
DR PDBsum; 3UJZ; -.
DR PDBsum; 4DNY; -.
DR AlphaFoldDB; O82882; -.
DR SMR; O82882; -.
DR DIP; DIP-59647N; -.
DR IntAct; O82882; 1.
DR STRING; 155864.EDL933_p0029; -.
DR MEROPS; M66.001; -.
DR EnsemblBacteria; AAC70099; AAC70099; Z_L7031.
DR EnsemblBacteria; BAA31757; BAA31757; BAA31757.
DR GeneID; 1789672; -.
DR KEGG; ece:Z_L7031; -.
DR KEGG; ecs:pO157p01; -.
DR eggNOG; ENOG502ZA83; Bacteria.
DR OMA; MNKFHVN; -.
DR Proteomes; UP000000558; Plasmid pO157.
DR Proteomes; UP000002519; Plasmid pO157.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR019503; Peptidase_M66_dom.
DR InterPro; IPR040966; StcE_C.
DR InterPro; IPR022218; TagA_dom.
DR Pfam; PF17945; Crystall_4; 1.
DR Pfam; PF12561; TagA; 1.
DR PROSITE; PS51694; PEPTIDASE_M66; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Metal-binding; Metalloprotease; Plasmid; Protease;
KW Reference proteome; Secreted; Signal; Virulence; Zinc.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..898
FT /note="Metalloprotease StcE"
FT /id="PRO_0000248145"
FT DOMAIN 296..551
FT /note="Peptidase M66"
FT ACT_SITE 447
FT BINDING 446
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 450
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 456
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT MUTAGEN 447
FT /note="E->D: Prevents both cleavage and binding to
FT SERPING1. Unable to aggregate T-cells. Still able to bind
FT zinc."
FT /evidence="ECO:0000269|PubMed:12123444"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:3UJZ"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:3UJZ"
FT STRAND 59..72
FT /evidence="ECO:0007829|PDB:3UJZ"
FT STRAND 82..86
FT /evidence="ECO:0007829|PDB:3UJZ"
FT STRAND 88..96
FT /evidence="ECO:0007829|PDB:3UJZ"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:3UJZ"
FT STRAND 103..108
FT /evidence="ECO:0007829|PDB:3UJZ"
FT STRAND 114..119
FT /evidence="ECO:0007829|PDB:3UJZ"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:3UJZ"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:4DNY"
FT STRAND 150..153
FT /evidence="ECO:0007829|PDB:4DNY"
FT HELIX 156..160
FT /evidence="ECO:0007829|PDB:4DNY"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:4DNY"
FT HELIX 168..174
FT /evidence="ECO:0007829|PDB:4DNY"
FT STRAND 178..185
FT /evidence="ECO:0007829|PDB:4DNY"
FT STRAND 191..194
FT /evidence="ECO:0007829|PDB:4DNY"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:4DNY"
FT STRAND 205..211
FT /evidence="ECO:0007829|PDB:4DNY"
FT STRAND 216..220
FT /evidence="ECO:0007829|PDB:4DNY"
FT STRAND 223..227
FT /evidence="ECO:0007829|PDB:4DNY"
FT STRAND 232..238
FT /evidence="ECO:0007829|PDB:4DNY"
FT STRAND 241..244
FT /evidence="ECO:0007829|PDB:4DNY"
FT HELIX 249..252
FT /evidence="ECO:0007829|PDB:3UJZ"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:3UJZ"
FT STRAND 260..264
FT /evidence="ECO:0007829|PDB:3UJZ"
FT HELIX 266..268
FT /evidence="ECO:0007829|PDB:3UJZ"
FT STRAND 274..279
FT /evidence="ECO:0007829|PDB:3UJZ"
FT STRAND 282..286
FT /evidence="ECO:0007829|PDB:3UJZ"
FT STRAND 296..308
FT /evidence="ECO:0007829|PDB:3UJZ"
FT HELIX 315..318
FT /evidence="ECO:0007829|PDB:3UJZ"
FT HELIX 320..327
FT /evidence="ECO:0007829|PDB:3UJZ"
FT STRAND 333..340
FT /evidence="ECO:0007829|PDB:3UJZ"
FT STRAND 343..349
FT /evidence="ECO:0007829|PDB:3UJZ"
FT STRAND 355..358
FT /evidence="ECO:0007829|PDB:3UJZ"
FT HELIX 370..374
FT /evidence="ECO:0007829|PDB:3UJZ"
FT HELIX 375..380
FT /evidence="ECO:0007829|PDB:3UJZ"
FT HELIX 381..389
FT /evidence="ECO:0007829|PDB:3UJZ"
FT STRAND 393..397
FT /evidence="ECO:0007829|PDB:3UJZ"
FT STRAND 408..418
FT /evidence="ECO:0007829|PDB:3UJZ"
FT STRAND 421..424
FT /evidence="ECO:0007829|PDB:3UJZ"
FT STRAND 427..430
FT /evidence="ECO:0007829|PDB:3UJZ"
FT STRAND 433..435
FT /evidence="ECO:0007829|PDB:3UJZ"
FT HELIX 441..450
FT /evidence="ECO:0007829|PDB:3UJZ"
FT TURN 451..453
FT /evidence="ECO:0007829|PDB:3UJZ"
FT HELIX 460..464
FT /evidence="ECO:0007829|PDB:3UJZ"
FT STRAND 471..473
FT /evidence="ECO:0007829|PDB:3UJZ"
FT STRAND 477..479
FT /evidence="ECO:0007829|PDB:3UJZ"
FT TURN 480..483
FT /evidence="ECO:0007829|PDB:3UJZ"
FT STRAND 484..486
FT /evidence="ECO:0007829|PDB:3UJZ"
FT STRAND 488..493
FT /evidence="ECO:0007829|PDB:3UJZ"
FT STRAND 498..500
FT /evidence="ECO:0007829|PDB:3UJZ"
FT STRAND 503..505
FT /evidence="ECO:0007829|PDB:3UJZ"
FT STRAND 511..513
FT /evidence="ECO:0007829|PDB:3UJZ"
FT TURN 517..520
FT /evidence="ECO:0007829|PDB:3UJZ"
FT HELIX 535..546
FT /evidence="ECO:0007829|PDB:3UJZ"
FT STRAND 548..551
FT /evidence="ECO:0007829|PDB:3UJZ"
FT STRAND 558..563
FT /evidence="ECO:0007829|PDB:3UJZ"
FT TURN 564..567
FT /evidence="ECO:0007829|PDB:3UJZ"
FT STRAND 568..571
FT /evidence="ECO:0007829|PDB:3UJZ"
FT STRAND 682..695
FT /evidence="ECO:0007829|PDB:3UJZ"
FT STRAND 709..716
FT /evidence="ECO:0007829|PDB:3UJZ"
FT STRAND 755..762
FT /evidence="ECO:0007829|PDB:3UJZ"
FT HELIX 763..765
FT /evidence="ECO:0007829|PDB:3UJZ"
FT STRAND 793..798
FT /evidence="ECO:0007829|PDB:3UJZ"
FT STRAND 806..811
FT /evidence="ECO:0007829|PDB:3UJZ"
FT TURN 812..814
FT /evidence="ECO:0007829|PDB:3UJZ"
FT STRAND 817..821
FT /evidence="ECO:0007829|PDB:3UJZ"
FT TURN 832..836
FT /evidence="ECO:0007829|PDB:3UJZ"
FT STRAND 839..843
FT /evidence="ECO:0007829|PDB:3UJZ"
FT STRAND 847..857
FT /evidence="ECO:0007829|PDB:3UJZ"
FT STRAND 862..865
FT /evidence="ECO:0007829|PDB:3UJZ"
FT STRAND 867..869
FT /evidence="ECO:0007829|PDB:3UJZ"
FT HELIX 871..873
FT /evidence="ECO:0007829|PDB:3UJZ"
FT STRAND 874..878
FT /evidence="ECO:0007829|PDB:3UJZ"
FT STRAND 880..885
FT /evidence="ECO:0007829|PDB:3UJZ"
FT STRAND 891..897
FT /evidence="ECO:0007829|PDB:3UJZ"
SQ SEQUENCE 898 AA; 99548 MW; 3C1AE23E3EAE1FAB CRC64;
MNTKMNERWR TPMKLKYLSC TILAPLAIGV FSATAADNNS AIYFNTSQPI NDLQGSLAAE
VKFAQSQILP AHPKEGDSQP HLTSLRKSLL LVRPVKADDK TPVQVEARDD NNKILGTLTL
YPPSSLPDTI YHLDGVPEGG IDFTPHNGTK KIINTVAEVN KLSDASGSSI HSHLTNNALV
EIHTANGRWV RDIYLPQGPD LEGKMVRFVS SAGYSSTVFY GDRKVTLSVG NTLLFKYVNG
QWFRSGELEN NRITYAQHIW SAELPAHWIV PGLNLVIKQG NLSGRLNDIK IGAPGELLLH
TIDIGMLTTP RDRFDFAKDK EAHREYFQTI PVSRMIVNNY APLHLKEVML PTGELLTDMD
PGNGGWHSGT MRQRIGKELV SHGIDNANYG LNSTAGLGEN SHPYVVAQLA AHNSRGNYAN
GIQVHGGSGG GGIVTLDSTL GNEFSHEVGH NYGLGHYVDG FKGSVHRSAE NNNSTWGWDG
DKKRFIPNFY PSQTNEKSCL NNQCQEPFDG HKFGFDAMAG GSPFSAANRF TMYTPNSSAI
IQRFFENKAV FDSRSSTGFS KWNADTQEME PYEHTIDRAE QITASVNELS ESKMAELMAE
YAVVKVHMWN GNWTRNIYIP TASADNRGSI LTINHEAGYN SYLFINGDEK VVSQGYKKSF
VSDGQFWKER DVVDTREARK PEQFGVPVTT LVGYYDPEGT LSSYIYPAMY GAYGFTYSDD
SQNLSDNDCQ LQVDTKEGQL RFRLANHRAN NTVMNKFHIN VPTESQPTQA TLVCNNKILD
TKSLTPAPEG LTYTVNGQAL PAKENEGCIV SVNSGKRYCL PVGQRSGYSL PDWIVGQEVY
VDSGAKAKVL LSDWDNLSYN RIGEFVGNVN PADMKKVKAW NGQYLDFSKP RSMRVVYK
