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Protein

Serine protease EspP

Gene

espP

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

Functioni

Serine protease capable of cleaving pepsin A and human coagulation factor V, which may contribute to the mucosal hemorrhage observed in hemorrhagic colitis.2 Publications

Enzyme regulationi

Inhibition of cytotoxic activity by phenylmethylsulfonyl fluoride.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei127 – 1271Charge relay systemPROSITE-ProRule annotation
Active sitei156 – 1561Charge relay systemPROSITE-ProRule annotation
Active sitei263 – 2631Charge relay systemPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Virulence

Enzyme and pathway databases

BioCyciECOL386585:GJFA-5453-MONOMER.

Protein family/group databases

MEROPSiS06.002.
TCDBi1.B.12.4.3. the autotransporter-1 (at-1) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine protease EspP (EC:3.4.21.-)
Cleaved into the following 2 chains:
Alternative name(s):
Extracellular serine protease plasmid-encoded EspP
Gene namesi
Name:espP
Ordered Locus Names:L7020, ECO57PM78
Encoded oniPlasmid pO1570 Publication
OrganismiEscherichia coli O157:H7
Taxonomic identifieri83334 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000558 Componenti: Plasmid pO157
  • UP000002519 Componenti: Plasmid pO157

Subcellular locationi

Autotransporter protein EspP translocator :

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell outer membrane, Membrane, Periplasm, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 55551 PublicationAdd
BLAST
Chaini56 – 13001245Serine protease EspPPRO_0000387594Add
BLAST
Chaini56 – 1023968Secreted autotransporter protein EspPPRO_0000042020Add
BLAST
Chaini1024 – 1300277Autotransporter protein EspP translocatorBy similarityPRO_0000042021Add
BLAST

Post-translational modificationi

Cleaved to release the mature protein from the outer membrane.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei1023 – 10242Cleavage

Keywords - PTMi

Zymogen

Expressioni

Inductioni

Expression is optimal at 37 degrees Celsius, and inhibited at 20 degrees Celsius. It is dependent on both temperature and pH.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
surAP0ABZ83EBI-6408724,EBI-6408783

Protein-protein interaction databases

IntActiQ7BSW5. 4 interactions.
STRINGi155864.L7020.

Structurei

Secondary structure

1
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi57 – 593Combined sources
Beta strandi61 – 633Combined sources
Helixi65 – 739Combined sources
Beta strandi86 – 883Combined sources
Beta strandi94 – 963Combined sources
Beta strandi121 – 1255Combined sources
Helixi126 – 1283Combined sources
Helixi133 – 1364Combined sources
Beta strandi137 – 1404Combined sources
Beta strandi143 – 15311Combined sources
Turni154 – 1563Combined sources
Beta strandi157 – 1648Combined sources
Helixi182 – 1898Combined sources
Beta strandi191 – 1988Combined sources
Beta strandi200 – 2056Combined sources
Beta strandi208 – 2136Combined sources
Beta strandi216 – 2205Combined sources
Helixi227 – 2293Combined sources
Beta strandi231 – 24818Combined sources
Beta strandi251 – 2544Combined sources
Beta strandi266 – 2716Combined sources
Turni272 – 2754Combined sources
Beta strandi276 – 28813Combined sources
Helixi290 – 2923Combined sources
Beta strandi294 – 3007Combined sources
Helixi303 – 31210Combined sources
Beta strandi314 – 3185Combined sources
Beta strandi324 – 3285Combined sources
Beta strandi331 – 3377Combined sources
Beta strandi344 – 3518Combined sources
Beta strandi353 – 3597Combined sources
Beta strandi368 – 3703Combined sources
Beta strandi375 – 3795Combined sources
Beta strandi384 – 3885Combined sources
Beta strandi390 – 3923Combined sources
Beta strandi397 – 4004Combined sources
Beta strandi402 – 4043Combined sources
Beta strandi410 – 42011Combined sources
Beta strandi428 – 43710Combined sources
Beta strandi446 – 45712Combined sources
Beta strandi466 – 4683Combined sources
Beta strandi471 – 4733Combined sources
Beta strandi478 – 4814Combined sources
Beta strandi487 – 4904Combined sources
Beta strandi499 – 5024Combined sources
Beta strandi505 – 5073Combined sources
Beta strandi509 – 5135Combined sources
Beta strandi519 – 5213Combined sources
Beta strandi523 – 53412Combined sources
Beta strandi544 – 5463Combined sources
Beta strandi548 – 5514Combined sources
Beta strandi556 – 5605Combined sources
Beta strandi562 – 5654Combined sources
Helixi596 – 6038Combined sources
Helixi605 – 6117Combined sources
Helixi614 – 6174Combined sources
Beta strandi632 – 64312Combined sources
Beta strandi645 – 6484Combined sources
Beta strandi652 – 66211Combined sources
Beta strandi664 – 6685Combined sources
Beta strandi670 – 6756Combined sources
Turni676 – 6794Combined sources
Turni684 – 6874Combined sources
Beta strandi693 – 6975Combined sources
Beta strandi702 – 7065Combined sources
Beta strandi708 – 7125Combined sources
Beta strandi714 – 7174Combined sources
Beta strandi721 – 7255Combined sources
Beta strandi729 – 7335Combined sources
Beta strandi735 – 7384Combined sources
Beta strandi743 – 7464Combined sources
Beta strandi750 – 7545Combined sources
Beta strandi756 – 76510Combined sources
Beta strandi777 – 78711Combined sources
Beta strandi793 – 81018Combined sources
Beta strandi813 – 8186Combined sources
Helixi832 – 8398Combined sources
Beta strandi842 – 8487Combined sources
Beta strandi850 – 86617Combined sources
Beta strandi870 – 87910Combined sources
Beta strandi881 – 8844Combined sources
Beta strandi895 – 90511Combined sources
Beta strandi907 – 9159Combined sources
Beta strandi919 – 9279Combined sources
Beta strandi931 – 9399Combined sources
Beta strandi943 – 9453Combined sources
Beta strandi949 – 9557Combined sources
Helixi960 – 9623Combined sources
Beta strandi963 – 9653Combined sources
Beta strandi975 – 9839Combined sources
Beta strandi985 – 99713Combined sources
Helixi999 – 102022Combined sources
Helixi1025 – 10295Combined sources
Beta strandi1038 – 105215Combined sources
Helixi1053 – 10553Combined sources
Beta strandi1056 – 107318Combined sources
Beta strandi1076 – 109318Combined sources
Beta strandi1096 – 111318Combined sources
Beta strandi1116 – 113419Combined sources
Helixi1136 – 11383Combined sources
Beta strandi1140 – 115718Combined sources
Beta strandi1159 – 117820Combined sources
Beta strandi1182 – 11876Combined sources
Beta strandi1190 – 11967Combined sources
Beta strandi1202 – 121615Combined sources
Beta strandi1219 – 123315Combined sources
Beta strandi1238 – 12425Combined sources
Beta strandi1247 – 12515Combined sources
Beta strandi1256 – 126813Combined sources
Turni1269 – 12713Combined sources
Beta strandi1272 – 130029Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2QOMX-ray2.66A/B1024-1300[»]
3SLJX-ray2.48A999-1300[»]
3SLOX-ray2.52A999-1300[»]
3SLTX-ray2.46A999-1300[»]
3SZEX-ray2.50A56-1023[»]
ProteinModelPortaliQ7BSW5.
SMRiQ7BSW5. Positions 538-668, 842-999, 1024-1300.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ7BSW5.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini57 – 311255Peptidase S6PROSITE-ProRule annotationAdd
BLAST
Domaini1034 – 1300267AutotransporterPROSITE-ProRule annotationAdd
BLAST

Domaini

The signal peptide, cleaved at the inner membrane, guides the autotransporter protein to the periplasmic space. Then, insertion of the C-terminal translocator domain in the outer membrane forms a hydrophilic pore for the translocation of the passenger domain to the bacterial cell surface, with subsequent cleavage (PubMed:15615856).1 Publication

Sequence similaritiesi

Contains 1 autotransporter (TC 1.B.12) domain. [View classification]PROSITE-ProRule annotation
Contains 1 peptidase S6 domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane beta strand

Phylogenomic databases

eggNOGiENOG4105I1J. Bacteria.
COG3468. LUCA.
HOGENOMiHOG000117212.
KOiK12684.
OMAiLVMQGHA.
OrthoDBiEOG6S7XQ2.

Family and domain databases

Gene3Di2.160.20.20. 1 hit.
2.40.128.130. 1 hit.
InterProiIPR005546. Autotransporte_beta.
IPR024973. ESPR.
IPR006315. OM_autotransptr_brl.
IPR012332. P22_tailspike_C-like.
IPR011050. Pectin_lyase_fold/virulence.
IPR000710. Peptidase_S6.
IPR030396. Peptidase_S6_dom.
[Graphical view]
PfamiPF03797. Autotransporter. 1 hit.
PF13018. ESPR. 1 hit.
PF02395. Peptidase_S6. 1 hit.
[Graphical view]
PRINTSiPR00921. IGASERPTASE.
SMARTiSM00869. Autotransporter. 1 hit.
[Graphical view]
SUPFAMiSSF103515. SSF103515. 1 hit.
SSF51126. SSF51126. 2 hits.
TIGRFAMsiTIGR01414. autotrans_barl. 1 hit.
PROSITEiPS51208. AUTOTRANSPORTER. 1 hit.
PS51691. PEPTIDASE_S6. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q7BSW5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNKIYSLKYS HITGGLIAVS ELSGRVSSRA TGKKKHKRIL ALCFLGLLQS
60 70 80 90 100
SYSFASQMDI SNFYIRDYMD FAQNKGIFQA GATNIEIVKK DGSTLKLPEV
110 120 130 140 150
PFPDFSPVAN KGSTTSIGGA YSITATHNTK NHHSVATQNW GNSTYKQTDW
160 170 180 190 200
NTSHPDFAVS RLDKFVVETR GATEGADISL SKQQALERYG VNYKGEKKLI
210 220 230 240 250
AFRAGSGVVS VKKNGRITPF NEVSYKPEML NGSFVHIDDW SGWLILTNNQ
260 270 280 290 300
FDEFNNIASQ GDSGSALFVY DNQKKKWVVA GTVWGIYNYA NGKNHAAYSK
310 320 330 340 350
WNQTTIDNLK NKYSYNVDMS GAQVATIENG KLTGTGSDTT DIKNKDLIFT
360 370 380 390 400
GGGDILLKSS FDNGAGGLVF NDKKTYRVNG DDFTFKGAGV DTRNGSTVEW
410 420 430 440 450
NIRYDNKDNL HKIGDGTLDV RKTQNTNLKT GEGLVILGAE KTFNNIYITS
460 470 480 490 500
GDGTVRLNAE NALSGGEYNG IFFAKNGGTL DLNGYNQSFN KIAATDSGAV
510 520 530 540 550
ITNTSTKKSI LSLNNTADYI YHGNINGNLD VLQHHETKKE NRRLILDGGV
560 570 580 590 600
DTTNDISLRN TQLSMQGHAT EHAIYRDGAF SCSLPAPMRF LCGSDYVAGM
610 620 630 640 650
QNTEADAVKQ NGNAYKTNNA VSDLSQPDWE TGTFRFGTLH LENSDFSVGR
660 670 680 690 700
NANVIGDIQA SKSNITIGDT TAYIDLHAGK NITGDGFGFR QNIVRGNSQG
710 720 730 740 750
ETLFTGGITA EDSTIVIKDK AKALFSNYVY LLNTKATIEN GADVTTQSGM
760 770 780 790 800
FSTSDISISG NLSMTGNPDK DNKFEPSIYL NDASYLLTDD SARLVAKNKA
810 820 830 840 850
SVVGDIHSTK SASIMFGHDE SDLSQLSDRT SKGLALGLLG GFDVSYRGSV
860 870 880 890 900
NAPSASATMN NTWWQLTGDS ALKTLKSTNS MVYFTDSANN KKFHTLTVDE
910 920 930 940 950
LATSNSAYAM RTNLSESDKL EVKKHLSGEN NILLVDFLQK PTPEKQLNIE
960 970 980 990 1000
LVSAPKDTNE NVFKASKQTI GFSDVTPVIT TRETDDKITW SLTGYNTVAN
1010 1020 1030 1040 1050
KEATRNAAAL FSVDYKAFLN EVNNLNKRMG DLRDINGEAG AWARIMSGTG
1060 1070 1080 1090 1100
SASGGFSDNY THVQVGVDKK HELDGLDLFT GFTVTHTDSS ASADVFSGKT
1110 1120 1130 1140 1150
KSVGAGLYAS AMFDSGAYID LIGKYVHHDN EYTATFAGLG TRDYSTHSWY
1160 1170 1180 1190 1200
AGAEAGYRYH VTEDAWIEPQ AELVYGSVSG KQFAWKDQGM HLSMKDKDYN
1210 1220 1230 1240 1250
PLIGRTGVDV GKSFSGKDWK VTARAGLGYQ FDLLANGETV LRDASGEKRI
1260 1270 1280 1290 1300
KGEKDSRMLM SVGLNAEIRD NVRFGLEFEK SAFGKYNVDN AVNANFRYSF
Length:1,300
Mass (Da):141,758
Last modified:July 5, 2004 - v1
Checksum:iE34D3F037DEC672F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X97542 Genomic DNA. Translation: CAA66144.1.
AF074613 Genomic DNA. Translation: AAC70088.1.
AB011549 Genomic DNA. Translation: BAA31836.1.
AJ010390 Genomic DNA. Translation: CAB42538.1.
PIRiT00317.
RefSeqiNP_052685.1. NC_002128.1.
WP_001034100.1. NZ_LKAL01000035.1.
YP_002756610.1. NC_012487.1.

Genome annotation databases

EnsemblBacteriaiAAC70088; AAC70088; Z_L7020.
BAA31836; BAA31836; BAA31836.
GeneIDi1789732.
7701441.
KEGGiece:Z_L7020.
ecs:pO157p78.
pg:7701441.
PATRICi18360417. VBIEscCol44059_5610.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X97542 Genomic DNA. Translation: CAA66144.1.
AF074613 Genomic DNA. Translation: AAC70088.1.
AB011549 Genomic DNA. Translation: BAA31836.1.
AJ010390 Genomic DNA. Translation: CAB42538.1.
PIRiT00317.
RefSeqiNP_052685.1. NC_002128.1.
WP_001034100.1. NZ_LKAL01000035.1.
YP_002756610.1. NC_012487.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2QOMX-ray2.66A/B1024-1300[»]
3SLJX-ray2.48A999-1300[»]
3SLOX-ray2.52A999-1300[»]
3SLTX-ray2.46A999-1300[»]
3SZEX-ray2.50A56-1023[»]
ProteinModelPortaliQ7BSW5.
SMRiQ7BSW5. Positions 538-668, 842-999, 1024-1300.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ7BSW5. 4 interactions.
STRINGi155864.L7020.

Protein family/group databases

MEROPSiS06.002.
TCDBi1.B.12.4.3. the autotransporter-1 (at-1) family.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC70088; AAC70088; Z_L7020.
BAA31836; BAA31836; BAA31836.
GeneIDi1789732.
7701441.
KEGGiece:Z_L7020.
ecs:pO157p78.
pg:7701441.
PATRICi18360417. VBIEscCol44059_5610.

Phylogenomic databases

eggNOGiENOG4105I1J. Bacteria.
COG3468. LUCA.
HOGENOMiHOG000117212.
KOiK12684.
OMAiLVMQGHA.
OrthoDBiEOG6S7XQ2.

Enzyme and pathway databases

BioCyciECOL386585:GJFA-5453-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ7BSW5.

Family and domain databases

Gene3Di2.160.20.20. 1 hit.
2.40.128.130. 1 hit.
InterProiIPR005546. Autotransporte_beta.
IPR024973. ESPR.
IPR006315. OM_autotransptr_brl.
IPR012332. P22_tailspike_C-like.
IPR011050. Pectin_lyase_fold/virulence.
IPR000710. Peptidase_S6.
IPR030396. Peptidase_S6_dom.
[Graphical view]
PfamiPF03797. Autotransporter. 1 hit.
PF13018. ESPR. 1 hit.
PF02395. Peptidase_S6. 1 hit.
[Graphical view]
PRINTSiPR00921. IGASERPTASE.
SMARTiSM00869. Autotransporter. 1 hit.
[Graphical view]
SUPFAMiSSF103515. SSF103515. 1 hit.
SSF51126. SSF51126. 2 hits.
TIGRFAMsiTIGR01414. autotrans_barl. 1 hit.
PROSITEiPS51208. AUTOTRANSPORTER. 1 hit.
PS51691. PEPTIDASE_S6. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "EspP, a novel extracellular serine protease of enterohaemorrhagic Escherichia coli O157:H7 cleaves human coagulation factor V."
    Brunder W., Schmidt H., Karch H.
    Mol. Microbiol. 24:767-778(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 56-65 AND 1024-1033, FUNCTION, ENZYME REGULATION.
    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 large plasmids of Shiga-toxin-producing Escherichia coli (STEC) are highly variable genetic elements."
    Brunder W., Schmidt H., Frosch M., Karch H.
    Microbiology 145:1005-1014(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 455-1300.
    Strain: O157:H7 / 3010/96 / EHEC.
  5. "Hydrophobic residues of the autotransporter EspP linker domain are important for outer membrane translocation of its passenger."
    Velarde J.J., Nataro J.P.
    J. Biol. Chem. 279:31495-31504(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS.
  6. "An unusual signal peptide facilitates late steps in the biogenesis of a bacterial autotransporter."
    Szabady R.L., Peterson J.H., Skillman K.M., Bernstein H.D.
    Proc. Natl. Acad. Sci. U.S.A. 102:221-226(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE SIGNAL PEPTIDE.
    Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.

Entry informationi

Entry nameiESPP_ECO57
AccessioniPrimary (citable) accession number: Q7BSW5
Secondary accession number(s): O32555, Q9S6R3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 27, 2005
Last sequence update: July 5, 2004
Last modified: May 11, 2016
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Mutagenesis experiments show the presence of a linker region, which is required for the translocation of the protease domain across the outer membrane. This linker region is located immediately upstream of the C-terminal helper domain.
The signal peptide may also act as a transient membrane anchor that prevents the protease domain from misfolding in the periplasm.

Caution

Strain 3010/96 exhibits a partial deletion of the gene.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, 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.