Serine protease espP precursor - Escherichia coli O157:H7

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Q7BSW5 (ESPP_ECO57) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 57. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Serine protease espP
EC=3.4.21.-

Cleaved into the following 2 chains:

Secreted autotransporter protein espP
Alternative name(s):
Extracellular serine protease plasmid-encoded espP
Autotransporter protein espP translocator

Gene names

Name:	espP
Ordered Locus Names:	L7020, ECO57PM78

Encoded on

Plasmid pO157

Organism

Escherichia coli O157:H7 [Complete proteome] [HAMAP]

Taxonomic identifier

83334 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	1300 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	Serine protease capable of cleaving pepsin A and human coagulation factor V, which may contribute to the mucosal hemorrhage observed in hemorrhagic colitis. Ref.1 Ref.6
Enzyme regulation	Inhibition of cytotoxic activity by phenylmethylsulfonyl fluoride. Ref.1
Subcellular location	Serine protease espP: Periplasm By similarity. Secreted autotransporter protein espP: Secreted. Cell surface. Autotransporter protein espP translocator: Cell outer membrane; Multi-pass membrane protein By similarity. Note: The cleaved C-terminal fragment (autotransporter domain) is localized in the outer membrane By similarity.
Induction	Expression is optimal at 37 degrees Celsius, and inhibited at 20 degrees Celsius. It is dependent on both temperature and pH. Ref.1
Domain	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.
Post-translational modification	Cleaved to release the mature protein from the outer membrane.
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.
Sequence similarities	Contains 1 autotransporter (TC 1.B.12) domain. [View classification] Contains 1 peptidase S6 domain.
Caution	Strain 3010/96 exhibits a partial deletion of the gene.

Ontologies

Keywords
Biological process	Virulence
Cellular component	Cell membrane Cell outer membrane Membrane Periplasm Secreted
Domain	Signal Transmembrane Transmembrane beta strand
Molecular function	Hydrolase Protease Serine protease
PTM	Zymogen
Technical term	3D-structure Complete proteome Direct protein sequencing Plasmid
Gene Ontology (GO)
Biological process	pathogenesis Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cell outer membrane Inferred from electronic annotation. Source: UniProtKB-SubCell cell surface Inferred from electronic annotation. Source: UniProtKB-SubCell extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW periplasmic space Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 55

Ref.1

Chain

56 – 1300

1245

Serine protease espP

PRO_0000387594

Chain

56 – 1023

968

Secreted autotransporter protein espP

PRO_0000042020

Chain

1024 – 1300

277

Autotransporter protein espP translocator By similarity

PRO_0000042021

Regions

Domain

1034 – 1300

267

Autotransporter

Sites

Active site

127

Charge relay system By similarity

Active site

156

Charge relay system By similarity

Active site

263

Charge relay system By similarity

Site

1023 – 1024

Cleavage

Secondary structure

1300

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

Q7BSW5 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: E34D3F037DEC672F
Show »

FASTA

1,300

141,758

        10         20         30         40         50         60 
MNKIYSLKYS HITGGLIAVS ELSGRVSSRA TGKKKHKRIL ALCFLGLLQS SYSFASQMDI 

        70         80         90        100        110        120 
SNFYIRDYMD FAQNKGIFQA GATNIEIVKK DGSTLKLPEV PFPDFSPVAN KGSTTSIGGA 

       130        140        150        160        170        180 
YSITATHNTK NHHSVATQNW GNSTYKQTDW NTSHPDFAVS RLDKFVVETR GATEGADISL 

       190        200        210        220        230        240 
SKQQALERYG VNYKGEKKLI AFRAGSGVVS VKKNGRITPF NEVSYKPEML NGSFVHIDDW 

       250        260        270        280        290        300 
SGWLILTNNQ FDEFNNIASQ GDSGSALFVY DNQKKKWVVA GTVWGIYNYA NGKNHAAYSK 

       310        320        330        340        350        360 
WNQTTIDNLK NKYSYNVDMS GAQVATIENG KLTGTGSDTT DIKNKDLIFT GGGDILLKSS 

       370        380        390        400        410        420 
FDNGAGGLVF NDKKTYRVNG DDFTFKGAGV DTRNGSTVEW NIRYDNKDNL HKIGDGTLDV 

       430        440        450        460        470        480 
RKTQNTNLKT GEGLVILGAE KTFNNIYITS GDGTVRLNAE NALSGGEYNG IFFAKNGGTL 

       490        500        510        520        530        540 
DLNGYNQSFN KIAATDSGAV ITNTSTKKSI LSLNNTADYI YHGNINGNLD VLQHHETKKE 

       550        560        570        580        590        600 
NRRLILDGGV DTTNDISLRN TQLSMQGHAT EHAIYRDGAF SCSLPAPMRF LCGSDYVAGM 

       610        620        630        640        650        660 
QNTEADAVKQ NGNAYKTNNA VSDLSQPDWE TGTFRFGTLH LENSDFSVGR NANVIGDIQA 

       670        680        690        700        710        720 
SKSNITIGDT TAYIDLHAGK NITGDGFGFR QNIVRGNSQG ETLFTGGITA EDSTIVIKDK 

       730        740        750        760        770        780 
AKALFSNYVY LLNTKATIEN GADVTTQSGM FSTSDISISG NLSMTGNPDK DNKFEPSIYL 

       790        800        810        820        830        840 
NDASYLLTDD SARLVAKNKA SVVGDIHSTK SASIMFGHDE SDLSQLSDRT SKGLALGLLG 

       850        860        870        880        890        900 
GFDVSYRGSV NAPSASATMN NTWWQLTGDS ALKTLKSTNS MVYFTDSANN KKFHTLTVDE 

       910        920        930        940        950        960 
LATSNSAYAM RTNLSESDKL EVKKHLSGEN NILLVDFLQK PTPEKQLNIE LVSAPKDTNE 

       970        980        990       1000       1010       1020 
NVFKASKQTI GFSDVTPVIT TRETDDKITW SLTGYNTVAN KEATRNAAAL FSVDYKAFLN 

      1030       1040       1050       1060       1070       1080 
EVNNLNKRMG DLRDINGEAG AWARIMSGTG SASGGFSDNY THVQVGVDKK HELDGLDLFT 

      1090       1100       1110       1120       1130       1140 
GFTVTHTDSS ASADVFSGKT KSVGAGLYAS AMFDSGAYID LIGKYVHHDN EYTATFAGLG 

      1150       1160       1170       1180       1190       1200 
TRDYSTHSWY AGAEAGYRYH VTEDAWIEPQ AELVYGSVSG KQFAWKDQGM HLSMKDKDYN 

      1210       1220       1230       1240       1250       1260 
PLIGRTGVDV GKSFSGKDWK VTARAGLGYQ FDLLANGETV LRDASGEKRI KGEKDSRMLM 

      1270       1280       1290       1300 
SVGLNAEIRD NVRFGLEFEK SAFGKYNVDN AVNANFRYSF

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 9194704] [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: 9722640] [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: 9628576] [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: 10376815] [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: 15151995] [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: 15615856] [Abstract] Cited for: FUNCTION OF THE SIGNAL PEPTIDE. Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X97542 Genomic DNA. Translation: CAA66144.1.
AF074613 Genomic DNA. Translation: AAC70088.1.
AB011549 Genomic DNA. Translation: BAA31836.1.
AJ010390 Genomic DNA. Translation: CAB42538.1.

PIR

T00317.

RefSeq

NP_052685.1. NC_002128.1.
YP_002756610.1. NC_012487.1.
YP_325580.1. NC_007414.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2QOM	X-ray	2.66	A/B	1024-1300	[»]
3SLJ	X-ray	2.48	A	999-1300	[»]
3SLO	X-ray	2.52	A	999-1300	[»]
3SLT	X-ray	2.46	A	999-1300	[»]
3SZE	X-ray	2.50	A	56-1023	[»]

ProteinModelPortal

Q7BSW5.

SMR

Q7BSW5. Positions 538-668, 842-999, 1024-1300.

ModBase

Search...

Protein family/group databases

MEROPS

S06.002.

TCDB

1.B.12.4.3. autotransporter-1 (AT-1) family.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000029401; EBESCP00000028106; EBESCG00000028451.
EBESCT00000060680; EBESCP00000058324; EBESCG00000059727.

GeneID

1789732.
3683719.
7701441.

GenomeReviews

Gene locus ECO57PM78 in contig AB011549_GR.
Gene locus L7020 in contig AF074613_GR.

KEGG

ece:L7020.

PATRIC

18360417. VBIEscCol44059_5610.

Organism-specific databases

CMR

Search...

Phylogenomic databases

GeneTree

EBGT00050000008323.

HOGENOM

HBG467630.

OMA

AWARIIS.

ProtClustDB

CLSK2517096.

Family and domain databases

InterPro

IPR005546. Auto_transptbeta.
IPR006315. OM_autotransptr_brl.
IPR012332. P22_tailspike_C-like.
IPR011050. Pectin_lyase_fold/virulence.
IPR000710. Peptidase_S6.
[Graphical view]

Gene3D

G3DSA:2.160.20.20. P22_tailspike. 1 hit.

K12684.

Pfam

PF03797. Autotransporter. 1 hit.
PF02395. Peptidase_S6. 1 hit.
[Graphical view]

PRINTS

PR00921. IGASERPTASE.

SMART

SM00869. Autotransporter. 1 hit.
[Graphical view]

SUPFAM

SSF103515. Auto_transptbeta. 1 hit.
SSF51126. Pectin_lyas_like. 1 hit.

TIGRFAMs

TIGR01414. Autotrans_barl. 1 hit.

PROSITE

PS51208. AUTOTRANSPORTER. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

ESPP_ECO57

Accession

Primary (citable) accession number: Q7BSW5
Secondary accession number(s): O32555, Q9S6R3

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 27, 2005
Last sequence update:	July 5, 2004
Last modified:	January 25, 2012
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Cleaved into the following 2 chains:

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents