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1.B.12.4.3 Autotransporter of serine protease, EspP (with long N-terminal leader that prevents improper folding in the periplasm) (Szabady et al., 2005; Ieva et al., 2008). Energy for export is provided by the folding of the C-terminal domain (Peterson et al., 2010).
Accession Number:	Q7BSW5
Protein Name:	Putative exoprotein-precursor (Serine protease EspP)
Length:	1300
Molecular Weight:	141758.00
Species:	Escherichia coli O157:H7 [83334]
Number of TMSs:	1
Location¹ / Topology² / Orientation³:	Cell outer membrane¹ / Multi-pass membrane protein²
Substrate

Structure:
RefSeq:	NP_052685.1 YP_002756610.1 YP_325580.1
Entrez Gene ID:	1789732 3683719 7701441
Pfam:	PF03797 PF02395
KEGG:	ece:L7020
Gene Ontology GO:0009279 C:cell outer membrane GO:0009986 C:cell surface GO:0005576 C:extracellular region GO:0016021 C:integral to membrane GO:0042597 C:periplasmic space GO:0005886 C:plasma membrane GO:0004252 F:serine-type endopeptidase activity GO:0009405 P:pathogenesis GO:0006508 P:proteolysis
References (6) [1] “EspP, a novel extracellular serine protease of enterohaemorrhagic Escherichia coli O157:H7 cleaves human coagulation factor V.” Brunder W.et.al. 9194704 [2] “The complete DNA sequence and analysis of the large virulence plasmid of Escherichia coli O157:H7.” Burland V.et.al. 9722640 [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.et.al. 9628576 [4] “The large plasmids of Shiga-toxin-producing Escherichia coli (STEC) are highly variable genetic elements.” Brunder W.et.al. 10376815 [5] “Hydrophobic residues of the autotransporter EspP linker domain are important for outer membrane translocation of its passenger.” Velarde J.J.et.al. 15151995 [6] “An unusual signal peptide facilitates late steps in the biogenesis of a bacterial autotransporter.” Szabady R.L.et.al. 15615856
2QOM 3SLJ 3SLO 3SLT 3SZE

UniProt (Universal Protein Resource)
CDD Search (Conserved Domain Database)

Predict TMSs (Predict number of transmembrane segments)

FASTA formatted sequence

1:	MNKIYSLKYS HITGGLIAVS ELSGRVSSRA TGKKKHKRIL ALCFLGLLQS SYSFASQMDI 
61:	SNFYIRDYMD FAQNKGIFQA GATNIEIVKK DGSTLKLPEV PFPDFSPVAN KGSTTSIGGA 
121:	YSITATHNTK NHHSVATQNW GNSTYKQTDW NTSHPDFAVS RLDKFVVETR GATEGADISL 
181:	SKQQALERYG VNYKGEKKLI AFRAGSGVVS VKKNGRITPF NEVSYKPEML NGSFVHIDDW 
241:	SGWLILTNNQ FDEFNNIASQ GDSGSALFVY DNQKKKWVVA GTVWGIYNYA NGKNHAAYSK 
301:	WNQTTIDNLK NKYSYNVDMS GAQVATIENG KLTGTGSDTT DIKNKDLIFT GGGDILLKSS 
361:	FDNGAGGLVF NDKKTYRVNG DDFTFKGAGV DTRNGSTVEW NIRYDNKDNL HKIGDGTLDV 
421:	RKTQNTNLKT GEGLVILGAE KTFNNIYITS GDGTVRLNAE NALSGGEYNG IFFAKNGGTL 
481:	DLNGYNQSFN KIAATDSGAV ITNTSTKKSI LSLNNTADYI YHGNINGNLD VLQHHETKKE 
541:	NRRLILDGGV DTTNDISLRN TQLSMQGHAT EHAIYRDGAF SCSLPAPMRF LCGSDYVAGM 
601:	QNTEADAVKQ NGNAYKTNNA VSDLSQPDWE TGTFRFGTLH LENSDFSVGR NANVIGDIQA 
661:	SKSNITIGDT TAYIDLHAGK NITGDGFGFR QNIVRGNSQG ETLFTGGITA EDSTIVIKDK 
721:	AKALFSNYVY LLNTKATIEN GADVTTQSGM FSTSDISISG NLSMTGNPDK DNKFEPSIYL 
781:	NDASYLLTDD SARLVAKNKA SVVGDIHSTK SASIMFGHDE SDLSQLSDRT SKGLALGLLG 
841:	GFDVSYRGSV NAPSASATMN NTWWQLTGDS ALKTLKSTNS MVYFTDSANN KKFHTLTVDE 
901:	LATSNSAYAM RTNLSESDKL EVKKHLSGEN NILLVDFLQK PTPEKQLNIE LVSAPKDTNE 
961:	NVFKASKQTI GFSDVTPVIT TRETDDKITW SLTGYNTVAN KEATRNAAAL FSVDYKAFLN 
1021:	EVNNLNKRMG DLRDINGEAG AWARIMSGTG SASGGFSDNY THVQVGVDKK HELDGLDLFT 
1081:	GFTVTHTDSS ASADVFSGKT KSVGAGLYAS AMFDSGAYID LIGKYVHHDN EYTATFAGLG 
1141:	TRDYSTHSWY AGAEAGYRYH VTEDAWIEPQ AELVYGSVSG KQFAWKDQGM HLSMKDKDYN 
1201:	PLIGRTGVDV GKSFSGKDWK VTARAGLGYQ FDLLANGETV LRDASGEKRI KGEKDSRMLM 
1261:	SVGLNAEIRD NVRFGLEFEK SAFGKYNVDN AVNANFRYSF

1.B.12.4.3
Autotransporter of serine protease, EspP (with long N-terminal leader that prevents improper folding in the periplasm) (Szabady et al., 2005; Ieva et al., 2008). Energy for export is provided by the folding of the C-terminal domain (Peterson et al., 2010).

Cross database links:

Gene Ontology

References (6)

External Searches:

Analyze:

1.B.12.4.3Autotransporter of serine protease, EspP (with long N-terminal leader that prevents improper folding in the periplasm) (Szabady et al., 2005; Ieva et al., 2008). Energy for export is provided by the folding of the C-terminal domain (Peterson et al., 2010).

Cross database links:

Gene Ontology

References (6)

External Searches:

Analyze:

1.B.12.4.3
Autotransporter of serine protease, EspP (with long N-terminal leader that prevents improper folding in the periplasm) (Szabady et al., 2005; Ieva et al., 2008). Energy for export is provided by the folding of the C-terminal domain (Peterson et al., 2010).