| Tag | Content |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Serine protease EspP |
Protein Synonyms/Alias | |
Gene Name | espP |
Gene Synonyms/Alias | L7020, ECO57PM78 |
Created Date | 3-June-2014 |
Organism | Escherichia coli O157:H7 |
NCBI Taxa ID | 83334 |
Phosphorylation | Position | Peptide | Code | Type | References | | 189 | KQQALERYGVNYKGE | Y | HTP | [1] | |
Reference | [1]The Escherichia coli phosphotyrosine proteome relates to core pathways and virulence. Hansen AM,Chaerkady R,Sharma J,Díaz-Mejía JJ,Tyagi N,Renuse S,Jacob HK,Pinto SM,Sahasrabuddhe NA,Kim MS,Delanghe B,Srinivasan N,Emili A,Kaper JB,Pandey A PLoS Pathog. 2013;9(6):e1003403. [ PMID:23785281] |
Functional Description From UniProt | FUNCTION: Serine protease capable of cleaving pepsin A and human coagulation factor V, which may contribute to the mucosal hemorrhage observed in hemorrhagic colitis |
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| 3D-structure; Celloutermembrane; Completeproteome; Directproteinsequencing; Hydrolase; Membrane; Periplasm; Plasmid; Protease; Secreted; Serineprotease; Signal; Transmembrane; Transmembranebetastrand; Virulence; Zymogen |
Protein Sequence | MNKIYSLKYS HITGGLIAVS ELSGRVSSRA TGKKKHKRIL ALCFLGLLQS SYSFASQMDI 60
SNFYIRDYMD FAQNKGIFQA GATNIEIVKK DGSTLKLPEV PFPDFSPVAN KGSTTSIGGA 120
YSITATHNTK NHHSVATQNW GNSTYKQTDW NTSHPDFAVS RLDKFVVETR GATEGADISL 180
SKQQALERYG VNYKGEKKLI AFRAGSGVVS VKKNGRITPF NEVSYKPEML NGSFVHIDDW 240
SGWLILTNNQ FDEFNNIASQ GDSGSALFVY DNQKKKWVVA GTVWGIYNYA NGKNHAAYSK 300
WNQTTIDNLK NKYSYNVDMS GAQVATIENG KLTGTGSDTT DIKNKDLIFT GGGDILLKSS 360
FDNGAGGLVF NDKKTYRVNG DDFTFKGAGV DTRNGSTVEW NIRYDNKDNL HKIGDGTLDV 420
RKTQNTNLKT GEGLVILGAE KTFNNIYITS GDGTVRLNAE NALSGGEYNG IFFAKNGGTL 480
DLNGYNQSFN KIAATDSGAV ITNTSTKKSI LSLNNTADYI YHGNINGNLD VLQHHETKKE 540
NRRLILDGGV DTTNDISLRN TQLSMQGHAT EHAIYRDGAF SCSLPAPMRF LCGSDYVAGM 600
QNTEADAVKQ NGNAYKTNNA VSDLSQPDWE TGTFRFGTLH LENSDFSVGR NANVIGDIQA 660
SKSNITIGDT TAYIDLHAGK NITGDGFGFR QNIVRGNSQG ETLFTGGITA EDSTIVIKDK 720
AKALFSNYVY LLNTKATIEN GADVTTQSGM FSTSDISISG NLSMTGNPDK DNKFEPSIYL 780
NDASYLLTDD SARLVAKNKA SVVGDIHSTK SASIMFGHDE SDLSQLSDRT SKGLALGLLG 840
GFDVSYRGSV NAPSASATMN NTWWQLTGDS ALKTLKSTNS MVYFTDSANN KKFHTLTVDE 900
LATSNSAYAM RTNLSESDKL EVKKHLSGEN NILLVDFLQK PTPEKQLNIE LVSAPKDTNE 960
NVFKASKQTI GFSDVTPVIT TRETDDKITW SLTGYNTVAN KEATRNAAAL FSVDYKAFLN 1020
EVNNLNKRMG DLRDINGEAG AWARIMSGTG SASGGFSDNY THVQVGVDKK HELDGLDLFT 1080
GFTVTHTDSS ASADVFSGKT KSVGAGLYAS AMFDSGAYID LIGKYVHHDN EYTATFAGLG 1140
TRDYSTHSWY AGAEAGYRYH VTEDAWIEPQ AELVYGSVSG KQFAWKDQGM HLSMKDKDYN 1200
PLIGRTGVDV GKSFSGKDWK VTARAGLGYQ FDLLANGETV LRDASGEKRI KGEKDSRMLM 1260
SVGLNAEIRD NVRFGLEFEK SAFGKYNVDN AVNANFRYSF 1300 |
| GO:0009279 C:cell outer membrane IEA:UniProtKB-SubCell GO:0009986 C:cell surface IEA:UniProtKB-SubCell GO:0005576 C:extracellular region IEA:UniProtKB-SubCell GO:0016021 C:integral component of membrane IEA:UniProtKB-KW GO:0042597 C:periplasmic space IEA:UniProtKB-SubCell GO:0004252 F:serine-type endopeptidase activity IEA:InterPro GO:0009405 P:pathogenesis IEA:UniProtKB-KW |
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