ESPP_ECOLX
ID ESPP_ECOLX Reviewed; 1300 AA.
AC O32591;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Serine protease EspP;
DE EC=3.4.21.-;
DE Contains:
DE RecName: Full=Secreted autotransporter protein EspP;
DE AltName: Full=Extracellular serine protease plasmid-encoded EspP;
DE Contains:
DE RecName: Full=Autotransporter protein EspP translocator;
DE Flags: Precursor;
GN Name=espP; Synonyms=pssA;
OS Escherichia coli.
OG Plasmid unnamed.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 56-85, AND FUNCTION.
RC STRAIN=O26:H- / 413/89-1 / EHEC; PLASMID=unnamed;
RX PubMed=9379905; DOI=10.1046/j.1365-2958.1997.5141874.x;
RA Djafari S., Ebel F., Deibel C., Kraemer S., Hudel M., Chakraborty T.;
RT "Characterization of an exported protease from Shiga toxin-producing
RT Escherichia coli.";
RL Mol. Microbiol. 25:771-784(1997).
CC -!- FUNCTION: Serine protease with cytotoxic effect. Disrupts actin
CC cytoskeleton resulting cell detachment in vitro.
CC {ECO:0000269|PubMed:9379905}.
CC -!- INTERACTION:
CC O32591; P0A6A8: acpP; Xeno; NbExp=2; IntAct=EBI-852989, EBI-542566;
CC O32591; P0A8Z3: ybgC; Xeno; NbExp=2; IntAct=EBI-852989, EBI-543276;
CC -!- SUBCELLULAR LOCATION: [Serine protease EspP]: Periplasm {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Secreted autotransporter protein EspP]:
CC Secreted. Cell surface.
CC -!- SUBCELLULAR LOCATION: [Autotransporter protein EspP translocator]: Cell
CC outer membrane {ECO:0000250}; Multi-pass membrane protein
CC {ECO:0000250}. Note=The cleaved C-terminal fragment (autotransporter
CC domain) is localized in the outer membrane. {ECO:0000250}.
CC -!- DOMAIN: The signal peptide, cleaved at the inner membrane, guides the
CC autotransporter protein to the periplasmic space. Then, insertion of
CC the C-terminal translocator domain in the outer membrane forms a
CC hydrophilic pore for the translocation of the passenger domain to the
CC bacterial cell surface, with subsequent cleavage (By similarity).
CC {ECO:0000250}.
CC -!- PTM: Cleaved to release the mature protein from the outer membrane.
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: Encoded on an unnamed 94 kb plasmid.
CC {ECO:0000305|PubMed:9379905}.
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DR EMBL; Y13614; CAA73935.1; -; Genomic_DNA.
DR AlphaFoldDB; O32591; -.
DR SMR; O32591; -.
DR IntAct; O32591; 3.
DR MEROPS; N04.002; -.
DR MEROPS; S06.002; -.
DR PRIDE; O32591; -.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.160.20.20; -; 1.
DR Gene3D; 2.40.128.130; -; 1.
DR InterPro; IPR005546; Autotransporte_beta.
DR InterPro; IPR036709; Autotransporte_beta_dom_sf.
DR InterPro; IPR012332; Autotransporter_pectin_lyase_C.
DR InterPro; IPR024973; ESPR.
DR InterPro; IPR006315; OM_autotransptr_brl.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR000710; Peptidase_S6.
DR InterPro; IPR030396; Peptidase_S6_dom.
DR Pfam; PF03797; Autotransporter; 1.
DR Pfam; PF13018; ESPR; 1.
DR Pfam; PF02395; Peptidase_S6; 1.
DR PRINTS; PR00921; IGASERPTASE.
DR SMART; SM00869; Autotransporter; 1.
DR SUPFAM; SSF103515; SSF103515; 1.
DR SUPFAM; SSF51126; SSF51126; 1.
DR TIGRFAMs; TIGR01414; autotrans_barl; 1.
DR PROSITE; PS51208; AUTOTRANSPORTER; 1.
DR PROSITE; PS51691; PEPTIDASE_S6; 1.
PE 1: Evidence at protein level;
KW Cell outer membrane; Direct protein sequencing; Hydrolase; Membrane;
KW Periplasm; Plasmid; Protease; Secreted; Serine protease; Signal;
KW Transmembrane; Transmembrane beta strand; Virulence; Zymogen.
FT SIGNAL 1..55
FT /evidence="ECO:0000269|PubMed:9379905"
FT CHAIN 56..1300
FT /note="Serine protease EspP"
FT /id="PRO_0000387593"
FT CHAIN 56..1023
FT /note="Secreted autotransporter protein EspP"
FT /id="PRO_0000042018"
FT CHAIN 1024..1300
FT /note="Autotransporter protein EspP translocator"
FT /evidence="ECO:0000250"
FT /id="PRO_0000042019"
FT DOMAIN 57..311
FT /note="Peptidase S6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01028"
FT DOMAIN 1034..1300
FT /note="Autotransporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00556"
FT ACT_SITE 127
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01028"
FT ACT_SITE 156
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01028"
FT ACT_SITE 263
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01028"
FT SITE 1023..1024
FT /note="Cleavage"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1300 AA; 141710 MW; F84D24086DE77C24 CRC64;
MNKIYSLKYS HITGGLIAVS ELSGRVSSRA TGKKKHKRIL ALCFLGLLQS SYSFASQMDI
SNFYIRDYMD FAQNKGIFQA GATNIEIVKK DGSTLKLPEV PFPDFSPVAN KGSTTSIGGA
YSITATHNTK NHHSVATQNW GNSTYKQTDW NTSHPDFAVS RLDKFVVETR GATEGADISL
SKQQALERYG VNYKGEKKLI AFRAGSGVVS VKKNGRITPF NEVSYKPEML NGSFVHIDDW
SGWLILTNNQ FDEFNNIASQ GDSGSALFVY DNQKKKWVVA GTVWGIYNYA NGKNHAAYSK
WNQTTIDNLK NKYSYNVDMS GAQVATIENG KLTGTGSDTT DIKNKDLIFT GGGDILLKSS
FDNGAGGLVF NDKKTYRVNG DDFTFKGAGV DTRNGSTVEW NIRYDNKDNL HKIGDGTLDV
RKTQNTNLKT GEGLVILGAE KTFNNIYITS GDGTVRLNAE NALSGGEYNG IFFAKNGGTL
DLNGYNQSFN KIAATDSGAV ITNTSTKKSI LSLNNTADYI YHGNINGNLD VLQHHETKKE
NRRLILDGGV DTTNDISLRN TQLSMQGHAT EHAIYRDGAF SCSLPAPMRF LCGSDYVAGM
QNTEADAVKQ NGNAYKTNNA VSDLSQPDWE TGTFRFGTLH LENSDFSVGR NANVIGDIQA
SKSNITIGDT TAYIDLHAGK NITGDGFGFR QNIVRGNSQG ETLFTGGITA EDSTIVIKDK
AKALFSNYVY LLNTKATIEN GADVTTQSGM FSTSDISISG NLSMTGNPDK DNKFEPSIYL
NDASYLLTDD SARLVAKNKA SVVGDIHSTK SASIMFGHDE SDLSQLSDRT SKGLALGLLG
GFDVSYRGSV NAPSASATMN NTWWQLTGDS ALKTLKSTNS MVYFTDSANN KKFHTLTVDE
LATSNSAYAM RTNLSESDKL EVKKHLSGEN NILLVDFLQK PTPEKQLNIE LVSAPKDTNE
NVFKASKQTI GFSDVTPVIT TRETDDKITW SLTGYNTVAN KEATRNAAAL FSVDYKAFLN
EVNNLNKRMG DLRDINGEAG AWARIMSGTG SASGGFSDNY THVQVGVDKK HELDGLDLFT
GFTVTHTDSS ASADVFSGKT KSVGAGLYAS AMVDSGAYID LIGKYVHHDN EYTATFAGLG
TRDYSTHSWY AGAEAGYRYH VTEDAWIEPQ AELVYGSVSG KQFAWKDQGM HLSMKDKDYN
PLIGRTGVDV GKSFSGKDWK VTARAGLGYQ FDLLANGETV LRDASGEKRI KGEKDSRMLM
SVGLNAEIRD NVRFGLEFEK SAFGKYNVDN AVNANFRYSF
