UniProtKB - Q9EZE7 (ESPC_ECO27)
Protein
Serine protease EspC
Gene
espC
Organism
Escherichia coli O127:H6 (strain E2348/69 / EPEC)
Status
Functioni
Serine protease with enterotoxic and cytotoxic activities. Cleaves fodrin, but does not cause its redistribution within epithelial cells. The exact role of EspC in EPEC pathogenesis is still unknown.1 Publication
Activity regulationi
Inhibition of cytotoxic activity by phenylmethylsulfonyl fluoride.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 125 | Charge relay systemPROSITE-ProRule annotation | 1 | |
Active sitei | 153 | Charge relay systemPROSITE-ProRule annotation | 1 | |
Active sitei | 256 | Charge relay systemPROSITE-ProRule annotation | 1 |
GO - Molecular functioni
- serine-type endopeptidase activity Source: InterPro
GO - Biological processi
- pathogenesis Source: UniProtKB-KW
Keywordsi
Molecular function | Hydrolase, Protease, Serine protease |
Biological process | Virulence |
Protein family/group databases
MEROPSi | S06.010 |
TCDBi | 1.B.12.4.1, the autotransporter-1 (at-1) family |
Names & Taxonomyi
Protein namesi | Recommended name: Serine protease EspC (EC:3.4.21.-)Cleaved into the following 2 chains: Alternative name(s): EPEC-secreted protein C |
Gene namesi | Name:espC Ordered Locus Names:E2348C_2915 |
Organismi | Escherichia coli O127:H6 (strain E2348/69 / EPEC) |
Taxonomic identifieri | 574521 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Subcellular locationi
Other locations
- Periplasm By similarity
Extracellular region or secreted
Other locations
Other locations
- Cell outer membrane By similarity; Multi-pass membrane protein By similarity
Note: The cleaved C-terminal fragment (autotransporter domain) is localized in the outer membrane.By similarity
Extracellular region or secreted
- extracellular region Source: UniProtKB-SubCell
Other locations
- cell outer membrane Source: UniProtKB-SubCell
- cell surface Source: UniProtKB-SubCell
- integral component of membrane Source: UniProtKB-KW
- periplasmic space Source: UniProtKB-SubCell
Keywords - Cellular componenti
Cell outer membrane, Membrane, Periplasm, SecretedPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 256 | S → I: Abolishes protease and cytotoxic activities. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 53 | 1 PublicationAdd BLAST | 53 | |
ChainiPRO_0000041758 | 54 – 1305 | Serine protease EspCAdd BLAST | 1252 | |
ChainiPRO_0000387592 | 54 – 1018 | Secreted autotransporter protein EspCAdd BLAST | 965 | |
ChainiPRO_0000041759 | 1019 – 1305 | Autotransporter protein EspC translocatorBy similarityAdd BLAST | 287 |
Post-translational modificationi
Cleaved to release the mature protein from the outer membrane.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 1018 – 1019 | CleavageBy similarity | 2 |
Keywords - PTMi
ZymogenProteomic databases
PRIDEi | Q9EZE7 |
Expressioni
Inductioni
Expression is repressed by glucose.
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 55 – 297 | Peptidase S6PROSITE-ProRule annotationAdd BLAST | 243 | |
Domaini | 1039 – 1305 | AutotransporterPROSITE-ProRule annotationAdd BLAST | 267 |
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 (Probable).Curated
Keywords - Domaini
Signal, Transmembrane, Transmembrane beta strandPhylogenomic databases
HOGENOMi | CLU_000723_0_0_6 |
OMAi | IIGFRVG |
Family and domain databases
Gene3Di | 2.160.20.20, 1 hit 2.40.128.130, 1 hit |
InterProi | View protein in InterPro IPR005546, Autotransporte_beta IPR036709, Autotransporte_beta_dom_sf IPR024973, ESPR IPR006315, OM_autotransptr_brl IPR012332, P22_tailspike-like_C_sf IPR011050, Pectin_lyase_fold/virulence IPR000710, Peptidase_S6 IPR030396, Peptidase_S6_dom |
Pfami | View protein in Pfam PF03797, Autotransporter, 1 hit PF13018, ESPR, 1 hit PF02395, Peptidase_S6, 1 hit |
PRINTSi | PR00921, IGASERPTASE |
SMARTi | View protein in SMART SM00869, Autotransporter, 1 hit |
SUPFAMi | SSF103515, SSF103515, 1 hit SSF51126, SSF51126, 2 hits |
TIGRFAMsi | TIGR01414, autotrans_barl, 1 hit |
PROSITEi | View protein in PROSITE PS51208, AUTOTRANSPORTER, 1 hit PS51691, PEPTIDASE_S6, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
Q9EZE7-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MNKIYALKYC HATGGLIAVS ELASRVMKKA ARGSLLALFN LSLYGAFLSA
60 70 80 90 100
SQAAQLNIDN VWARDYLDLA QNKGVFKAGA TNVSIQLKNG QTFNFPNVPI
110 120 130 140 150
PDFSPASNKG ATTSIGGAYS VTATHNGTTH HAISTQNWGQ SSYKYIDRMT
160 170 180 190 200
NGDFAVTRLD KFVVETTGVK NSVDFSLNSH DALERYGVEI NGEKKIIGFR
210 220 230 240 250
VGAGTTYTVQ NGNTYSTGQV YNPLLLSASM FQLNWDNKRP YNNTTPFYNE
260 270 280 290 300
TTGGDSGSGF YLYDNVKKEW VMLGTLFGIA SSGADVWSIL NQYDENTVNG
310 320 330 340 350
LKNKFTQKVQ LNNNTMSLNS DSFTLAGNNT AVEKNNNNYK DLSFSGGGSI
360 370 380 390 400
NFDNDVNIGS GGLIFDAGHH YTVTGNNKTF KGAGLDIGDN TTVDWNVKGV
410 420 430 440 450
VGDNLHKIGA GTLNVNVSQG NNLKTGDGLV VLNSANAFDN IYMASGHGVV
460 470 480 490 500
KINHSAALNQ NNDYRGIFFT ENGGTLDLNG YDQSFNKIAA TDIGALITNS
510 520 530 540 550
AVQKAVLSVN NQSNYMYHGS VSGNTEINHQ FDTQKNNSRL ILDGNVDITN
560 570 580 590 600
DINIKNSQLT MQGHATSHAV FREGGVTCML PGVICEKDYV SGIQQQENSA
610 620 630 640 650
NKNNNTDYKT NNQVSSFEQP DWENRLFKFK TLNLINSDFI VGRNAIVVGD
660 670 680 690 700
ISANNSTLSL SGKDTKVHID MYDGKNITGD GFGFRQDIKD GVSVSPESSS
710 720 730 740 750
YFGNVTLNNH SLLDIGNKFT GGIEAYDSSV SVTSQNAVFD RVGSFVNSSL
760 770 780 790 800
TLEKGAKLTA QGGIFSTGAV DVKENASLIL TGTPSAQKQE YYSPVISTTE
810 820 830 840 850
GINLGDKASL SVKNMGYLSS DIHAGTTAAT INLGDGDAET DSPLFSSLMK
860 870 880 890 900
GYNAVLSGNI TGEQSTVNMN NALWYSDGNS TIGTLKSTGG RVELGGGKDF
910 920 930 940 950
ATLRVKELNA NNATFLMHTN NSQADQLNVT NKLLGSNNTV LVDFLNKPAS
960 970 980 990 1000
EMNVTLITAP KGSDEKTFTA GTQQIGFSNV TPVISTEKTD DATKWMLTGY
1010 1020 1030 1040 1050
QTVSDAGASK TATDFMASGY KSFLTEVNNL NKRMGDLRDT QGDAGVWARI
1060 1070 1080 1090 1100
MNGTGSADGG YSDNYTHVQI GADRKHELDG VDLFTGALLT YTDSNASSHA
1110 1120 1130 1140 1150
FSGKTKSVGG GLYASALFDS GAYFDLIGKY LHHDNQYTAS FASLGTKDYS
1160 1170 1180 1190 1200
SHSWYAGAEV GYRYHLSEES WVEPQMELVY GSVSGKSFSW EDRGMALSMK
1210 1220 1230 1240 1250
DKDYNPLIGR TGVDVGRTFS GDDWKITARA GLGYQFDLLA NGETVLRDAS
1260 1270 1280 1290 1300
GEKRFEGEKD SRMLMNVGMN AEIKDNMRFG LELEKSAFGK YNVDNAINAN
FRYSF
Sequence cautioni
The sequence AAC44731 differs from that shown. Reason: Frameshift.Curated
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 55 | Q → G AA sequence (PubMed:7644526).Curated | 1 | |
Sequence conflicti | 209 | V → A in AAC44731 (PubMed:8932311).Curated | 1 | |
Sequence conflicti | 287 | W → G in AAC44731 (PubMed:8932311).Curated | 1 | |
Sequence conflicti | 333 | E → A in AAC44731 (PubMed:8932311).Curated | 1 | |
Sequence conflicti | 514 | N → H in AAC44731 (PubMed:8932311).Curated | 1 | |
Sequence conflicti | 849 – 850 | MK → IR in AAC44731 (PubMed:8932311).Curated | 2 | |
Sequence conflicti | 921 | N → T in AAC44731 (PubMed:8932311).Curated | 1 | |
Sequence conflicti | 1189 | S → I in AAC44731 (PubMed:8932311).Curated | 1 | |
Sequence conflicti | 1300 | N → D in AAG37043 (PubMed:11119520).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U69128 Genomic DNA Translation: AAC44731.1 Frameshift. AF297061 Genomic DNA Translation: AAG37043.1 FM180568 Genomic DNA Translation: CAS10463.1 |
RefSeqi | WP_001034000.1, NC_011601.1 |
Genome annotation databases
EnsemblBacteriai | CAS10463; CAS10463; E2348C_2915 |
KEGGi | ecg:E2348C_2915 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U69128 Genomic DNA Translation: AAC44731.1 Frameshift. AF297061 Genomic DNA Translation: AAG37043.1 FM180568 Genomic DNA Translation: CAS10463.1 |
RefSeqi | WP_001034000.1, NC_011601.1 |
3D structure databases
SMRi | Q9EZE7 |
ModBasei | Search... |
Protein family/group databases
MEROPSi | S06.010 |
TCDBi | 1.B.12.4.1, the autotransporter-1 (at-1) family |
Proteomic databases
PRIDEi | Q9EZE7 |
Genome annotation databases
EnsemblBacteriai | CAS10463; CAS10463; E2348C_2915 |
KEGGi | ecg:E2348C_2915 |
Phylogenomic databases
HOGENOMi | CLU_000723_0_0_6 |
OMAi | IIGFRVG |
Family and domain databases
Gene3Di | 2.160.20.20, 1 hit 2.40.128.130, 1 hit |
InterProi | View protein in InterPro IPR005546, Autotransporte_beta IPR036709, Autotransporte_beta_dom_sf IPR024973, ESPR IPR006315, OM_autotransptr_brl IPR012332, P22_tailspike-like_C_sf IPR011050, Pectin_lyase_fold/virulence IPR000710, Peptidase_S6 IPR030396, Peptidase_S6_dom |
Pfami | View protein in Pfam PF03797, Autotransporter, 1 hit PF13018, ESPR, 1 hit PF02395, Peptidase_S6, 1 hit |
PRINTSi | PR00921, IGASERPTASE |
SMARTi | View protein in SMART SM00869, Autotransporter, 1 hit |
SUPFAMi | SSF103515, SSF103515, 1 hit SSF51126, SSF51126, 2 hits |
TIGRFAMsi | TIGR01414, autotrans_barl, 1 hit |
PROSITEi | View protein in PROSITE PS51208, AUTOTRANSPORTER, 1 hit PS51691, PEPTIDASE_S6, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | ESPC_ECO27 | |
Accessioni | Q9EZE7Primary (citable) accession number: Q9EZE7 Secondary accession number(s): B7UH71, P77070 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | September 13, 2005 |
Last sequence update: | May 5, 2009 | |
Last modified: | December 2, 2020 | |
This is version 110 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |