ESPC_ECO27
ID ESPC_ECO27 Reviewed; 1305 AA.
AC Q9EZE7; B7UH71; P77070;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Serine protease EspC;
DE EC=3.4.21.-;
DE Contains:
DE RecName: Full=Secreted autotransporter protein EspC;
DE AltName: Full=EPEC-secreted protein C;
DE Contains:
DE RecName: Full=Autotransporter protein EspC translocator;
DE Flags: Precursor;
GN Name=espC; OrderedLocusNames=E2348C_2915;
OS Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=574521;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBCELLULAR LOCATION.
RX PubMed=8932311; DOI=10.1128/jb.178.22.6546-6554.1996;
RA Stein M., Kenny B., Stein M.A., Finlay B.B.;
RT "Characterization of EspC, a 110-kilodalton protein secreted by
RT enteropathogenic Escherichia coli which is homologous to members of the
RT immunoglobulin A protease-like family of secreted proteins.";
RL J. Bacteriol. 178:6546-6554(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11119520; DOI=10.1128/iai.69.1.315-324.2001;
RA Mellies J.L., Navarro-Garcia F., Okeke I., Frederickson J., Nataro J.P.,
RA Kaper J.B.;
RT "EspC pathogenicity island of enteropathogenic Escherichia coli encodes an
RT enterotoxin.";
RL Infect. Immun. 69:315-324(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E2348/69 / EPEC;
RX PubMed=18952797; DOI=10.1128/jb.01238-08;
RA Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T., Henderson I.R.,
RA Harris D., Asadulghani M., Kurokawa K., Dean P., Kenny B., Quail M.A.,
RA Thurston S., Dougan G., Hayashi T., Parkhill J., Frankel G.;
RT "Complete genome sequence and comparative genome analysis of
RT enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL J. Bacteriol. 191:347-354(2009).
RN [4]
RP PROTEIN SEQUENCE OF 54-74.
RX PubMed=7644526; DOI=10.1073/pnas.92.17.7991;
RA Kenny B., Finlay B.B.;
RT "Protein secretion by enteropathogenic Escherichia coli is essential for
RT transducing signals to epithelial cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:7991-7995(1995).
RN [5]
RP FUNCTION, AND MUTAGENESIS OF SER-256.
RX PubMed=15155671; DOI=10.1128/iai.72.6.3609-3621.2004;
RA Navarro-Garcia F., Canizalez-Roman A., Sui B.Q., Nataro J.P., Azamar Y.;
RT "The serine protease motif of EspC from enteropathogenic Escherichia coli
RT produces epithelial damage by a mechanism different from that of Pet toxin
RT from enteroaggregative E. coli.";
RL Infect. Immun. 72:3609-3621(2004).
CC -!- FUNCTION: Serine protease with enterotoxic and cytotoxic activities.
CC Cleaves fodrin, but does not cause its redistribution within epithelial
CC cells. The exact role of EspC in EPEC pathogenesis is still unknown.
CC {ECO:0000269|PubMed:15155671}.
CC -!- ACTIVITY REGULATION: Inhibition of cytotoxic activity by
CC phenylmethylsulfonyl fluoride.
CC -!- SUBCELLULAR LOCATION: [Serine protease EspC]: Periplasm {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Secreted autotransporter protein EspC]:
CC Secreted. Cell surface.
CC -!- SUBCELLULAR LOCATION: [Autotransporter protein EspC 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 -!- INDUCTION: Expression is repressed by glucose.
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 (Probable).
CC {ECO:0000305}.
CC -!- PTM: Cleaved to release the mature protein from the outer membrane.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC44731.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U69128; AAC44731.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AF297061; AAG37043.1; -; Genomic_DNA.
DR EMBL; FM180568; CAS10463.1; -; Genomic_DNA.
DR RefSeq; WP_001034000.1; NC_011601.1.
DR AlphaFoldDB; Q9EZE7; -.
DR SMR; Q9EZE7; -.
DR MEROPS; N04.002; -.
DR MEROPS; S06.010; -.
DR TCDB; 1.B.12.4.1; the autotransporter-1 (at-1) family.
DR PRIDE; Q9EZE7; -.
DR EnsemblBacteria; CAS10463; CAS10463; E2348C_2915.
DR KEGG; ecg:E2348C_2915; -.
DR HOGENOM; CLU_000723_0_0_6; -.
DR OMA; IIGFRVG; -.
DR Proteomes; UP000008205; Chromosome.
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; 2.
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; Protease; Secreted; Serine protease; Signal; Transmembrane;
KW Transmembrane beta strand; Virulence; Zymogen.
FT SIGNAL 1..53
FT /evidence="ECO:0000269|PubMed:7644526"
FT CHAIN 54..1305
FT /note="Serine protease EspC"
FT /id="PRO_0000041758"
FT CHAIN 54..1018
FT /note="Secreted autotransporter protein EspC"
FT /id="PRO_0000387592"
FT CHAIN 1019..1305
FT /note="Autotransporter protein EspC translocator"
FT /evidence="ECO:0000250"
FT /id="PRO_0000041759"
FT DOMAIN 55..297
FT /note="Peptidase S6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01028"
FT DOMAIN 1039..1305
FT /note="Autotransporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00556"
FT ACT_SITE 125
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01028"
FT ACT_SITE 153
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01028"
FT ACT_SITE 256
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01028"
FT SITE 1018..1019
FT /note="Cleavage"
FT /evidence="ECO:0000250"
FT MUTAGEN 256
FT /note="S->I: Abolishes protease and cytotoxic activities."
FT /evidence="ECO:0000269|PubMed:15155671"
FT CONFLICT 55
FT /note="Q -> G (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 209
FT /note="V -> A (in Ref. 1; AAC44731)"
FT /evidence="ECO:0000305"
FT CONFLICT 287
FT /note="W -> G (in Ref. 1; AAC44731)"
FT /evidence="ECO:0000305"
FT CONFLICT 333
FT /note="E -> A (in Ref. 1; AAC44731)"
FT /evidence="ECO:0000305"
FT CONFLICT 514
FT /note="N -> H (in Ref. 1; AAC44731)"
FT /evidence="ECO:0000305"
FT CONFLICT 849..850
FT /note="MK -> IR (in Ref. 1; AAC44731)"
FT /evidence="ECO:0000305"
FT CONFLICT 921
FT /note="N -> T (in Ref. 1; AAC44731)"
FT /evidence="ECO:0000305"
FT CONFLICT 1189
FT /note="S -> I (in Ref. 1; AAC44731)"
FT /evidence="ECO:0000305"
FT CONFLICT 1300
FT /note="N -> D (in Ref. 2; AAG37043)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1305 AA; 140782 MW; 8ECE9ED225CDFF5C CRC64;
MNKIYALKYC HATGGLIAVS ELASRVMKKA ARGSLLALFN LSLYGAFLSA SQAAQLNIDN
VWARDYLDLA QNKGVFKAGA TNVSIQLKNG QTFNFPNVPI PDFSPASNKG ATTSIGGAYS
VTATHNGTTH HAISTQNWGQ SSYKYIDRMT NGDFAVTRLD KFVVETTGVK NSVDFSLNSH
DALERYGVEI NGEKKIIGFR VGAGTTYTVQ NGNTYSTGQV YNPLLLSASM FQLNWDNKRP
YNNTTPFYNE TTGGDSGSGF YLYDNVKKEW VMLGTLFGIA SSGADVWSIL NQYDENTVNG
LKNKFTQKVQ LNNNTMSLNS DSFTLAGNNT AVEKNNNNYK DLSFSGGGSI NFDNDVNIGS
GGLIFDAGHH YTVTGNNKTF KGAGLDIGDN TTVDWNVKGV VGDNLHKIGA GTLNVNVSQG
NNLKTGDGLV VLNSANAFDN IYMASGHGVV KINHSAALNQ NNDYRGIFFT ENGGTLDLNG
YDQSFNKIAA TDIGALITNS AVQKAVLSVN NQSNYMYHGS VSGNTEINHQ FDTQKNNSRL
ILDGNVDITN DINIKNSQLT MQGHATSHAV FREGGVTCML PGVICEKDYV SGIQQQENSA
NKNNNTDYKT NNQVSSFEQP DWENRLFKFK TLNLINSDFI VGRNAIVVGD ISANNSTLSL
SGKDTKVHID MYDGKNITGD GFGFRQDIKD GVSVSPESSS YFGNVTLNNH SLLDIGNKFT
GGIEAYDSSV SVTSQNAVFD RVGSFVNSSL TLEKGAKLTA QGGIFSTGAV DVKENASLIL
TGTPSAQKQE YYSPVISTTE GINLGDKASL SVKNMGYLSS DIHAGTTAAT INLGDGDAET
DSPLFSSLMK GYNAVLSGNI TGEQSTVNMN NALWYSDGNS TIGTLKSTGG RVELGGGKDF
ATLRVKELNA NNATFLMHTN NSQADQLNVT NKLLGSNNTV LVDFLNKPAS EMNVTLITAP
KGSDEKTFTA GTQQIGFSNV TPVISTEKTD DATKWMLTGY QTVSDAGASK TATDFMASGY
KSFLTEVNNL NKRMGDLRDT QGDAGVWARI MNGTGSADGG YSDNYTHVQI GADRKHELDG
VDLFTGALLT YTDSNASSHA FSGKTKSVGG GLYASALFDS GAYFDLIGKY LHHDNQYTAS
FASLGTKDYS SHSWYAGAEV GYRYHLSEES WVEPQMELVY GSVSGKSFSW EDRGMALSMK
DKDYNPLIGR TGVDVGRTFS GDDWKITARA GLGYQFDLLA NGETVLRDAS GEKRFEGEKD
SRMLMNVGMN AEIKDNMRFG LELEKSAFGK YNVDNAINAN FRYSF
