PIC_ECOL6
ID PIC_ECOL6 Reviewed; 1371 AA.
AC Q8CWC7;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Serine protease pic autotransporter;
DE EC=3.4.21.-;
DE Contains:
DE RecName: Full=Serine protease pic;
DE Contains:
DE RecName: Full=Serine protease pic translocator;
DE Flags: Precursor;
GN Name=pic; Synonyms=she; OrderedLocusNames=c0350;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
RN [2]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=14688142; DOI=10.1128/iai.72.1.593-597.2004;
RA Heimer S.R., Rasko D.A., Lockatell C.V., Johnson D.E., Mobley H.L.T.;
RT "Autotransporter genes pic and tsh are associated with Escherichia coli
RT strains that cause acute pyelonephritis and are expressed during urinary
RT tract infection.";
RL Infect. Immun. 72:593-597(2004).
CC -!- FUNCTION: Involved in virulence of uropathogenic E.coli although it is
CC not known how it contributes to it. Has no mucinase activity.
CC {ECO:0000269|PubMed:14688142}.
CC -!- SUBCELLULAR LOCATION: [Serine protease pic autotransporter]: Periplasm
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Serine protease pic]: Secreted. Cell surface.
CC -!- SUBCELLULAR LOCATION: [Serine protease pic translocator]: Cell outer
CC membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
CC Note=The cleaved C-terminal fragment (autotransporter domain) is
CC 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:0000305}.
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DR EMBL; AE014075; AAN78833.1; -; Genomic_DNA.
DR RefSeq; WP_001045652.1; NC_004431.1.
DR AlphaFoldDB; Q8CWC7; -.
DR SMR; Q8CWC7; -.
DR STRING; 199310.c0350; -.
DR MEROPS; S06.005; -.
DR EnsemblBacteria; AAN78833; AAN78833; c0350.
DR KEGG; ecc:c0350; -.
DR eggNOG; COG3210; Bacteria.
DR eggNOG; COG3468; Bacteria.
DR HOGENOM; CLU_000723_0_0_6; -.
DR OMA; ADNSHIA; -.
DR BioCyc; ECOL199310:C0350-MON; -.
DR Proteomes; UP000001410; 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 3: Inferred from homology;
KW Cell outer membrane; Hydrolase; Membrane; Periplasm; Protease; Secreted;
KW Serine protease; Signal; Transmembrane; Transmembrane beta strand;
KW Virulence; Zymogen.
FT SIGNAL 1..55
FT CHAIN 56..1371
FT /note="Serine protease pic autotransporter"
FT /id="PRO_0000387606"
FT CHAIN 56..1094
FT /note="Serine protease pic"
FT /id="PRO_0000026974"
FT CHAIN 1095..1371
FT /note="Serine protease pic translocator"
FT /evidence="ECO:0000255"
FT /id="PRO_0000026975"
FT DOMAIN 56..301
FT /note="Peptidase S6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01028"
FT DOMAIN 1105..1371
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 155
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01028"
FT ACT_SITE 258
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01028"
FT SITE 1094..1095
FT /note="Cleavage"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1371 AA; 146588 MW; B93F6681821A2513 CRC64;
MNKVYSLKYC PVTGGLIVVS ELASRVIKKT CRRLTHILLA GIPAVYLYYP QISQAGIVRS
DIAYQIYRDF AENKGLFVPG ATDIPVYDKD GKLVGRLDKA PMADFSSVSS NGVATLVSPQ
YIVSVKHNGG YQSVSFGNGK NTYSLVDRNN HSSVDFHAPR LNKLVTEVIP SAITSEGTKA
NAYKDTERYT AFYRVGSGTQ YTKDKDGNLV KVAGGYAFKT GGTTGVPLIS DATIVSNPGQ
TYNPVNGPLP DYGAPGDSGS PLFAYDEQQK KWVIVAVLRA YAGINGATNW WNVIPTDYLN
QVMQDDFDAP VDFVSGLPPL NWTYDKTSGT GTLSQGSKNW TMHGQKDNDL NAGKNLVFSG
QNGAIVLKDS VTQGAGYLEF KDSYTVSAES GKTWTGAGII TDKGTNVTWK VNGVAGDNLH
KLGEGTLTIN GTGVNPGGLK TGDGTVVLNQ QADTAGNVQA FSSVNLASGR PTVVLGDARQ
VNPDNISWGY RGGKLDLNGN AVTFTRLQAA DYGAVITNNA QQKSRLLLDL KAQDTNVSVP
IGSISPFGGT GTPGNLYSMI LNGQTRFYIL KSASYGNTLW GNSLNDPAQW EFVGTDKNKA
VQTVKDRILA GRAKQPVIFH GQLTGNMDVT IPQLPGGRKV ILDGSVNLPE GTLSEDSGTL
IFQGHPVIHA SVSGSAPVSL NQKDWENRQF IMKTLSLKDA DFHLSRNASL NSDIKSDNSH
ITLGSDRVFV DKNDGTGNYV ILEEGTSVPD TVNDRSQYEG NITLDHNSTL DIGSRFTGGI
EAYDSAVSIT SPDVLLTAPG AFAGSSLTVH DGGHLTALNG LFSDGHIQAG KNSKITLSGT
PVKDTANQYA PAVYLTDGYD LTGDNATLEI TRGAHASGDI HASAASTVTI GSDTPAELAS
AETTASAFAG SLLEGYNAAF NGAITGGRAD VSMHNALWTL GGDSAIHTLT VRNSRISSEG
DRTFRTLTVN KLDATGSDFV LRTDLKNADK INVTEKATGS DNSLNVSFMK DPAQGQSLNI
PLVTAPAGTS AEMFKAGTRM IGFSRVTPTL HVDTSGGNTK WILDGFKAEA DKAAAAKADS
FMNAGYKNFM TEVNNLNKRM GDLRDTNGDA GAWARIMSGA GSADGGYSDN YTHVQVGFDK
KHELDGVDLF TGVTMTYTDS SADSHAFSGK TKSVGGGLYA SALFESGAYI DLIGKYIHHD
NDYTGNFAGL GTKHYNTHSW YAGAETGYRY HLTEETFIEP QAELVYGAVS GKTFRWKDGD
MDLSMKNRDF SPLIGRTGIE LGKTFSGKDW SVTARAGTSW QFDLLNNGET VLRDASGEKR
IKGEKDSRML FNVGMNAQIK DNMRFGLEFE KSAFGKYNVD NAVNANFRYM F
