ID PIC_ECO44 Reviewed; 1372 AA.
AC Q7BS42; D3GV21;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 27-MAR-2024, entry version 102.
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=EC042_4593;
OS Escherichia coli O44:H18 (strain 042 / EAEC).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=216592;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 56-62; 75-82 AND
RP 441-459, MUTAGENESIS OF SER-258, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10531204; DOI=10.1128/iai.67.11.5587-5596.1999;
RA Henderson I.R., Czeczulin J., Eslava C., Noriega F.R., Nataro J.P.;
RT "Characterization of pic, a secreted protease of Shigella flexneri and
RT enteroaggregative Escherichia coli.";
RL Infect. Immun. 67:5587-5596(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=042 / EAEC;
RX PubMed=20098708; DOI=10.1371/journal.pone.0008801;
RA Chaudhuri R.R., Sebaihia M., Hobman J.L., Webber M.A., Leyton D.L.,
RA Goldberg M.D., Cunningham A.F., Scott-Tucker A., Ferguson P.R.,
RA Thomas C.M., Frankel G., Tang C.M., Dudley E.G., Roberts I.S., Rasko D.A.,
RA Pallen M.J., Parkhill J., Nataro J.P., Thomson N.R., Henderson I.R.;
RT "Complete genome sequence and comparative metabolic profiling of the
RT prototypical enteroaggregative Escherichia coli strain 042.";
RL PLoS ONE 5:E8801-E8801(2010).
CC -!- FUNCTION: Involved in intestinal colonization, displays in vitro
CC mucinolytic activity, serum resistance, and hemagglutination. Important
CC to penetrate the intestinal mucus layer. {ECO:0000269|PubMed:10531204}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.0-9.0.;
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius.;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF097644; AAD23953.1; -; Genomic_DNA.
DR EMBL; FN554766; CBG37419.1; -; Genomic_DNA.
DR RefSeq; WP_001045649.1; NC_017626.1.
DR AlphaFoldDB; Q7BS42; -.
DR SMR; Q7BS42; -.
DR MEROPS; N04.002; -.
DR MEROPS; S06.005; -.
DR TCDB; 1.B.12.4.5; the autotransporter-1 (at-1) family.
DR KEGG; elo:EC042_4593; -.
DR PATRIC; fig|216592.3.peg.4768; -.
DR HOGENOM; CLU_000723_0_0_6; -.
DR PHI-base; PHI:3792; -.
DR Proteomes; UP000001407; 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: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 CDD; cd01343; PL1_Passenger_AT; 1.
DR Gene3D; 2.160.20.20; -; 1.
DR Gene3D; 2.40.10.120; -; 1.
DR Gene3D; 2.40.128.130; Autotransporter beta-domain; 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_dom.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR000710; Peptidase_S6.
DR InterPro; IPR030396; Peptidase_S6_dom.
DR NCBIfam; TIGR01414; autotrans_barl; 1.
DR PANTHER; PTHR12338:SF9; ANTIGEN 43; 1.
DR PANTHER; PTHR12338; AUTOTRANSPORTER; 1.
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; Autotransporter; 1.
DR SUPFAM; SSF51126; Pectin lyase-like; 2.
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..55
FT /evidence="ECO:0000269|PubMed:10531204"
FT CHAIN 56..1372
FT /note="Serine protease pic autotransporter"
FT /id="PRO_0000387605"
FT CHAIN 56..1095
FT /note="Serine protease pic"
FT /id="PRO_0000026972"
FT CHAIN 1096..1372
FT /note="Serine protease pic translocator"
FT /evidence="ECO:0000255"
FT /id="PRO_0000026973"
FT DOMAIN 56..301
FT /note="Peptidase S6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01028"
FT DOMAIN 1106..1372
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 1095..1096
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT MUTAGEN 258
FT /note="S->I: No mucinase activity."
FT /evidence="ECO:0000269|PubMed:10531204"
FT CONFLICT 354
FT /note="K -> E (in Ref. 1; AAD23953)"
FT /evidence="ECO:0000305"
FT CONFLICT 385
FT /note="T -> P (in Ref. 1; AAD23953)"
FT /evidence="ECO:0000305"
FT CONFLICT 597
FT /note="D -> N (in Ref. 1; AAD23953)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1372 AA; 146454 MW; 584280AD96814407 CRC64;
MNKVYSLKYC PVTGGLIAVS ELARRVIKKT CRRLTHILLA GIPAICLCYS QISQAGIVRS
DIAYQIYRDF AENKGLFVPG ANDIPVYDKD GKLVGRLGKA PMADFSSVSS NGVATLVSPQ
YIVSVKHNGG YRSVSFGNGK NTYSLVDRNN HPSIDFHAPR LNKLVTEVIP SAVTSEGTKA
NAYKYTERYT AFYRVGSGTQ YTKDKDGNLV KVAGGYAFKT GGTTGVPLIS DATIVSNPGQ
TYNPVNGPLP DYGAPGDSGS PLFAYDKQQK KWVIVAVLRA YAGINGATNW WNVIPTDYLN
QVMQDDFDAP VDFVSGLGPL NWTYDKTSGT GTLSQGSKNW TMHGQKDNDL NAGKNLVFSG
QNGAIILKDS VTQGAGYLEF KDSYTVSAES GKTWTGAGII TDKGTNVTWK VNGVAGDNLH
KLGEGTLTIN GTGVNPGGLK TGDGIVVLNQ QADTAGNIQA FSSVNLASGR PTVVLGDARQ
VNPDNISWGY RGGKLDLNGN AVTFTRLQAA DYGAVITNNA QQKSQLLLDL KAQDTNVSEP
TIGNISPFGG TGTPGNLYSM ILNSQTRFYI LKSASYGNTL WGNSLNDPAQ WEFVGMDKNK
AVQTVKDRIL AGRAKQPVIF HGQLTGNMDV AIPQVPGGRK VIFDGSVNLP EGTLSQDSGT
LIFQGHPVIH ASISGSAPVS LNQKDWENRQ FTMKTLSLKD ADFHLSRNAS LNSDIKSDNS
HITLGSDRAF VDKNDGTGNY VIPEEGTSVP DTVNDRSQYE GNITLNHNSA LDIGSRFTGG
IDAYDSAVSI TSPDVLLTAP GAFAGSSLTV HDGGHLTALN GLFSDGHIQA GKNGKITLSG
TPVKDTANQY APAVYLTDGY DLTGDNAALE ITRGAHASGD IHASAASTVT IGSDTPAELA
SAETAASAFA GSLLEGYNAA FNGAITGGRA DVSMHNALWT LGGDSAIHSL TVRNSRISSE
GDRTFRTLTV NKLDATGSDF VLRTDLKNAD KINVTEKATG SDNSLNVSFM NNPAQGQALN
IPLVTAPAGT SAEMFKAGTR VTGFSRVTPT LHVDTSGGNT KWILDGFKAE ADKAAAAKAD
SFMNAGYKNF MTEVNNLNKR MGDLRDTNGD AGAWARIMSG AGSADGGYSD NYTHVQVGFD
KKHELDGVDL FTGVTMTYTD SSADSHAFSG KTKSVGGGLY ASALFESGAY IDLIGKYIHH
DNDYTGNFAS LGTKHYNTHS WYAGAETGYR YHLTEDTFIE PQAELVYGAV SGKTFRWKDG
DMDLSMKNRD FSPLVGRTGV ELGKTFSGKD WSVTARAGTS WQFDLLNNGE TVLRDASGEK
RIKGEKDSRM LFNVGMNAQI KDNMRFGLEF EKSAFGKYNV DNAVNANFRY MF
//
