PIC_SHIFL
ID PIC_SHIFL Reviewed; 1372 AA.
AC Q54151; Q7UBM2; Q83Q79; Q9AL58;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 3.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Serine protease pic autotransporter;
DE EC=3.4.21.-;
DE AltName: Full=ShMu;
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, sigA; OrderedLocusNames=SF2973, S3178;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=M4243;
RA Noriega F.R.;
RT "ShMu, a protein of S. flexneri 2a with hemagglutinin and mucinase
RT activities is encoded by an open reading frame (she) that forms an
RT antisense gene pair with the operon encoding Shigella entertoxin 1
RT (ShET1).";
RL Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=YSH6000 / Serotype 2a;
RX PubMed=10768931; DOI=10.1128/iai.68.5.2457-2463.2000;
RA Al-Hasani K., Henderson I.R., Sakellaris H., Rajakumar K., Grant T.,
RA Nataro J.P., Robins-Browne R., Adler B.;
RT "The sigA gene which is borne on the she pathogenicity island of Shigella
RT flexneri 2a encodes an exported cytopathic protease involved in intestinal
RT fluid accumulation.";
RL Infect. Immun. 68:2457-2463(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=YSH6000 / Serotype 2a;
RX PubMed=11162180; DOI=10.1006/mpat.2000.0404;
RA Al-Hasani K., Rajakumar K., Bulach D., Robins-Browne R., Adler B.,
RA Sakellaris H.;
RT "Genetic organization of the she pathogenicity island in Shigella flexneri
RT 2a.";
RL Microb. Pathog. 30:1-8(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
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).
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 -!- 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 -!- MISCELLANEOUS: The S.flexneri genes encoding ShET1 enterotoxin subunits
CC set1A and set1B are contained within the pic gene, on the complementary
CC non-coding strand.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK00464.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAN44454.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAP18274.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U35656; AAB58244.1; -; Genomic_DNA.
DR EMBL; AF200692; AAK00464.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE005674; AAN44454.2; ALT_INIT; Genomic_DNA.
DR EMBL; AE014073; AAP18274.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_001045650.1; NZ_UIPV01000021.1.
DR AlphaFoldDB; Q54151; -.
DR SMR; Q54151; -.
DR STRING; 198214.SF2973; -.
DR MEROPS; N04.002; -.
DR MEROPS; S06.005; -.
DR EnsemblBacteria; AAN44454; AAN44454; SF2973.
DR EnsemblBacteria; AAP18274; AAP18274; S3178.
DR KEGG; sfx:S3178; -.
DR HOGENOM; CLU_000723_0_0_6; -.
DR PHI-base; PHI:2980; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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;
KW Reference proteome; Secreted; Serine protease; Signal; Transmembrane;
KW Transmembrane beta strand; Virulence; Zymogen.
FT SIGNAL 1..55
FT /evidence="ECO:0000255"
FT CHAIN 56..1372
FT /note="Serine protease pic autotransporter"
FT /id="PRO_0000387607"
FT CHAIN 56..1095
FT /note="Serine protease pic"
FT /id="PRO_0000026976"
FT CHAIN 1096..1372
FT /note="Serine protease pic translocator"
FT /evidence="ECO:0000255"
FT /id="PRO_0000026977"
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 VARIANT 354
FT /note="K -> E (in strain: M4243 and YSH6000T)"
FT VARIANT 385
FT /note="T -> P (in strain: M4243 and YSH6000T)"
SQ SEQUENCE 1372 AA; 146453 MW; AE47B3C621A61F67 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 WEFVGMNKNK
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
