SEPA_SHIFL
ID SEPA_SHIFL Reviewed; 1364 AA.
AC Q8VSL2; Q54165; Q99QC6;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Serine protease SepA autotransporter;
DE EC=3.4.21.-;
DE Contains:
DE RecName: Full=Serine protease SepA;
DE Contains:
DE RecName: Full=Serine protease SepA translocator;
DE Flags: Precursor;
GN Name=sepA; OrderedLocusNames=CP0070;
OS Shigella flexneri.
OG Plasmid pWR100, and Plasmid pCP301.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 57-72; 541-555
RP AND 1054-1066.
RC STRAIN=M90T / Serotype 5a; PLASMID=pWR100;
RX PubMed=7476198; DOI=10.1111/j.1365-2958.1995.mmi_17010123.x;
RA Benjelloun-Touimi Z., Sansonetti P.J., Parsot C.;
RT "SepA, the major extracellular protein of Shigella flexneri: autonomous
RT secretion and involvement in tissue invasion.";
RL Mol. Microbiol. 17:123-135(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=M90T / Serotype 5a; PLASMID=pWR100;
RX PubMed=11115111; DOI=10.1046/j.1365-2958.2000.02179.x;
RA Buchrieser C., Glaser P., Rusniok C., Nedjari H., d'Hauteville H.,
RA Kunst F., Sansonetti P.J., Parsot C.;
RT "The virulence plasmid pWR100 and the repertoire of proteins secreted by
RT the type III secretion apparatus of Shigella flexneri.";
RL Mol. Microbiol. 38:760-771(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=M90T / Serotype 5a; PLASMID=pWR100;
RX PubMed=11292750; DOI=10.1128/iai.69.5.3271-3285.2001;
RA Venkatesan M.M., Goldberg M.B., Rose D.J., Grotbeck E.J., Burland V.,
RA Blattner F.R.;
RT "Complete DNA sequence and analysis of the large virulence plasmid of
RT Shigella flexneri.";
RL Infect. Immun. 69:3271-3285(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a; PLASMID=pCP301;
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 FUNCTION, ACTIVITY REGULATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=M90T / Serotype 5a; PLASMID=pWR100;
RX PubMed=9695914; DOI=10.1099/00221287-144-7-1815;
RA Benjelloun-Touimi Z., Si Tahar M., Montecucco C., Sansonetti P.J.,
RA Parsot C.;
RT "SepA, the 110 kDa protein secreted by Shigella flexneri: two-domain
RT structure and proteolytic activity.";
RL Microbiology 144:1815-1822(1998).
CC -!- FUNCTION: Major protein secreted in laboratory media showing
CC proteolytic activity. May be involved in invasion and destruction of
CC host intestinal epithelium. {ECO:0000269|PubMed:9695914}.
CC -!- ACTIVITY REGULATION: Inhibited by the serine protease inhibitor PMSF,
CC but not by benzamidine, alpha 1-antitrypsin, alpha 1-antichymotrypsin.
CC Not inhibited by metalloprotease inhibitors such as EDTA and
CC orthophenanthroline. {ECO:0000269|PubMed:9695914}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius.;
CC -!- SUBCELLULAR LOCATION: [Serine protease SepA autotransporter]: Periplasm
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Serine protease SepA]: Secreted. Cell surface.
CC -!- SUBCELLULAR LOCATION: [Serine protease SepA 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 Cleavage is performed by an unknown protease.
CC -!- DISRUPTION PHENOTYPE: Mutants exhibit an attenuated virulence in the
CC rabbit ligated ileal loop model. {ECO:0000269|PubMed:9695914}.
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DR EMBL; Z48219; CAA88252.1; -; Genomic_DNA.
DR EMBL; AL391753; CAC05786.1; -; Genomic_DNA.
DR EMBL; AF348706; AAK18385.1; -; Genomic_DNA.
DR EMBL; AF386526; AAL72309.1; -; Genomic_DNA.
DR PIR; S57664; S57664.
DR RefSeq; NP_858203.1; NC_004851.1.
DR RefSeq; WP_010921633.1; NZ_QWST01000246.1.
DR PDB; 5J44; X-ray; 2.91 A; A/B=57-1089.
DR PDBsum; 5J44; -.
DR AlphaFoldDB; Q8VSL2; -.
DR SMR; Q8VSL2; -.
DR STRING; 198214.CP0070; -.
DR MEROPS; S06.013; -.
DR EnsemblBacteria; AAL72309; AAL72309; SF_p0070.
DR GeneID; 1238005; -.
DR KEGG; sfl:CP0070; -.
DR PATRIC; fig|198214.7.peg.5314; -.
DR HOGENOM; CLU_000723_0_0_6; -.
DR Proteomes; UP000001006; Plasmid pCP301.
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; IPR009003; Peptidase_S1_PA.
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; SSF50494; SSF50494; 1.
DR SUPFAM; SSF51126; SSF51126; 1.
DR TIGRFAMs; TIGR01414; autotrans_barl; 1.
DR PROSITE; PS51208; AUTOTRANSPORTER; 1.
DR PROSITE; PS51691; PEPTIDASE_S6; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Direct protein sequencing; Hydrolase;
KW Membrane; Periplasm; Plasmid; Protease; Reference proteome; Secreted;
KW Serine protease; Signal; Transmembrane; Transmembrane beta strand;
KW Virulence; Zymogen.
FT SIGNAL 1..56
FT /evidence="ECO:0000269|PubMed:7476198"
FT CHAIN 57..1364
FT /note="Serine protease SepA autotransporter"
FT /id="PRO_0000387609"
FT CHAIN 57..1089
FT /note="Serine protease SepA"
FT /id="PRO_0000026980"
FT CHAIN 1090..1364
FT /note="Serine protease SepA translocator"
FT /evidence="ECO:0000255"
FT /id="PRO_0000026981"
FT DOMAIN 57..307
FT /note="Peptidase S6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01028"
FT DOMAIN 1098..1364
FT /note="Autotransporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00556"
FT ACT_SITE 134
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01028"
FT ACT_SITE 162
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01028"
FT ACT_SITE 267
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01028"
FT SITE 1089..1090
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT VARIANT 600
FT /note="R -> H (in plasmid pWR100)"
FT VARIANT 740
FT /note="F -> S (in plasmid pWR100)"
FT CONFLICT 252..254
FT /note="NPA -> LIPP (in Ref. 1; CAA88252)"
FT /evidence="ECO:0000305"
FT CONFLICT 347..355
FT /note="DMHGKKGND -> GYAWKERKLI (in Ref. 1; CAA88252)"
FT /evidence="ECO:0000305"
FT CONFLICT 460
FT /note="A -> R (in Ref. 1; CAA88252)"
FT /evidence="ECO:0000305"
FT CONFLICT 1251
FT /note="D -> A (in Ref. 1; CAA88252)"
FT /evidence="ECO:0000305"
FT STRAND 58..63
FT /evidence="ECO:0007829|PDB:5J44"
FT HELIX 65..73
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 85..88
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 94..98
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 122..125
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 139..145
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 148..157
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 164..170
FT /evidence="ECO:0007829|PDB:5J44"
FT TURN 187..190
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 194..203
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 216..218
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 227..230
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:5J44"
FT TURN 238..241
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 242..245
FT /evidence="ECO:0007829|PDB:5J44"
FT HELIX 253..255
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 270..275
FT /evidence="ECO:0007829|PDB:5J44"
FT TURN 276..279
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 280..290
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 295..299
FT /evidence="ECO:0007829|PDB:5J44"
FT HELIX 302..305
FT /evidence="ECO:0007829|PDB:5J44"
FT HELIX 307..311
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 321..323
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 326..331
FT /evidence="ECO:0007829|PDB:5J44"
FT TURN 332..335
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 336..341
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 344..349
FT /evidence="ECO:0007829|PDB:5J44"
FT HELIX 356..358
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 361..373
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 383..388
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 390..397
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 399..407
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 412..416
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 424..435
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 438..440
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 443..447
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 449..454
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 460..462
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 468..472
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 478..483
FT /evidence="ECO:0007829|PDB:5J44"
FT HELIX 489..491
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 492..494
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 499..502
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 508..511
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 520..523
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 526..528
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 530..534
FT /evidence="ECO:0007829|PDB:5J44"
FT HELIX 541..543
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 548..550
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 563..566
FT /evidence="ECO:0007829|PDB:5J44"
FT TURN 567..570
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 571..575
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 577..580
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 590..596
FT /evidence="ECO:0007829|PDB:5J44"
FT HELIX 600..614
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 619..621
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 623..633
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 637..639
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 641..644
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 654..664
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 686..697
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 699..702
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 706..717
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 719..723
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 726..730
FT /evidence="ECO:0007829|PDB:5J44"
FT TURN 731..735
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 741..745
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 756..766
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 768..771
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 773..783
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 785..788
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 791..803
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 805..808
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 813..818
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 820..824
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 826..828
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 833..836
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 842..844
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 851..856
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 858..860
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 865..868
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 870..875
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 886..890
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 893..895
FT /evidence="ECO:0007829|PDB:5J44"
FT HELIX 903..906
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 911..915
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 919..930
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 932..934
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 939..948
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 950..952
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 956..958
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 961..971
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 973..978
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 985..993
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 997..1005
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 1013..1019
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 1026..1029
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 1032..1034
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 1037..1046
FT /evidence="ECO:0007829|PDB:5J44"
FT STRAND 1049..1061
FT /evidence="ECO:0007829|PDB:5J44"
SQ SEQUENCE 1364 AA; 146017 MW; 653B98500C398D06 CRC64;
MNKIYYLKYC HITKSLIAVS ELARRVTCKS HRRLSRRVIL TSVAALSLSS AWPALSATVS
AEIPYQIFRD FAENKGQFTP GTTNISIYDK QGNLVGKLDK APMADFSSAT ITTGSLPPGD
HTLYSPQYVV TAKHVSGSDT MSFGYAKNTY TAVGTNNNSG LDIKTRRLSK LVTEVAPAEV
SDIGAVSGAY QAGGRFTEFY RLGGGMQYVK DKNGNRTQVY TNGGFLVGGT VSALNSYNNG
QMITAQTGDI FNPANGPLAN YLNMGDSGSP LFAYDSLQKK WVLIGVLSSG TNYGNNWVVT
TQDFLGQQPQ NDFDKTIAYT SGEGVLQWKY DAANGTGTLT QGNTTWDMHG KKGNDLNAGK
NLLFTGNNGE VVLQNSVNQG AGYLQFAGDY RVSALNGQTW MGGGIITDKG THVLWQVNGV
AGDNLHKTGE GTLTVNGTGV NAGGLKVGDG TVILNQQADA DGKVQAFSSV GIASGRPTVV
LSDSQQVNPD NISWGYRGGR LELNGNNLTF TRLQAADYGA IITNNSEKKS TVTLDLQTLK
ASDINVPVNT VSIFGGRGAP GDLYYDSSTK QYFILKASSY SPFFSDLNNS SVWQNVGKDR
NKAIDTVKQQ KIEASSQPYM YHGQLNGNMD VNIPQLSGKD VLALDGSVNL PEGSITKKSG
TLIFQGHPVI HAGTTTSSSQ SDWETRQFTL EKLKLDAATF HLSRNGKMQG DINATNGSTV
ILGSSRVFTD RSDGTGNAVF SVEGSATATT VGDQSDYSGN VTLENKSSLQ IMERFTGGIE
AYDSTVSVTS QNAVFDRVGS FVNSSLTLGK GAKLTAQSGI FSTGAVDVKE NASLTLTGMP
SAQKQGYYSP VISTTEGINL EDNASFSVKN MGYLSSDIHA GTTAATINLG DSDADAGKTD
SPLFSSLMKG YNAVLRGSIT GAQSTVNMIN ALWYSDGKSE AGALKAKGSR IELGDGKHFA
TLQVKELSAD NTTFLMHTNN SRADQLNVTD KLSGSNNSVL VDFLNKPASE MSVTLITAPK
GSDEKTFTAG TQQIGFSNVT PVISTEKTDD ATKWVLTGYQ TTADAGASKA AKDFMASGYK
SFLTEVNNLN KRMGDLRDTQ GDAGVWARIM NGTGSADGDY SDNYTHVQIG VDRKHELDGV
DLFTGALLTY TDSNASSHAF SGKNKSVGGG LYASALFNSG AYFDLIGKYL HHDNQHTANF
ASLGTKDYSS HSWYAGAEVG YRYHLTKESW VEPQIELVYG SVSGKAFSWE DRGMALSMKD
KDYNPLIGRT GVDVGRAFSG DDWKITARAG LGYQFDLLAN GETVLQDASG EKRFEGEKDS
RMLMTVGMNA EIKDNMRLGL ELEKSAFGKY NVDNAINANF RYVF
