ESPP_ECO57
ID ESPP_ECO57 Reviewed; 1300 AA.
AC Q7BSW5; O32555; Q9S6R3;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Serine protease EspP;
DE EC=3.4.21.-;
DE Contains:
DE RecName: Full=Secreted autotransporter protein EspP;
DE AltName: Full=Extracellular serine protease plasmid-encoded EspP;
DE Contains:
DE RecName: Full=Autotransporter protein EspP translocator;
DE Flags: Precursor;
GN Name=espP; OrderedLocusNames=L7020, ECO57PM78;
OS Escherichia coli O157:H7.
OG Plasmid pO157.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 56-65 AND 1024-1033,
RP FUNCTION, AND ACTIVITY REGULATION.
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=9194704; DOI=10.1046/j.1365-2958.1997.3871751.x;
RA Brunder W., Schmidt H., Karch H.;
RT "EspP, a novel extracellular serine protease of enterohaemorrhagic
RT Escherichia coli O157:H7 cleaves human coagulation factor V.";
RL Mol. Microbiol. 24:767-778(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=9722640; DOI=10.1093/nar/26.18.4196;
RA Burland V., Shao Y., Perna N.T., Plunkett G. III, Sofia H.J.,
RA Blattner F.R.;
RT "The complete DNA sequence and analysis of the large virulence plasmid of
RT Escherichia coli O157:H7.";
RL Nucleic Acids Res. 26:4196-4204(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=9628576; DOI=10.1093/dnares/5.1.1;
RA Makino K., Ishii K., Yasunaga T., Hattori M., Yokoyama K., Yatsudo H.C.,
RA Kubota Y., Yamaichi Y., Iida T., Yamamoto K., Honda T., Han C.G.,
RA Ohtsubo A., Kasamatsu M., Hayashi T., Kuhara S., Shinagawa H.;
RT "Complete nucleotide sequences of 93-kb and 3.3-kb plasmids of an
RT enterohemorrhagic Escherichia coli O157:H7 derived from Sakai outbreak.";
RL DNA Res. 5:1-9(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 455-1300.
RC STRAIN=O157:H7 / 3010/96 / EHEC;
RX PubMed=10376815; DOI=10.1099/13500872-145-5-1005;
RA Brunder W., Schmidt H., Frosch M., Karch H.;
RT "The large plasmids of Shiga-toxin-producing Escherichia coli (STEC) are
RT highly variable genetic elements.";
RL Microbiology 145:1005-1014(1999).
RN [5]
RP MUTAGENESIS.
RX PubMed=15151995; DOI=10.1074/jbc.m404424200;
RA Velarde J.J., Nataro J.P.;
RT "Hydrophobic residues of the autotransporter EspP linker domain are
RT important for outer membrane translocation of its passenger.";
RL J. Biol. Chem. 279:31495-31504(2004).
RN [6]
RP FUNCTION OF THE SIGNAL PEPTIDE.
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=15615856; DOI=10.1073/pnas.0406055102;
RA Szabady R.L., Peterson J.H., Skillman K.M., Bernstein H.D.;
RT "An unusual signal peptide facilitates late steps in the biogenesis of a
RT bacterial autotransporter.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:221-226(2005).
CC -!- FUNCTION: Serine protease capable of cleaving pepsin A and human
CC coagulation factor V, which may contribute to the mucosal hemorrhage
CC observed in hemorrhagic colitis. {ECO:0000269|PubMed:15615856,
CC ECO:0000269|PubMed:9194704}.
CC -!- ACTIVITY REGULATION: Inhibition of cytotoxic activity by
CC phenylmethylsulfonyl fluoride. {ECO:0000269|PubMed:9194704}.
CC -!- INTERACTION:
CC Q7BSW5; P0ABZ8: surA; NbExp=3; IntAct=EBI-6408724, EBI-6408783;
CC -!- SUBCELLULAR LOCATION: [Serine protease EspP]: Periplasm {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Secreted autotransporter protein EspP]:
CC Secreted. Cell surface.
CC -!- SUBCELLULAR LOCATION: [Autotransporter protein EspP 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 optimal at 37 degrees Celsius, and inhibited
CC at 20 degrees Celsius. It is dependent on both temperature and pH.
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 (PubMed:15615856).
CC {ECO:0000269|PubMed:15615856}.
CC -!- PTM: Cleaved to release the mature protein from the outer membrane.
CC -!- MISCELLANEOUS: Mutagenesis experiments show the presence of a linker
CC region, which is required for the translocation of the protease domain
CC across the outer membrane. This linker region is located immediately
CC upstream of the C-terminal helper domain.
CC -!- MISCELLANEOUS: The signal peptide may also act as a transient membrane
CC anchor that prevents the protease domain from misfolding in the
CC periplasm.
CC -!- CAUTION: Strain 3010/96 exhibits a partial deletion of the gene.
CC {ECO:0000305}.
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DR EMBL; X97542; CAA66144.1; -; Genomic_DNA.
DR EMBL; AF074613; AAC70088.1; -; Genomic_DNA.
DR EMBL; AB011549; BAA31836.1; -; Genomic_DNA.
DR EMBL; AJ010390; CAB42538.1; -; Genomic_DNA.
DR PIR; T00317; T00317.
DR RefSeq; NP_052685.1; NC_002128.1.
DR RefSeq; WP_001034100.1; NZ_SEKS01000027.1.
DR RefSeq; YP_002756610.1; NC_012487.1.
DR PDB; 2QOM; X-ray; 2.66 A; A/B=1024-1300.
DR PDB; 3SLJ; X-ray; 2.48 A; A=999-1300.
DR PDB; 3SLO; X-ray; 2.52 A; A=999-1300.
DR PDB; 3SLT; X-ray; 2.46 A; A=999-1300.
DR PDB; 3SZE; X-ray; 2.50 A; A=56-1023.
DR PDBsum; 2QOM; -.
DR PDBsum; 3SLJ; -.
DR PDBsum; 3SLO; -.
DR PDBsum; 3SLT; -.
DR PDBsum; 3SZE; -.
DR AlphaFoldDB; Q7BSW5; -.
DR SMR; Q7BSW5; -.
DR IntAct; Q7BSW5; 4.
DR STRING; 155864.EDL933_p0019; -.
DR MEROPS; S06.002; -.
DR TCDB; 1.B.12.4.3; the autotransporter-1 (at-1) family.
DR EnsemblBacteria; AAC70088; AAC70088; Z_L7020.
DR EnsemblBacteria; BAA31836; BAA31836; BAA31836.
DR GeneID; 1789732; -.
DR KEGG; ece:Z_L7020; -.
DR KEGG; ecs:pO157p78; -.
DR PATRIC; fig|386585.9.peg.90; -.
DR eggNOG; COG3468; Bacteria.
DR HOGENOM; CLU_000723_0_0_6; -.
DR OMA; IIGFRVG; -.
DR EvolutionaryTrace; Q7BSW5; -.
DR Proteomes; UP000000558; Plasmid pO157.
DR Proteomes; UP000002519; Plasmid pO157.
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; 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..55
FT /evidence="ECO:0000269|PubMed:9194704"
FT CHAIN 56..1300
FT /note="Serine protease EspP"
FT /id="PRO_0000387594"
FT CHAIN 56..1023
FT /note="Secreted autotransporter protein EspP"
FT /id="PRO_0000042020"
FT CHAIN 1024..1300
FT /note="Autotransporter protein EspP translocator"
FT /evidence="ECO:0000250"
FT /id="PRO_0000042021"
FT DOMAIN 57..311
FT /note="Peptidase S6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01028"
FT DOMAIN 1034..1300
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 156
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01028"
FT ACT_SITE 263
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01028"
FT SITE 1023..1024
FT /note="Cleavage"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:3SZE"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:3SZE"
FT HELIX 65..73
FT /evidence="ECO:0007829|PDB:3SZE"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:3SZE"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:3SZE"
FT STRAND 121..125
FT /evidence="ECO:0007829|PDB:3SZE"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:3SZE"
FT HELIX 133..136
FT /evidence="ECO:0007829|PDB:3SZE"
FT STRAND 137..140
FT /evidence="ECO:0007829|PDB:3SZE"
FT STRAND 143..153
FT /evidence="ECO:0007829|PDB:3SZE"
FT TURN 154..156
FT /evidence="ECO:0007829|PDB:3SZE"
FT STRAND 157..164
FT /evidence="ECO:0007829|PDB:3SZE"
FT HELIX 182..189
FT /evidence="ECO:0007829|PDB:3SZE"
FT STRAND 191..198
FT /evidence="ECO:0007829|PDB:3SZE"
FT STRAND 200..205
FT /evidence="ECO:0007829|PDB:3SZE"
FT STRAND 208..213
FT /evidence="ECO:0007829|PDB:3SZE"
FT STRAND 216..220
FT /evidence="ECO:0007829|PDB:3SZE"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:3SZE"
FT STRAND 231..248
FT /evidence="ECO:0007829|PDB:3SZE"
FT STRAND 251..254
FT /evidence="ECO:0007829|PDB:3SZE"
FT STRAND 266..271
FT /evidence="ECO:0007829|PDB:3SZE"
FT TURN 272..275
FT /evidence="ECO:0007829|PDB:3SZE"
FT STRAND 276..288
FT /evidence="ECO:0007829|PDB:3SZE"
FT HELIX 290..292
FT /evidence="ECO:0007829|PDB:3SZE"
FT STRAND 294..300
FT /evidence="ECO:0007829|PDB:3SZE"
FT HELIX 303..312
FT /evidence="ECO:0007829|PDB:3SZE"
FT STRAND 314..318
FT /evidence="ECO:0007829|PDB:3SZE"
FT STRAND 324..328
FT /evidence="ECO:0007829|PDB:3SZE"
FT STRAND 331..337
FT /evidence="ECO:0007829|PDB:3SZE"
FT STRAND 344..351
FT /evidence="ECO:0007829|PDB:3SZE"
FT STRAND 353..359
FT /evidence="ECO:0007829|PDB:3SZE"
FT STRAND 368..370
FT /evidence="ECO:0007829|PDB:3SZE"
FT STRAND 375..379
FT /evidence="ECO:0007829|PDB:3SZE"
FT STRAND 384..388
FT /evidence="ECO:0007829|PDB:3SZE"
FT STRAND 390..392
FT /evidence="ECO:0007829|PDB:3SZE"
FT STRAND 397..400
FT /evidence="ECO:0007829|PDB:3SZE"
FT STRAND 402..404
FT /evidence="ECO:0007829|PDB:3SZE"
FT STRAND 410..420
FT /evidence="ECO:0007829|PDB:3SZE"
FT STRAND 428..437
FT /evidence="ECO:0007829|PDB:3SZE"
FT STRAND 446..457
FT /evidence="ECO:0007829|PDB:3SZE"
FT STRAND 466..468
FT /evidence="ECO:0007829|PDB:3SZE"
FT STRAND 471..473
FT /evidence="ECO:0007829|PDB:3SZE"
FT STRAND 478..481
FT /evidence="ECO:0007829|PDB:3SZE"
FT STRAND 487..490
FT /evidence="ECO:0007829|PDB:3SZE"
FT STRAND 499..502
FT /evidence="ECO:0007829|PDB:3SZE"
FT STRAND 505..507
FT /evidence="ECO:0007829|PDB:3SZE"
FT STRAND 509..513
FT /evidence="ECO:0007829|PDB:3SZE"
FT STRAND 519..521
FT /evidence="ECO:0007829|PDB:3SZE"
FT STRAND 523..534
FT /evidence="ECO:0007829|PDB:3SZE"
FT STRAND 544..546
FT /evidence="ECO:0007829|PDB:3SZE"
FT STRAND 548..551
FT /evidence="ECO:0007829|PDB:3SZE"
FT STRAND 556..560
FT /evidence="ECO:0007829|PDB:3SZE"
FT STRAND 562..565
FT /evidence="ECO:0007829|PDB:3SZE"
FT HELIX 596..603
FT /evidence="ECO:0007829|PDB:3SZE"
FT HELIX 605..611
FT /evidence="ECO:0007829|PDB:3SZE"
FT HELIX 614..617
FT /evidence="ECO:0007829|PDB:3SZE"
FT STRAND 632..643
FT /evidence="ECO:0007829|PDB:3SZE"
FT STRAND 645..648
FT /evidence="ECO:0007829|PDB:3SZE"
FT STRAND 652..662
FT /evidence="ECO:0007829|PDB:3SZE"
FT STRAND 664..668
FT /evidence="ECO:0007829|PDB:3SZE"
FT STRAND 670..675
FT /evidence="ECO:0007829|PDB:3SZE"
FT TURN 676..679
FT /evidence="ECO:0007829|PDB:3SZE"
FT TURN 684..687
FT /evidence="ECO:0007829|PDB:3SZE"
FT STRAND 693..697
FT /evidence="ECO:0007829|PDB:3SZE"
FT STRAND 702..706
FT /evidence="ECO:0007829|PDB:3SZE"
FT STRAND 708..712
FT /evidence="ECO:0007829|PDB:3SZE"
FT STRAND 714..717
FT /evidence="ECO:0007829|PDB:3SZE"
FT STRAND 721..725
FT /evidence="ECO:0007829|PDB:3SZE"
FT STRAND 729..733
FT /evidence="ECO:0007829|PDB:3SZE"
FT STRAND 735..738
FT /evidence="ECO:0007829|PDB:3SZE"
FT STRAND 743..746
FT /evidence="ECO:0007829|PDB:3SZE"
FT STRAND 750..754
FT /evidence="ECO:0007829|PDB:3SZE"
FT STRAND 756..765
FT /evidence="ECO:0007829|PDB:3SZE"
FT STRAND 777..787
FT /evidence="ECO:0007829|PDB:3SZE"
FT STRAND 793..810
FT /evidence="ECO:0007829|PDB:3SZE"
FT STRAND 813..818
FT /evidence="ECO:0007829|PDB:3SZE"
FT HELIX 832..839
FT /evidence="ECO:0007829|PDB:3SZE"
FT STRAND 842..848
FT /evidence="ECO:0007829|PDB:3SZE"
FT STRAND 850..866
FT /evidence="ECO:0007829|PDB:3SZE"
FT STRAND 870..879
FT /evidence="ECO:0007829|PDB:3SZE"
FT STRAND 881..884
FT /evidence="ECO:0007829|PDB:3SZE"
FT STRAND 895..905
FT /evidence="ECO:0007829|PDB:3SZE"
FT STRAND 907..915
FT /evidence="ECO:0007829|PDB:3SZE"
FT STRAND 919..927
FT /evidence="ECO:0007829|PDB:3SZE"
FT STRAND 931..939
FT /evidence="ECO:0007829|PDB:3SZE"
FT STRAND 943..945
FT /evidence="ECO:0007829|PDB:3SZE"
FT STRAND 949..955
FT /evidence="ECO:0007829|PDB:3SZE"
FT HELIX 960..962
FT /evidence="ECO:0007829|PDB:3SZE"
FT STRAND 963..965
FT /evidence="ECO:0007829|PDB:3SZE"
FT STRAND 975..983
FT /evidence="ECO:0007829|PDB:3SZE"
FT STRAND 985..997
FT /evidence="ECO:0007829|PDB:3SZE"
FT HELIX 999..1020
FT /evidence="ECO:0007829|PDB:3SLT"
FT HELIX 1025..1029
FT /evidence="ECO:0007829|PDB:3SLT"
FT STRAND 1038..1052
FT /evidence="ECO:0007829|PDB:3SLT"
FT HELIX 1053..1055
FT /evidence="ECO:0007829|PDB:3SLT"
FT STRAND 1056..1073
FT /evidence="ECO:0007829|PDB:3SLT"
FT STRAND 1076..1093
FT /evidence="ECO:0007829|PDB:3SLT"
FT STRAND 1096..1113
FT /evidence="ECO:0007829|PDB:3SLT"
FT STRAND 1116..1134
FT /evidence="ECO:0007829|PDB:3SLT"
FT HELIX 1136..1138
FT /evidence="ECO:0007829|PDB:3SLT"
FT STRAND 1140..1157
FT /evidence="ECO:0007829|PDB:3SLT"
FT STRAND 1159..1178
FT /evidence="ECO:0007829|PDB:3SLT"
FT STRAND 1182..1187
FT /evidence="ECO:0007829|PDB:3SLT"
FT STRAND 1190..1196
FT /evidence="ECO:0007829|PDB:3SLT"
FT STRAND 1202..1216
FT /evidence="ECO:0007829|PDB:3SLT"
FT STRAND 1219..1233
FT /evidence="ECO:0007829|PDB:3SLT"
FT STRAND 1238..1242
FT /evidence="ECO:0007829|PDB:3SLT"
FT STRAND 1247..1251
FT /evidence="ECO:0007829|PDB:3SLT"
FT STRAND 1256..1268
FT /evidence="ECO:0007829|PDB:3SLT"
FT TURN 1269..1271
FT /evidence="ECO:0007829|PDB:3SLT"
FT STRAND 1272..1300
FT /evidence="ECO:0007829|PDB:3SLT"
SQ SEQUENCE 1300 AA; 141758 MW; E34D3F037DEC672F CRC64;
MNKIYSLKYS HITGGLIAVS ELSGRVSSRA TGKKKHKRIL ALCFLGLLQS SYSFASQMDI
SNFYIRDYMD FAQNKGIFQA GATNIEIVKK DGSTLKLPEV PFPDFSPVAN KGSTTSIGGA
YSITATHNTK NHHSVATQNW GNSTYKQTDW NTSHPDFAVS RLDKFVVETR GATEGADISL
SKQQALERYG VNYKGEKKLI AFRAGSGVVS VKKNGRITPF NEVSYKPEML NGSFVHIDDW
SGWLILTNNQ FDEFNNIASQ GDSGSALFVY DNQKKKWVVA GTVWGIYNYA NGKNHAAYSK
WNQTTIDNLK NKYSYNVDMS GAQVATIENG KLTGTGSDTT DIKNKDLIFT GGGDILLKSS
FDNGAGGLVF NDKKTYRVNG DDFTFKGAGV DTRNGSTVEW NIRYDNKDNL HKIGDGTLDV
RKTQNTNLKT GEGLVILGAE KTFNNIYITS GDGTVRLNAE NALSGGEYNG IFFAKNGGTL
DLNGYNQSFN KIAATDSGAV ITNTSTKKSI LSLNNTADYI YHGNINGNLD VLQHHETKKE
NRRLILDGGV DTTNDISLRN TQLSMQGHAT EHAIYRDGAF SCSLPAPMRF LCGSDYVAGM
QNTEADAVKQ NGNAYKTNNA VSDLSQPDWE TGTFRFGTLH LENSDFSVGR NANVIGDIQA
SKSNITIGDT TAYIDLHAGK NITGDGFGFR QNIVRGNSQG ETLFTGGITA EDSTIVIKDK
AKALFSNYVY LLNTKATIEN GADVTTQSGM FSTSDISISG NLSMTGNPDK DNKFEPSIYL
NDASYLLTDD SARLVAKNKA SVVGDIHSTK SASIMFGHDE SDLSQLSDRT SKGLALGLLG
GFDVSYRGSV NAPSASATMN NTWWQLTGDS ALKTLKSTNS MVYFTDSANN KKFHTLTVDE
LATSNSAYAM RTNLSESDKL EVKKHLSGEN NILLVDFLQK PTPEKQLNIE LVSAPKDTNE
NVFKASKQTI GFSDVTPVIT TRETDDKITW SLTGYNTVAN KEATRNAAAL FSVDYKAFLN
EVNNLNKRMG DLRDINGEAG AWARIMSGTG SASGGFSDNY THVQVGVDKK HELDGLDLFT
GFTVTHTDSS ASADVFSGKT KSVGAGLYAS AMFDSGAYID LIGKYVHHDN EYTATFAGLG
TRDYSTHSWY AGAEAGYRYH VTEDAWIEPQ AELVYGSVSG KQFAWKDQGM HLSMKDKDYN
PLIGRTGVDV GKSFSGKDWK VTARAGLGYQ FDLLANGETV LRDASGEKRI KGEKDSRMLM
SVGLNAEIRD NVRFGLEFEK SAFGKYNVDN AVNANFRYSF
