ID CATE_ECOLI Reviewed; 753 AA. AC P21179; P76906; P78066; P78168; DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1991, sequence version 1. DT 04-NOV-2026, entry version 213. DE RecName: Full=Catalase HPII; DE EC=1.11.1.6; DE AltName: Full=Hydroxyperoxidase II; GN Name=katE; OrderedLocusNames=b1732, JW1721; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-10. RC STRAIN=K12; RX PubMed=1987146; DOI=10.1128/jb.173.2.514-520.1991; RA von Ossowski I., Mulvey M.R., Leco P.A., Borys A., Loewen P.C.; RT "Nucleotide sequence of Escherichia coli katE, which encodes catalase RT HPII."; RL J. Bacteriol. 173:514-520(1991). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=9097039; DOI=10.1093/dnares/3.6.363; RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., RA Wada C., Yamamoto Y., Horiuchi T.; RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to RT the 28.0-40.1 min region on the linkage map."; RL DNA Res. 3:363-377(1996). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., RA Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1462(1997). RN [4] RP SEQUENCE REVISION TO 198. RX PubMed=16397293; DOI=10.1093/nar/gkj405; RA Riley M., Abe T., Arnaud M.B., Berlyn M.K.B., Blattner F.R., RA Chaudhuri R.R., Glasner J.D., Horiuchi T., Keseler I.M., Kosuge T., RA Mori H., Perna N.T., Plunkett G. III, Rudd K.E., Serres M.H., Thomas G.H., RA Thomson N.R., Wishart D., Wanner B.L.; RT "Escherichia coli K-12: a cooperatively developed annotation snapshot RT -- 2005."; RL Nucleic Acids Res. 34:1-9(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 RT and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [6] RP CROSS-LINK 392-HIS--TYR-415. RX PubMed=9144772; DOI=10.1002/pro.5560060507; RA Bravo J., Fita I., Ferrer J.C., Ens W., Hillar A., Switala J., Loewen P.C.; RT "Identification of a novel bond between a histidine and the essential RT tyrosine in catalase HPII of Escherichia coli."; RL Protein Sci. 6:1016-1023(1997). RN [7] RP X-RAY CRYSTALLOGRAPHY. RX PubMed=7663946; DOI=10.1016/s0969-2126(01)00182-4; RA Bravo J., Verdaguer N., Tormo J., Betzel C., Switala J., Loewen P.C., RA Fita I.; RT "Crystal structure of catalase HPII from Escherichia coli."; RL Structure 3:491-502(1995). RN [8] RP X-RAY CRYSTALLOGRAPHY. RX PubMed=10091651; DOI=10.1110/ps.8.3.490; RA Sevinc M.S., Mate M.J., Switala J., Fita I., Loewen P.C.; RT "Role of the lateral channel in catalase HPII of Escherichia coli."; RL Protein Sci. 8:490-498(1999). RN [9] RP X-RAY CRYSTALLOGRAPHY. RX PubMed=11455600; DOI=10.1002/prot.1092; RA Melik-Adamyan W.R., Bravo J., Carpena X., Switala J., Mate M.J., Fita I., RA Loewen P.C.; RT "Substrate flow in catalases deduced from the crystal structures of active RT site variants of HPII from Escherichia coli."; RL Proteins 44:270-281(2001). CC -!- FUNCTION: Decomposes hydrogen peroxide into water and oxygen; serves to CC protect cells from the toxic effects of hydrogen peroxide. CC -!- CATALYTIC ACTIVITY: CC Reaction=2 H2O2 = O2 + 2 H2O; Xref=Rhea:RHEA:20309, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240; EC=1.11.1.6; CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10013}; CC -!- COFACTOR: CC Name=heme; Xref=ChEBI:CHEBI:30413; CC -!- SUBUNIT: Homotetramer. CC -!- INTERACTION: CC P21179; P21179: katE; NbExp=2; IntAct=EBI-549879, EBI-549879; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- INDUCTION: By entry into stationary phase. CC -!- SIMILARITY: Belongs to the catalase family. HPII subfamily. 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; M55161; AAA24039.1; -; Genomic_DNA. DR EMBL; U00096; AAT48137.1; -; Genomic_DNA. DR EMBL; AP009048; BAA15513.1; -; Genomic_DNA. DR PIR; A39129; A39129. DR RefSeq; WP_000077872.1; NZ_CP009789.1. DR RefSeq; YP_025308.1; NC_000913.3. DR PDB; 1CF9; X-ray; 1.80 A; A/B/C/D=1-753. DR PDB; 1GG9; X-ray; 1.89 A; A/B/C/D=1-753. DR PDB; 1GGE; X-ray; 1.89 A; A/B/C/D=1-753. DR PDB; 1GGF; X-ray; 2.28 A; A/B/C/D=1-753. DR PDB; 1GGH; X-ray; 2.15 A; A/B/C/D=1-753. DR PDB; 1GGJ; X-ray; 1.92 A; A/B/C/D=1-753. DR PDB; 1GGK; X-ray; 2.26 A; A/B/C/D=1-753. DR PDB; 1IPH; X-ray; 2.80 A; A/B/C/D=1-753. DR PDB; 1P7Y; X-ray; 2.40 A; A/B/C/D=1-753. DR PDB; 1P7Z; X-ray; 2.21 A; A/B/C/D=1-753. DR PDB; 1P80; X-ray; 1.65 A; A/B/C/D=1-753. DR PDB; 1P81; X-ray; 1.81 A; A/B/C/D=1-753. DR PDB; 1QF7; X-ray; 2.20 A; A/B/C/D=1-753. DR PDB; 1QWS; X-ray; 1.90 A; A/B/C/D=1-753. DR PDB; 1YE9; X-ray; 2.80 A; A/B/C/D/I/J/K/L=75-300, E/F/G/H/M/N/O/P=309-567. DR PDB; 28WU; X-ray; 2.50 A; A/B/C/D=1-753. DR PDB; 3P9P; X-ray; 1.50 A; A/B/C/D=1-753. DR PDB; 3P9Q; X-ray; 1.48 A; A/B/C/D=1-753. DR PDB; 3P9R; X-ray; 1.90 A; A/B/C/D=1-753. DR PDB; 3P9S; X-ray; 1.90 A; A/B/C/D=1-753. DR PDB; 3PQ2; X-ray; 1.79 A; A/B/C/D=1-753. DR PDB; 3PQ3; X-ray; 1.79 A; A/B/C/D=1-753. DR PDB; 3PQ4; X-ray; 1.79 A; A/B/C/D=1-753. DR PDB; 3PQ5; X-ray; 1.80 A; A/B/C/D=1-753. DR PDB; 3PQ6; X-ray; 1.80 A; A/B/C/D=1-753. DR PDB; 3PQ7; X-ray; 1.80 A; A/B/C/D=1-753. DR PDB; 3PQ8; X-ray; 1.80 A; A/B/C/D=1-753. DR PDB; 3TTT; X-ray; 1.58 A; A/B/C/D=1-753. DR PDB; 3TTU; X-ray; 1.89 A; A/B/C/D=1-753. DR PDB; 3TTV; X-ray; 1.45 A; A/B/C/D=1-753. DR PDB; 3TTW; X-ray; 1.62 A; A/B/C/D=1-753. DR PDB; 3TTX; X-ray; 1.74 A; A/B/C/D=1-753. DR PDB; 3VU3; X-ray; 2.85 A; A=1-753. DR PDB; 4BFL; X-ray; 1.64 A; A/B/C/D=1-753. DR PDB; 4ENP; X-ray; 1.50 A; A/B/C/D=1-753. DR PDB; 4ENQ; X-ray; 1.90 A; A/B/C/D=1-753. DR PDB; 4ENR; X-ray; 1.60 A; A/B/C/D=1-753. DR PDB; 4ENS; X-ray; 1.60 A; A/B/C/D=1-753. DR PDB; 4ENT; X-ray; 1.70 A; A/B/C/D=1-753. DR PDB; 4ENU; X-ray; 1.70 A; A/B/C/D=1-753. DR PDB; 4ENV; X-ray; 1.70 A; A/B/C/D=1-753. DR PDB; 4ENW; X-ray; 1.90 A; A/B/C/D=1-753. DR PDB; 5BV2; X-ray; 1.53 A; P/Q/R/S=1-753. DR PDB; 6BY0; X-ray; 2.93 A; A/B/C/D=1-753. DR PDB; 6ZTV; X-ray; 1.78 A; A/B/C/D=1-753. DR PDB; 6ZTW; X-ray; 1.84 A; A/B/C/D/E/F/G/H=1-753. DR PDB; 6ZTX; X-ray; 1.30 A; A/B/C/D=1-753. DR AlphaFoldDB; P21179; -. DR MDposit; P21179; -. DR SMR; P21179; -. DR BioGRID; 4263059; 44. DR BioGRID; 850594; 3. DR DIP; DIP-10052N; -. DR FunCoup; P21179; 699. DR IntAct; P21179; 11. DR STRING; 511145.b1732; -. DR PeroxiBase; 5321; EcoKat05. DR jPOST; P21179; -. DR PaxDb; 511145-b1732; -. DR EnsemblBacteria; AAT48137; AAT48137; b1732. DR GeneID; 946234; -. DR KEGG; ecj:JW1721; -. DR KEGG; eco:b1732; -. DR KEGG; ecoc:C3026_09900; -. DR PATRIC; fig|1411691.4.peg.524; -. DR EchoBASE; EB0504; -. DR eggNOG; COG0753; Bacteria. DR HOGENOM; CLU_010645_3_0_6; -. DR InParanoid; P21179; -. DR OMA; AADHHYE; -. DR OrthoDB; 9761719at2; -. DR PhylomeDB; P21179; -. DR BioCyc; EcoCyc:HYDROPEROXIDII-MONOMER; -. DR BioCyc; MetaCyc:HYDROPEROXIDII-MONOMER; -. DR SABIO-RK; P21179; -. DR EvolutionaryTrace; P21179; -. DR PRO; PR:P21179; -. DR Proteomes; UP000000625; Chromosome. DR AbasyAtlas; P21179; -. DR GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki. DR GO; GO:0005829; C:cytosol; HDA:UniProtKB. DR GO; GO:0004096; F:catalase activity; IDA:EcoCyc. DR GO; GO:0020037; F:heme binding; IDA:EcoliWiki. DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc. DR GO; GO:0005506; F:iron ion binding; IDA:EcoliWiki. DR GO; GO:0006974; P:DNA damage response; IEP:EcoliWiki. DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IMP:EcoliWiki. DR GO; GO:0006972; P:hyperosmotic response; IEP:EcoCyc. DR GO; GO:0006979; P:response to oxidative stress; IMP:EcoliWiki. DR CDD; cd08155; catalase_clade_2; 1. DR CDD; cd03132; GATase1_catalase; 1. DR FunFam; 2.40.180.10:FF:000003; Catalase; 1. DR FunFam; 1.20.1370.20:FF:000001; Catalase HPII; 1. DR FunFam; 3.40.50.880:FF:000049; Catalase HPII; 1. DR Gene3D; 1.20.1370.20; -; 1. DR Gene3D; 3.40.50.880; -; 1. DR Gene3D; 2.40.180.10; Catalase core domain; 1. DR InterPro; IPR018028; Catalase. DR InterPro; IPR024708; Catalase_AS. DR InterPro; IPR024712; Catalase_clade2. DR InterPro; IPR043156; Catalase_clade2_helical. DR InterPro; IPR011614; Catalase_core. DR InterPro; IPR002226; Catalase_haem_BS. DR InterPro; IPR010582; Catalase_immune_responsive. DR InterPro; IPR041399; Catalase_large_C. DR InterPro; IPR020835; Catalase_sf. DR InterPro; IPR029062; Class_I_gatase-like. DR NCBIfam; NF008422; katE; 1. DR PANTHER; PTHR42821; CATALASE; 1. DR PANTHER; PTHR42821:SF1; CATALASE-B; 1. DR Pfam; PF00199; Catalase; 1. DR Pfam; PF06628; Catalase-rel; 1. DR Pfam; PF18011; Catalase_C; 1. DR PIRSF; PIRSF038927; Catalase_clade2; 1. DR PRINTS; PR00067; CATALASE. DR SMART; SM01060; Catalase; 1. DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1. DR SUPFAM; SSF56634; Heme-dependent catalase-like; 1. DR PROSITE; PS00437; CATALASE_1; 1. DR PROSITE; PS00438; CATALASE_2; 1. DR PROSITE; PS51402; CATALASE_3; 1. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Direct protein sequencing; Heme; KW Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase; KW Reference proteome. FT CHAIN 1..753 FT /note="Catalase HPII" FT /id="PRO_0000084971" FT REGION 1..61 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 459..493 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 128 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10013" FT ACT_SITE 201 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10013" FT BINDING 415 FT /ligand="heme" FT /ligand_id="ChEBI:CHEBI:30413" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT CROSSLNK 392..415 FT /note="3'-histidyl-3-tyrosine (His-Tyr)" FT HELIX 19..22 FT /evidence="ECO:0007829|PDB:5BV2" FT STRAND 32..34 FT /evidence="ECO:0007829|PDB:1QWS" FT TURN 45..47 FT /evidence="ECO:0007829|PDB:6ZTW" FT HELIX 53..56 FT /evidence="ECO:0007829|PDB:6ZTX" FT HELIX 63..67 FT /evidence="ECO:0007829|PDB:6ZTX" FT HELIX 69..71 FT /evidence="ECO:0007829|PDB:6ZTX" FT STRAND 87..89 FT /evidence="ECO:0007829|PDB:6ZTX" FT STRAND 95..98 FT /evidence="ECO:0007829|PDB:6ZTX" FT HELIX 108..118 FT /evidence="ECO:0007829|PDB:6ZTX" FT HELIX 121..125 FT /evidence="ECO:0007829|PDB:1IPH" FT STRAND 126..128 FT /evidence="ECO:0007829|PDB:1IPH" FT STRAND 130..142 FT /evidence="ECO:0007829|PDB:6ZTX" FT TURN 145..147 FT /evidence="ECO:0007829|PDB:6ZTX" FT HELIX 151..153 FT /evidence="ECO:0007829|PDB:6ZTX" FT STRAND 160..167 FT /evidence="ECO:0007829|PDB:6ZTX" FT STRAND 169..171 FT /evidence="ECO:0007829|PDB:6ZTX" FT STRAND 179..181 FT /evidence="ECO:0007829|PDB:6ZTX" FT STRAND 184..191 FT /evidence="ECO:0007829|PDB:6ZTX" FT STRAND 194..205 FT /evidence="ECO:0007829|PDB:6ZTX" FT HELIX 211..213 FT /evidence="ECO:0007829|PDB:6ZTX" FT HELIX 214..221 FT /evidence="ECO:0007829|PDB:6ZTX" FT TURN 225..227 FT /evidence="ECO:0007829|PDB:6ZTX" FT HELIX 237..245 FT /evidence="ECO:0007829|PDB:6ZTX" FT HELIX 247..249 FT /evidence="ECO:0007829|PDB:6ZTX" FT HELIX 250..257 FT /evidence="ECO:0007829|PDB:6ZTX" FT HELIX 259..261 FT /evidence="ECO:0007829|PDB:6ZTX" FT STRAND 262..264 FT /evidence="ECO:0007829|PDB:6ZTX" FT HELIX 266..268 FT /evidence="ECO:0007829|PDB:6ZTX" FT STRAND 277..280 FT /evidence="ECO:0007829|PDB:6ZTX" FT STRAND 286..295 FT /evidence="ECO:0007829|PDB:6ZTX" FT HELIX 304..313 FT /evidence="ECO:0007829|PDB:6ZTX" FT HELIX 317..327 FT /evidence="ECO:0007829|PDB:6ZTX" FT STRAND 333..342 FT /evidence="ECO:0007829|PDB:6ZTX" FT HELIX 343..345 FT /evidence="ECO:0007829|PDB:6ZTX" FT STRAND 349..351 FT /evidence="ECO:0007829|PDB:6ZTX" FT TURN 362..364 FT /evidence="ECO:0007829|PDB:6ZTX" FT STRAND 367..377 FT /evidence="ECO:0007829|PDB:6ZTX" FT HELIX 382..387 FT /evidence="ECO:0007829|PDB:6ZTX" FT HELIX 406..417 FT /evidence="ECO:0007829|PDB:6ZTX" FT HELIX 419..422 FT /evidence="ECO:0007829|PDB:6ZTX" FT STRAND 423..425 FT /evidence="ECO:0007829|PDB:6ZTX" FT HELIX 428..430 FT /evidence="ECO:0007829|PDB:6ZTX" FT HELIX 432..434 FT /evidence="ECO:0007829|PDB:6ZTX" FT STRAND 459..462 FT /evidence="ECO:0007829|PDB:6ZTX" FT TURN 465..468 FT /evidence="ECO:0007829|PDB:6ZTX" FT STRAND 477..479 FT /evidence="ECO:0007829|PDB:6ZTX" FT STRAND 488..495 FT /evidence="ECO:0007829|PDB:6ZTX" FT HELIX 499..501 FT /evidence="ECO:0007829|PDB:6ZTX" FT HELIX 506..514 FT /evidence="ECO:0007829|PDB:6ZTX" FT HELIX 517..532 FT /evidence="ECO:0007829|PDB:6ZTX" FT HELIX 537..548 FT /evidence="ECO:0007829|PDB:6ZTX" FT HELIX 552..561 FT /evidence="ECO:0007829|PDB:6ZTX" FT HELIX 568..571 FT /evidence="ECO:0007829|PDB:6ZTX" FT HELIX 573..578 FT /evidence="ECO:0007829|PDB:6ZTX" FT HELIX 586..588 FT /evidence="ECO:0007829|PDB:6ZTX" FT STRAND 589..593 FT /evidence="ECO:0007829|PDB:6ZTX" FT STRAND 602..606 FT /evidence="ECO:0007829|PDB:6ZTX" FT STRAND 609..611 FT /evidence="ECO:0007829|PDB:1IPH" FT HELIX 613..625 FT /evidence="ECO:0007829|PDB:6ZTX" FT STRAND 629..641 FT /evidence="ECO:0007829|PDB:6ZTX" FT STRAND 647..649 FT /evidence="ECO:0007829|PDB:6ZTX" FT TURN 654..656 FT /evidence="ECO:0007829|PDB:6ZTX" FT HELIX 659..661 FT /evidence="ECO:0007829|PDB:6ZTX" FT STRAND 663..667 FT /evidence="ECO:0007829|PDB:6ZTX" FT HELIX 673..676 FT /evidence="ECO:0007829|PDB:6ZTX" FT HELIX 679..690 FT /evidence="ECO:0007829|PDB:6ZTX" FT STRAND 695..698 FT /evidence="ECO:0007829|PDB:6ZTX" FT HELIX 699..706 FT /evidence="ECO:0007829|PDB:6ZTX" FT TURN 707..709 FT /evidence="ECO:0007829|PDB:6ZTX" FT STRAND 718..724 FT /evidence="ECO:0007829|PDB:6ZTX" FT HELIX 728..737 FT /evidence="ECO:0007829|PDB:6ZTX" FT HELIX 742..744 FT /evidence="ECO:0007829|PDB:6ZTX" FT HELIX 745..748 FT /evidence="ECO:0007829|PDB:6ZTX" FT STRAND 749..751 FT /evidence="ECO:0007829|PDB:1P80" SQ SEQUENCE 753 AA; 84163 MW; 1F034E4866A70FB9 CRC64; MSQHNEKNPH QHQSPLHDSS EAKPGMDSLA PEDGSHRPAA EPTPPGAQPT APGSLKAPDT RNEKLNSLED VRKGSENYAL TTNQGVRIAD DQNSLRAGSR GPTLLEDFIL REKITHFDHE RIPERIVHAR GSAAHGYFQP YKSLSDITKA DFLSDPNKIT PVFVRFSTVQ GGAGSADTVR DIRGFATKFY TEEGIFDLVG NNTPIFFIQD AHKFPDFVHA VKPEPHWAIP QGQSAHDTFW DYVSLQPETL HNVMWAMSDR GIPRSYRTME GFGIHTFRLI NAEGKATFVR FHWKPLAGKA SLVWDEAQKL TGRDPDFHRR ELWEAIEAGD FPEYELGFQL IPEEDEFKFD FDLLDPTKLI PEELVPVQRV GKMVLNRNPD NFFAENEQAA FHPGHIVPGL DFTNDPLLQG RLFSYTDTQI SRLGGPNFHE IPINRPTCPY HNFQRDGMHR MGIDTNPANY EPNSINDNWP RETPPGPKRG GFESYQERVE GNKVRERSPS FGEYYSHPRL FWLSQTPFEQ RHIVDGFSFE LSKVVRPYIR ERVVDQLAHI DLTLAQAVAK NLGIELTDDQ LNITPPPDVN GLKKDPSLSL YAIPDGDVKG RVVAILLNDE VRSADLLAIL KALKAKGVHA KLLYSRMGEV TADDGTVLPI AATFAGAPSL TVDAVIVPCG NIADIADNGD ANYYLMEAYK HLKPIALAGD ARKFKATIKI ADQGEEGIVE ADSADGSFMD ELLTLMAAHR VWSRIPKIDK IPA //