CATE_ECOLI
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 03-AUG-2022, entry version 196.
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; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC 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 (2.8 ANGSTROMS).
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 (2.3 ANGSTROMS).
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 (1.89 ANGSTROMS).
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 = 2 H2O + O2; 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}.
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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_LN832404.1.
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; 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 PDBsum; 1CF9; -.
DR PDBsum; 1GG9; -.
DR PDBsum; 1GGE; -.
DR PDBsum; 1GGF; -.
DR PDBsum; 1GGH; -.
DR PDBsum; 1GGJ; -.
DR PDBsum; 1GGK; -.
DR PDBsum; 1IPH; -.
DR PDBsum; 1P7Y; -.
DR PDBsum; 1P7Z; -.
DR PDBsum; 1P80; -.
DR PDBsum; 1P81; -.
DR PDBsum; 1QF7; -.
DR PDBsum; 1QWS; -.
DR PDBsum; 1YE9; -.
DR PDBsum; 3P9P; -.
DR PDBsum; 3P9Q; -.
DR PDBsum; 3P9R; -.
DR PDBsum; 3P9S; -.
DR PDBsum; 3PQ2; -.
DR PDBsum; 3PQ3; -.
DR PDBsum; 3PQ4; -.
DR PDBsum; 3PQ5; -.
DR PDBsum; 3PQ6; -.
DR PDBsum; 3PQ7; -.
DR PDBsum; 3PQ8; -.
DR PDBsum; 3TTT; -.
DR PDBsum; 3TTU; -.
DR PDBsum; 3TTV; -.
DR PDBsum; 3TTW; -.
DR PDBsum; 3TTX; -.
DR PDBsum; 3VU3; -.
DR PDBsum; 4BFL; -.
DR PDBsum; 4ENP; -.
DR PDBsum; 4ENQ; -.
DR PDBsum; 4ENR; -.
DR PDBsum; 4ENS; -.
DR PDBsum; 4ENT; -.
DR PDBsum; 4ENU; -.
DR PDBsum; 4ENV; -.
DR PDBsum; 4ENW; -.
DR PDBsum; 5BV2; -.
DR PDBsum; 6BY0; -.
DR PDBsum; 6ZTV; -.
DR PDBsum; 6ZTW; -.
DR PDBsum; 6ZTX; -.
DR AlphaFoldDB; P21179; -.
DR SMR; P21179; -.
DR BioGRID; 4263059; 36.
DR BioGRID; 850594; 3.
DR DIP; DIP-10052N; -.
DR IntAct; P21179; 11.
DR STRING; 511145.b1732; -.
DR PeroxiBase; 5321; EcoKat05.
DR SWISS-2DPAGE; P21179; -.
DR jPOST; P21179; -.
DR PaxDb; P21179; -.
DR PRIDE; P21179; -.
DR EnsemblBacteria; AAT48137; AAT48137; b1732.
DR EnsemblBacteria; BAA15513; BAA15513; BAA15513.
DR GeneID; 946234; -.
DR KEGG; ecj:JW1721; -.
DR KEGG; eco:b1732; -.
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; VMWQMSD; -.
DR PhylomeDB; P21179; -.
DR BioCyc; EcoCyc:HYDROPEROXIDII-MON; -.
DR BioCyc; MetaCyc:HYDROPEROXIDII-MON; -.
DR SABIO-RK; P21179; -.
DR EvolutionaryTrace; P21179; -.
DR PRO; PR:P21179; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
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:cellular response to DNA damage stimulus; 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; cd03132; GATase1_catalase; 1.
DR Gene3D; 1.20.1370.20; -; 1.
DR Gene3D; 3.40.50.880; -; 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 PANTHER; PTHR42821; PTHR42821; 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; SSF52317; 1.
DR SUPFAM; SSF56634; SSF56634; 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 COMPBIAS 1..17
FT /note="Basic and acidic residues"
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 68..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 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 368..377
FT /evidence="ECO:0007829|PDB:6ZTX"
FT HELIX 382..385
FT /evidence="ECO:0007829|PDB:6ZTX"
FT TURN 386..388
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 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
