URE1_HELPY
ID URE1_HELPY Reviewed; 569 AA.
AC P69996; P14917; Q9R3B3;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Urease subunit beta {ECO:0000255|HAMAP-Rule:MF_01953};
DE EC=3.5.1.5 {ECO:0000255|HAMAP-Rule:MF_01953};
DE AltName: Full=Urea amidohydrolase subunit beta {ECO:0000255|HAMAP-Rule:MF_01953};
GN Name=ureB {ECO:0000255|HAMAP-Rule:MF_01953}; Synonyms=hpuB;
GN OrderedLocusNames=HP_0072;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=85P;
RX PubMed=2001995; DOI=10.1128/jb.173.6.1920-1931.1991;
RA Labigne A., Cussac V., Courcoux P.;
RT "Shuttle cloning and nucleotide sequences of Helicobacter pylori genes
RT responsible for urease activity.";
RL J. Bacteriol. 173:1920-1931(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CPM630;
RX PubMed=2326167; DOI=10.1093/nar/18.2.362;
RA Clayton C.L., Pallen M.J., Kleanthous H., Wren B.W., Tabaqchali S.;
RT "Nucleotide sequence of two genes from Helicobacter pylori encoding for
RT urease subunits.";
RL Nucleic Acids Res. 18:362-362(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
RN [4]
RP PROTEIN SEQUENCE OF 1-30, CATALYTIC ACTIVITY, AND KINETIC PARAMETERS.
RX PubMed=1857197; DOI=10.1016/0882-4010(91)90062-f;
RA Evans D.J. Jr., Evans D.G., Kirkpatrick S.S., Graham D.Y.;
RT "Characterization of the Helicobacter pylori urease and purification of its
RT subunits.";
RL Microb. Pathog. 10:15-26(1991).
RN [5]
RP PROTEIN SEQUENCE OF 1-20, CATALYTIC ACTIVITY, KINETIC PARAMETERS, AND
RP INTERACTION WITH UREA.
RX PubMed=2188975; DOI=10.1016/s0021-9258(19)38872-6;
RA Dunn B.E., Campbell G.P., Perez-Perez G.I., Blaser M.J.;
RT "Purification and characterization of urease from Helicobacter pylori.";
RL J. Biol. Chem. 265:9464-9469(1990).
RN [6]
RP PROTEIN SEQUENCE OF 1-15.
RX PubMed=2318539; DOI=10.1128/iai.58.4.992-998.1990;
RA Hu L.-T., Mobley H.L.T.;
RT "Purification and N-terminal analysis of urease from Helicobacter pylori.";
RL Infect. Immun. 58:992-998(1990).
RN [7]
RP PROTEIN SEQUENCE OF 1-12.
RC STRAIN=ATCC 43504 / NCTC 11637 / JCM 7653 / RPH 13487;
RX PubMed=1452359; DOI=10.1128/iai.60.12.5259-5266.1992;
RA Turbett G.R., Hoej P.B., Horne R., Mee B.J.;
RT "Purification and characterization of the urease enzymes of Helicobacter
RT species from humans and animals.";
RL Infect. Immun. 60:5259-5266(1992).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 565-569, AND DISRUPTION PHENOTYPE.
RC STRAIN=85P;
RX PubMed=1313413; DOI=10.1128/jb.174.8.2466-2473.1992;
RA Cussac V., Ferrero R.L., Labigne A.;
RT "Expression of Helicobacter pylori urease genes in Escherichia coli grown
RT under nitrogen-limiting conditions.";
RL J. Bacteriol. 174:2466-2473(1992).
RN [9]
RP CATALYTIC ACTIVITY.
RX PubMed=1612735; DOI=10.1128/iai.60.7.2657-2666.1992;
RA Hu L.-T., Foxall P.A., Russell R., Mobley H.L.T.;
RT "Purification of recombinant Helicobacter pylori urease apoenzyme encoded
RT by ureA and ureB.";
RL Infect. Immun. 60:2657-2666(1992).
RN [10]
RP FUNCTION, AND ROLE IN VIRULENCE.
RX PubMed=8039935; DOI=10.1128/iai.62.8.3586-3589.1994;
RA Tsuda M., Karita M., Morshed M.G., Okita K., Nakazawa T.;
RT "A urease-negative mutant of Helicobacter pylori constructed by allelic
RT exchange mutagenesis lacks the ability to colonize the nude mouse
RT stomach.";
RL Infect. Immun. 62:3586-3589(1994).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=8641799; DOI=10.1128/iai.64.3.905-912.1996;
RA Phadnis S.H., Parlow M.H., Levy M., Ilver D., Caulkins C.M., Connors J.B.,
RA Dunn B.E.;
RT "Surface localization of Helicobacter pylori urease and a heat shock
RT protein homolog requires bacterial autolysis.";
RL Infect. Immun. 64:905-912(1996).
RN [12]
RP INDUCTION.
RX PubMed=11447165; DOI=10.1128/iai.69.8.4891-4897.2001;
RA van Vliet A.H.M., Kuipers E.J., Waidner B., Davies B.J., de Vries N.,
RA Penn C.W., Vandenbroucke-Grauls C.M.J.E., Kist M., Bereswill S.,
RA Kusters J.G.;
RT "Nickel-responsive induction of urease expression in Helicobacter pylori is
RT mediated at the transcriptional level.";
RL Infect. Immun. 69:4891-4897(2001).
RN [13]
RP INDUCTION.
RX PubMed=16339943; DOI=10.1099/mic.0.28188-0;
RA Belzer C., Stoof J., Beckwith C.S., Kuipers E.J., Kusters J.G.,
RA van Vliet A.H.M.;
RT "Differential regulation of urease activity in Helicobacter hepaticus and
RT Helicobacter pylori.";
RL Microbiology 151:3989-3995(2005).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH NICKEL IONS, SUBUNIT
RP STRUCTURE, AND CARBOXYLATION AT LYS-219.
RX PubMed=11373617; DOI=10.1038/88563;
RA Ha N.-C., Oh S.-T., Sung J.Y., Cha K.A., Lee M.H., Oh B.-H.;
RT "Supramolecular assembly and acid resistance of Helicobacter pylori
RT urease.";
RL Nat. Struct. Biol. 8:505-509(2001).
CC -!- FUNCTION: Ammonia produced by ureolysis increases the gastric pH
CC thereby providing an environment permissive for colonization of the
CC stomach. {ECO:0000269|PubMed:8039935}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + H2O + urea = CO2 + 2 NH4(+); Xref=Rhea:RHEA:20557,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16199,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:28938; EC=3.5.1.5;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01953,
CC ECO:0000269|PubMed:1612735, ECO:0000269|PubMed:1857197,
CC ECO:0000269|PubMed:2188975};
CC -!- COFACTOR:
CC Name=Ni cation; Xref=ChEBI:CHEBI:25516;
CC Note=Binds 2 nickel ions per subunit.;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.48 mM for urea {ECO:0000269|PubMed:1857197,
CC ECO:0000269|PubMed:2188975};
CC Vmax=1.1 mmol/min/mg enzyme {ECO:0000269|PubMed:1857197,
CC ECO:0000269|PubMed:2188975};
CC pH dependence:
CC Optimum pH is 8.0. Active from pH 4.0 to 10.0. In unbuffered
CC solutions, the dodecameric complex is active at pH3.0.;
CC -!- PATHWAY: Nitrogen metabolism; urea degradation; CO(2) and NH(3) from
CC urea (urease route): step 1/1. {ECO:0000255|HAMAP-Rule:MF_01953}.
CC -!- SUBUNIT: Heterohexamer of 3 UreA (alpha) and 3 UreB (beta) subunits.
CC Four heterohexamers assemble to form a 16 nm dodecameric complex.
CC {ECO:0000255|HAMAP-Rule:MF_01953, ECO:0000269|PubMed:11373617}.
CC -!- INTERACTION:
CC P69996; P14916: ureA; NbExp=2; IntAct=EBI-7566591, EBI-7737170;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01953,
CC ECO:0000269|PubMed:8641799}. Note=Also associates with the outer
CC membrane upon autolysis of neighboring bacteria.
CC -!- INDUCTION: By nickel ions. {ECO:0000269|PubMed:11447165,
CC ECO:0000269|PubMed:16339943}.
CC -!- PTM: Carboxylation allows a single lysine to coordinate two nickel
CC ions. {ECO:0000255|HAMAP-Rule:MF_01953, ECO:0000269|PubMed:11373617}.
CC -!- DISRUPTION PHENOTYPE: Cells do not express urease.
CC {ECO:0000269|PubMed:1313413}.
CC -!- MISCELLANEOUS: The novel dodecameric structure of the enzyme may allow
CC it to remain active at the cell surface at acidic gastric pH. Within
CC this dodecameric structure the 12 active sites are clustered within the
CC interior of the proteinaceous shell. This may allow a high local
CC concentration of ammonia within the enzyme which may protect the
CC nickel-chelating groups from protonation.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Urease alpha subunit family. {ECO:0000255|HAMAP-Rule:MF_01953}.
CC -!- CAUTION: The orthologous protein is known as the alpha subunit (UreC)
CC in most other bacteria. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Going unnoticed - Issue 95
CC of June 2008;
CC URL="https://web.expasy.org/spotlight/back_issues/095";
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DR EMBL; M60398; AAA25021.1; -; Genomic_DNA.
DR EMBL; X17079; CAA34933.1; -; Genomic_DNA.
DR EMBL; AE000511; AAD07143.1; -; Genomic_DNA.
DR EMBL; M84338; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; B38537; URKCBP.
DR RefSeq; NP_206872.1; NC_000915.1.
DR RefSeq; WP_000724295.1; NC_018939.1.
DR PDB; 1E9Y; X-ray; 3.00 A; B=1-569.
DR PDB; 1E9Z; X-ray; 3.00 A; B=1-569.
DR PDB; 6QSU; EM; 2.40 A; B/D/F/H/J/L/N/P/R/T/V/X=1-569.
DR PDB; 6ZJA; EM; 2.00 A; B/D/F/H/J/L/N/P/R/T/V/X=1-569.
DR PDBsum; 1E9Y; -.
DR PDBsum; 1E9Z; -.
DR PDBsum; 6QSU; -.
DR PDBsum; 6ZJA; -.
DR AlphaFoldDB; P69996; -.
DR SMR; P69996; -.
DR IntAct; P69996; 13.
DR MINT; P69996; -.
DR STRING; 85962.C694_00350; -.
DR BindingDB; P69996; -.
DR ChEMBL; CHEMBL3885651; -.
DR MEROPS; M38.982; -.
DR PaxDb; P69996; -.
DR ABCD; P69996; 1 sequenced antibody.
DR EnsemblBacteria; AAD07143; AAD07143; HP_0072.
DR KEGG; hpy:HP_0072; -.
DR PATRIC; fig|85962.47.peg.76; -.
DR eggNOG; COG0804; Bacteria.
DR OMA; GFDSHIH; -.
DR PhylomeDB; P69996; -.
DR BioCyc; MetaCyc:HP_RS00365-MON; -.
DR SABIO-RK; P69996; -.
DR UniPathway; UPA00258; UER00370.
DR EvolutionaryTrace; P69996; -.
DR PHI-base; PHI:3145; -.
DR Proteomes; UP000000429; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016151; F:nickel cation binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009039; F:urease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0043419; P:urea catabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00375; Urease_alpha; 1.
DR Gene3D; 2.30.40.10; -; 1.
DR HAMAP; MF_01953; Urease_alpha; 1.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR InterPro; IPR011612; Urease_alpha_N_dom.
DR InterPro; IPR017950; Urease_AS.
DR InterPro; IPR005848; Urease_asu.
DR InterPro; IPR017951; Urease_asu_c.
DR InterPro; IPR029754; Urease_Ni-bd.
DR Pfam; PF01979; Amidohydro_1; 1.
DR Pfam; PF00449; Urease_alpha; 1.
DR PRINTS; PR01752; UREASE.
DR SUPFAM; SSF51338; SSF51338; 2.
DR SUPFAM; SSF51556; SSF51556; 1.
DR TIGRFAMs; TIGR01792; urease_alph; 1.
DR PROSITE; PS01120; UREASE_1; 1.
DR PROSITE; PS00145; UREASE_2; 1.
DR PROSITE; PS51368; UREASE_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Hydrolase;
KW Metal-binding; Nickel; Reference proteome; Virulence.
FT CHAIN 1..569
FT /note="Urease subunit beta"
FT /id="PRO_0000067533"
FT DOMAIN 131..569
FT /note="Urease"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT ACT_SITE 322
FT /note="Proton donor"
FT /evidence="ECO:0000305"
FT BINDING 136
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT BINDING 138
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT BINDING 219
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /note="via carbamate group"
FT BINDING 219
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT /note="via carbamate group"
FT BINDING 221
FT /ligand="substrate"
FT /evidence="ECO:0000305"
FT BINDING 248
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT BINDING 274
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT BINDING 362
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT MOD_RES 219
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953,
FT ECO:0000269|PubMed:11373617"
FT CONFLICT 10
FT /note="V -> A (in Ref. 2; CAA34933)"
FT /evidence="ECO:0000305"
FT CONFLICT 19
FT /note="D -> A (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 22
FT /note="R -> C (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 27
FT /note="D -> C (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 104
FT /note="M -> T (in Ref. 2; CAA34933)"
FT /evidence="ECO:0000305"
FT CONFLICT 181
FT /note="W -> F (in Ref. 2; CAA34933)"
FT /evidence="ECO:0000305"
FT CONFLICT 193
FT /note="L -> F (in Ref. 2; CAA34933)"
FT /evidence="ECO:0000305"
FT CONFLICT 218
FT /note="F -> L (in Ref. 2; CAA34933)"
FT /evidence="ECO:0000305"
FT CONFLICT 273
FT /note="F -> Y (in Ref. 2; CAA34933)"
FT /evidence="ECO:0000305"
FT CONFLICT 540
FT /note="P -> S (in Ref. 2; CAA34933)"
FT /evidence="ECO:0000305"
FT CONFLICT 554..569
FT /note="SKPANKVSLAQLFSIF -> LNQPIK (in Ref. 2; CAA34933)"
FT /evidence="ECO:0000305"
FT STRAND 2..4
FT /evidence="ECO:0007829|PDB:6ZJA"
FT HELIX 6..13
FT /evidence="ECO:0007829|PDB:6ZJA"
FT STRAND 20..22
FT /evidence="ECO:0007829|PDB:6ZJA"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:6ZJA"
FT STRAND 49..53
FT /evidence="ECO:0007829|PDB:6ZJA"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:6ZJA"
FT STRAND 67..77
FT /evidence="ECO:0007829|PDB:6ZJA"
FT STRAND 80..89
FT /evidence="ECO:0007829|PDB:6ZJA"
FT STRAND 92..97
FT /evidence="ECO:0007829|PDB:6ZJA"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:6ZJA"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:1E9Y"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:6ZJA"
FT STRAND 119..122
FT /evidence="ECO:0007829|PDB:6ZJA"
FT STRAND 127..130
FT /evidence="ECO:0007829|PDB:6ZJA"
FT STRAND 132..138
FT /evidence="ECO:0007829|PDB:6ZJA"
FT HELIX 144..151
FT /evidence="ECO:0007829|PDB:6ZJA"
FT STRAND 153..159
FT /evidence="ECO:0007829|PDB:6ZJA"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:6ZJA"
FT HELIX 165..169
FT /evidence="ECO:0007829|PDB:6ZJA"
FT HELIX 175..185
FT /evidence="ECO:0007829|PDB:6ZJA"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:6ZJA"
FT STRAND 190..195
FT /evidence="ECO:0007829|PDB:6ZJA"
FT HELIX 204..212
FT /evidence="ECO:0007829|PDB:6ZJA"
FT STRAND 217..220
FT /evidence="ECO:0007829|PDB:6ZJA"
FT HELIX 222..224
FT /evidence="ECO:0007829|PDB:6ZJA"
FT HELIX 228..241
FT /evidence="ECO:0007829|PDB:6ZJA"
FT STRAND 244..247
FT /evidence="ECO:0007829|PDB:6ZJA"
FT HELIX 258..265
FT /evidence="ECO:0007829|PDB:6ZJA"
FT STRAND 270..274
FT /evidence="ECO:0007829|PDB:6ZJA"
FT TURN 283..285
FT /evidence="ECO:0007829|PDB:6ZJA"
FT HELIX 286..291
FT /evidence="ECO:0007829|PDB:6ZJA"
FT STRAND 292..300
FT /evidence="ECO:0007829|PDB:6ZJA"
FT HELIX 301..303
FT /evidence="ECO:0007829|PDB:6ZJA"
FT HELIX 310..321
FT /evidence="ECO:0007829|PDB:6ZJA"
FT HELIX 329..338
FT /evidence="ECO:0007829|PDB:6ZJA"
FT HELIX 341..352
FT /evidence="ECO:0007829|PDB:6ZJA"
FT STRAND 358..360
FT /evidence="ECO:0007829|PDB:6ZJA"
FT STRAND 365..367
FT /evidence="ECO:0007829|PDB:6ZJA"
FT HELIX 372..387
FT /evidence="ECO:0007829|PDB:6ZJA"
FT STRAND 395..397
FT /evidence="ECO:0007829|PDB:6ZJA"
FT HELIX 399..407
FT /evidence="ECO:0007829|PDB:6ZJA"
FT TURN 408..410
FT /evidence="ECO:0007829|PDB:6ZJA"
FT HELIX 411..416
FT /evidence="ECO:0007829|PDB:6ZJA"
FT TURN 420..422
FT /evidence="ECO:0007829|PDB:6ZJA"
FT STRAND 423..425
FT /evidence="ECO:0007829|PDB:6ZJA"
FT STRAND 434..437
FT /evidence="ECO:0007829|PDB:6ZJA"
FT HELIX 439..441
FT /evidence="ECO:0007829|PDB:6ZJA"
FT TURN 442..444
FT /evidence="ECO:0007829|PDB:6ZJA"
FT STRAND 447..451
FT /evidence="ECO:0007829|PDB:6ZJA"
FT STRAND 454..460
FT /evidence="ECO:0007829|PDB:6ZJA"
FT STRAND 465..468
FT /evidence="ECO:0007829|PDB:6ZJA"
FT STRAND 470..472
FT /evidence="ECO:0007829|PDB:1E9Z"
FT STRAND 474..477
FT /evidence="ECO:0007829|PDB:6ZJA"
FT HELIX 479..481
FT /evidence="ECO:0007829|PDB:6ZJA"
FT HELIX 485..488
FT /evidence="ECO:0007829|PDB:6ZJA"
FT STRAND 491..494
FT /evidence="ECO:0007829|PDB:6ZJA"
FT HELIX 496..500
FT /evidence="ECO:0007829|PDB:6ZJA"
FT HELIX 503..507
FT /evidence="ECO:0007829|PDB:6ZJA"
FT STRAND 511..515
FT /evidence="ECO:0007829|PDB:6ZJA"
FT HELIX 524..526
FT /evidence="ECO:0007829|PDB:6ZJA"
FT STRAND 527..529
FT /evidence="ECO:0007829|PDB:6QSU"
FT STRAND 536..538
FT /evidence="ECO:0007829|PDB:6ZJA"
FT TURN 540..542
FT /evidence="ECO:0007829|PDB:6ZJA"
FT STRAND 545..547
FT /evidence="ECO:0007829|PDB:6ZJA"
FT STRAND 561..563
FT /evidence="ECO:0007829|PDB:6ZJA"
FT TURN 564..566
FT /evidence="ECO:0007829|PDB:6ZJA"
SQ SEQUENCE 569 AA; 61684 MW; 4C8A6BC6C8295584 CRC64;
MKKISRKEYV SMYGPTTGDK VRLGDTDLIA EVEHDYTIYG EELKFGGGKT LREGMSQSNN
PSKEELDLII TNALIVDYTG IYKADIGIKD GKIAGIGKGG NKDMQDGVKN NLSVGPATEA
LAGEGLIVTA GGIDTHIHFI SPQQIPTAFA SGVTTMIGGG TGPADGTNAT TITPGRRNLK
WMLRAAEEYS MNLGFLAKGN ASNDASLADQ IEAGAIGFKI HEDWGTTPSA INHALDVADK
YDVQVAIHTD TLNEAGCVED TMAAIAGRTM HTFHTEGAGG GHAPDIIKVA GEHNILPAST
NPTIPFTVNT EAEHMDMLMV CHHLDKSIKE DVQFADSRIR PQTIAAEDTL HDMGIFSITS
SDSQAMGRVG EVITRTWQTA DKNKKEFGRL KEEKGDNDNF RIKRYLSKYT INPAIAHGIS
EYVGSVEVGK VADLVLWSPA FFGVKPNMII KGGFIALSQM GDANASIPTP QPVYYREMFA
HHGKAKYDAN ITFVSQAAYD KGIKEELGLE RQVLPVKNCR NITKKDMQFN DTTAHIEVNP
ETYHVFVDGK EVTSKPANKV SLAQLFSIF
