URE1_SPOPA
ID URE1_SPOPA Reviewed; 570 AA.
AC P41020; A0A0H3YL32;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 02-JUN-2021, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Urease subunit alpha {ECO:0000255|HAMAP-Rule:MF_01953};
DE EC=3.5.1.5 {ECO:0000255|HAMAP-Rule:MF_01953, ECO:0000269|PubMed:30969470};
DE AltName: Full=Urea amidohydrolase subunit alpha {ECO:0000255|HAMAP-Rule:MF_01953};
GN Name=ureC {ECO:0000255|HAMAP-Rule:MF_01953}; ORFNames=NCTC4822_02163;
OS Sporosarcina pasteurii (Bacillus pasteurii).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Planococcaceae; Sporosarcina.
OX NCBI_TaxID=1474;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 11859 / DSM 33 / NCIB 8841 / NCTC 4822;
RA Moersdorf G., Weinmann P., Kaltwasser H.;
RT "Nucleotide sequence of three genes on a urease encoding DNA-fragment from
RT Bacillus pasteurii.";
RL Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 11859 / DSM 33 / NCIB 8841 / NCTC 4822;
RA Mazzei L., Musiani F., Zambelli B., Ciurli S.;
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11859 / DSM 33 / NCIB 8841 / NCTC 4822;
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 498-570.
RC STRAIN=ATCC 11859 / DSM 33 / NCIB 8841 / NCTC 4822;
RA You J.-H., Kim J.-G., Song B.-H., Lee M.-H., Kim S.-D.;
RT "Genetic organization and nucleotide sequence of the ure gene cluster in
RT Bacillus pasteurii.";
RL Mol. Cells 5:359-369(1995).
RN [5] {ECO:0007744|PDB:1UBP}
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH UREA; UREB; NICKEL
RP IONS AND BETA-MERCAPTOETHANOL, AND CARBOXYLATION AT LYS-220.
RC STRAIN=ATCC 11859 / DSM 33 / NCIB 8841 / NCTC 4822;
RX DOI=10.1007/s007750050231;
RA Benini S., Rypniewski W.R., Wilson K.S., Ciurli S., Mangani S.;
RT "The complex of Bacillus pasteurii urease with beta-mercaptoethanol from X-
RT ray data at 1.65-A resolution.";
RL J. Biol. Inorg. Chem. 3:268-273(1998).
RN [6] {ECO:0007744|PDB:2UBP, ECO:0007744|PDB:3UBP}
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH UREA; UREB; NICKEL
RP IONS AND DIAMIDOPHOSPHATE, AND CARBOXYLATION AT LYS-220.
RC STRAIN=ATCC 11859 / DSM 33 / NCIB 8841 / NCTC 4822;
RX PubMed=10368287; DOI=10.1016/s0969-2126(99)80026-4;
RA Benini S., Rypniewski W.R., Wilson K.S., Miletti S., Ciurli S., Mangani S.;
RT "A new proposal for urease mechanism based on the crystal structures of the
RT native and inhibited enzyme from Bacillus pasteurii: why urea hydrolysis
RT costs two nickels.";
RL Structure 7:205-216(1999).
RN [7] {ECO:0007744|PDB:4UBP}
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEX WITH UREA; UREB; NICKEL
RP IONS AND ACETOHYDROXAMIC ACID, AND CARBOXYLATION AT LYS-220.
RC STRAIN=ATCC 11859 / DSM 33 / NCIB 8841 / NCTC 4822;
RX PubMed=10766443; DOI=10.1007/s007750050014;
RA Benini S., Rypniewski W.R., Wilson K.S., Miletti S., Ciurli S., Mangani S.;
RT "The complex of Bacillus pasteurii urease with acetohydroxamate anion from
RT X-ray data at 1.55 A resolution.";
RL J. Biol. Inorg. Chem. 5:110-118(2000).
RN [8] {ECO:0007744|PDB:1IE7}
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH UREA; UREB; NICKEL
RP AND PHOSPHATE IONS, AND CARBOXYLATION AT LYS-220.
RC STRAIN=ATCC 11859 / DSM 33 / NCIB 8841 / NCTC 4822;
RX PubMed=11713685; DOI=10.1007/s007750100254;
RA Benini S., Rypniewski W.R., Wilson K.S., Ciurli S., Mangani S.;
RT "Structure-based rationalization of urease inhibition by phosphate: novel
RT insights into the enzyme mechanism.";
RL J. Biol. Inorg. Chem. 6:778-790(2001).
RN [9] {ECO:0007744|PDB:1S3T}
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH UREA; UREB; NICKEL
RP AND BORATE IONS, AND CARBOXYLATION AT LYS-220.
RC STRAIN=ATCC 11859 / DSM 33 / NCIB 8841 / NCTC 4822;
RX PubMed=15038715; DOI=10.1021/ja049618p;
RA Benini S., Rypniewski W.R., Wilson K.S., Mangani S., Ciurli S.;
RT "Molecular details of urease inhibition by boric acid: insights into the
RT catalytic mechanism.";
RL J. Am. Chem. Soc. 126:3714-3715(2004).
RN [10] {ECO:0007744|PDB:6QDY}
RP X-RAY CRYSTALLOGRAPHY (1.42 ANGSTROMS) IN COMPLEX WITH SUBSTRATE; UREA;
RP UREB; NICKEL AND FLUORIDE IONS, CATALYTIC ACTIVITY, REACTION MECHANISM,
RP ACTIVITY REGULATION, AND CARBOXYLATION AT LYS-220.
RX PubMed=30969470; DOI=10.1002/anie.201903565;
RA Mazzei L., Cianci M., Benini S., Ciurli S.;
RT "The Structure of the Elusive Urease-Urea Complex Unveils the Mechanism of
RT a Paradigmatic Nickel-Dependent Enzyme.";
RL Angew. Chem. Int. Ed. Engl. 58:7415-7419(2019).
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:30969470};
CC -!- COFACTOR:
CC Name=Ni cation; Xref=ChEBI:CHEBI:25516;
CC Note=Binds 2 nickel ions per subunit. {ECO:0000255|HAMAP-Rule:MF_01953,
CC ECO:0000269|PubMed:10368287, ECO:0000269|PubMed:10766443,
CC ECO:0000269|PubMed:11713685, ECO:0000269|PubMed:15038715,
CC ECO:0000269|PubMed:30969470, ECO:0000269|Ref.5};
CC -!- ACTIVITY REGULATION: Inhibited by fluoride.
CC {ECO:0000269|PubMed:30969470}.
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: Heterotrimer of UreA (gamma), UreB (beta) and UreC (alpha)
CC subunits. Three heterotrimers associate to form the active enzyme.
CC {ECO:0000255|HAMAP-Rule:MF_01953, ECO:0000269|PubMed:10368287,
CC ECO:0000269|PubMed:10766443, ECO:0000269|PubMed:11713685,
CC ECO:0000269|PubMed:15038715, ECO:0000269|PubMed:30969470,
CC ECO:0000269|Ref.5}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01953}.
CC -!- PTM: Carboxylation allows a single lysine to coordinate two nickel
CC ions. {ECO:0000269|PubMed:10368287, ECO:0000269|PubMed:10766443,
CC ECO:0000269|PubMed:11713685, ECO:0000269|PubMed:30969470,
CC ECO:0000269|Ref.5}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Urease alpha subunit family. {ECO:0000255|HAMAP-Rule:MF_01953}.
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; X78411; CAA55175.1; -; Genomic_DNA.
DR EMBL; KR133628; AKN22164.1; -; Genomic_DNA.
DR EMBL; UGYZ01000002; SUJ11615.1; -; Genomic_DNA.
DR EMBL; U29368; AAA73986.1; -; Genomic_DNA.
DR PIR; S47104; S47104.
DR PDB; 1IE7; X-ray; 1.85 A; C=1-570.
DR PDB; 1S3T; X-ray; 2.10 A; C=1-570.
DR PDB; 1UBP; X-ray; 1.65 A; C=1-570.
DR PDB; 2UBP; X-ray; 2.00 A; C=1-570.
DR PDB; 3UBP; X-ray; 2.00 A; C=1-570.
DR PDB; 4AC7; X-ray; 1.50 A; C=1-570.
DR PDB; 4CEU; X-ray; 1.58 A; C=1-570.
DR PDB; 4CEX; X-ray; 1.59 A; C=1-570.
DR PDB; 4UBP; X-ray; 1.55 A; C=1-570.
DR PDB; 5A6T; X-ray; 1.65 A; C=1-570.
DR PDB; 5FSD; X-ray; 1.75 A; C=1-570.
DR PDB; 5FSE; X-ray; 2.07 A; C=1-570.
DR PDB; 5OL4; X-ray; 1.28 A; C=1-570.
DR PDB; 6G48; X-ray; 1.91 A; C=1-570.
DR PDB; 6H8J; X-ray; 1.45 A; C=1-570.
DR PDB; 6I9Y; X-ray; 2.14 A; C=1-570.
DR PDB; 6QDY; X-ray; 1.42 A; C=1-570.
DR PDB; 6RKG; X-ray; 1.32 A; C=1-570.
DR PDB; 6RP1; X-ray; 1.49 A; C=1-570.
DR PDB; 6ZNY; X-ray; 1.50 A; CCC=1-570.
DR PDB; 6ZNZ; X-ray; 1.89 A; CCC=1-570.
DR PDB; 6ZO0; X-ray; 2.23 A; CCC=1-570.
DR PDB; 6ZO1; X-ray; 1.61 A; CCC=1-570.
DR PDB; 6ZO2; X-ray; 1.65 A; CCC=1-570.
DR PDB; 6ZO3; X-ray; 1.55 A; CCC=1-570.
DR PDB; 7B58; X-ray; 1.72 A; CCC=1-570.
DR PDB; 7B59; X-ray; 1.63 A; CCC=1-570.
DR PDB; 7B5A; X-ray; 1.97 A; CCC=1-570.
DR PDBsum; 1IE7; -.
DR PDBsum; 1S3T; -.
DR PDBsum; 1UBP; -.
DR PDBsum; 2UBP; -.
DR PDBsum; 3UBP; -.
DR PDBsum; 4AC7; -.
DR PDBsum; 4CEU; -.
DR PDBsum; 4CEX; -.
DR PDBsum; 4UBP; -.
DR PDBsum; 5A6T; -.
DR PDBsum; 5FSD; -.
DR PDBsum; 5FSE; -.
DR PDBsum; 5OL4; -.
DR PDBsum; 6G48; -.
DR PDBsum; 6H8J; -.
DR PDBsum; 6I9Y; -.
DR PDBsum; 6QDY; -.
DR PDBsum; 6RKG; -.
DR PDBsum; 6RP1; -.
DR PDBsum; 6ZNY; -.
DR PDBsum; 6ZNZ; -.
DR PDBsum; 6ZO0; -.
DR PDBsum; 6ZO1; -.
DR PDBsum; 6ZO2; -.
DR PDBsum; 6ZO3; -.
DR PDBsum; 7B58; -.
DR PDBsum; 7B59; -.
DR PDBsum; 7B5A; -.
DR AlphaFoldDB; P41020; -.
DR SMR; P41020; -.
DR BindingDB; P41020; -.
DR DrugBank; DB02899; N-Carboxymethionine.
DR MEROPS; M38.982; -.
DR EnsemblBacteria; SUJ11615; SUJ11615; NCTC4822_02163.
DR BRENDA; 3.5.1.5; 682.
DR UniPathway; UPA00258; UER00370.
DR EvolutionaryTrace; P41020; -.
DR Proteomes; UP000254519; Unassembled WGS sequence.
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; 1.
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; Hydrolase; Metal-binding; Nickel;
KW Reference proteome.
FT CHAIN 1..570
FT /note="Urease subunit alpha"
FT /id="PRO_0000067536"
FT DOMAIN 132..570
FT /note="Urease"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT ACT_SITE 323
FT /note="Proton donor"
FT /evidence="ECO:0000305"
FT BINDING 137
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953,
FT ECO:0000269|PubMed:10368287, ECO:0000269|PubMed:10766443,
FT ECO:0000269|PubMed:11713685, ECO:0000269|PubMed:15038715,
FT ECO:0000269|PubMed:30969470, ECO:0000269|Ref.5"
FT BINDING 139
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953,
FT ECO:0000269|PubMed:10368287, ECO:0000269|PubMed:10766443,
FT ECO:0000269|PubMed:11713685, ECO:0000269|PubMed:15038715,
FT ECO:0000269|PubMed:30969470, ECO:0000269|Ref.5"
FT BINDING 139
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:30969470"
FT BINDING 170
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:30969470"
FT BINDING 220
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /note="via carbamate group"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953,
FT ECO:0000269|PubMed:10368287, ECO:0000269|PubMed:10766443,
FT ECO:0000269|PubMed:11713685, ECO:0000269|PubMed:15038715,
FT ECO:0000269|PubMed:30969470, ECO:0000269|Ref.5"
FT BINDING 220
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT /note="via carbamate group"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953,
FT ECO:0000269|PubMed:10368287, ECO:0000269|PubMed:10766443,
FT ECO:0000269|PubMed:11713685, ECO:0000269|PubMed:15038715,
FT ECO:0000269|PubMed:30969470, ECO:0000269|Ref.5"
FT BINDING 222
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:30969470"
FT BINDING 249
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953,
FT ECO:0000269|PubMed:10368287, ECO:0000269|PubMed:10766443,
FT ECO:0000269|PubMed:11713685, ECO:0000269|PubMed:15038715,
FT ECO:0000269|PubMed:30969470, ECO:0000269|Ref.5"
FT BINDING 249
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:30969470"
FT BINDING 275
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953,
FT ECO:0000269|PubMed:10368287, ECO:0000269|PubMed:10766443,
FT ECO:0000269|PubMed:11713685, ECO:0000269|PubMed:15038715,
FT ECO:0000269|PubMed:30969470, ECO:0000269|Ref.5"
FT BINDING 363
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953,
FT ECO:0000269|PubMed:10368287, ECO:0000269|PubMed:10766443,
FT ECO:0000269|PubMed:11713685, ECO:0000269|PubMed:15038715,
FT ECO:0000269|PubMed:30969470, ECO:0000269|Ref.5"
FT BINDING 366
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:30969470"
FT MOD_RES 220
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953,
FT ECO:0000269|PubMed:10368287, ECO:0000269|PubMed:10766443,
FT ECO:0000269|PubMed:11713685, ECO:0000269|PubMed:15038715,
FT ECO:0000269|PubMed:30969470, ECO:0000269|Ref.5,
FT ECO:0007744|PDB:1IE7, ECO:0007744|PDB:1S3T,
FT ECO:0007744|PDB:1UBP, ECO:0007744|PDB:2UBP,
FT ECO:0007744|PDB:4UBP"
FT CONFLICT 19
FT /note="Q -> R (in Ref. 1; CAA55175)"
FT /evidence="ECO:0000305"
FT CONFLICT 28..29
FT /note="WI -> G (in Ref. 1; CAA55175)"
FT /evidence="ECO:0000305"
FT CONFLICT 35..41
FT /note="TTYGDEA -> YYLGDEV (in Ref. 1; CAA55175)"
FT /evidence="ECO:0000305"
FT CONFLICT 263
FT /note="L -> V (in Ref. 1; CAA55175)"
FT /evidence="ECO:0000305"
FT CONFLICT 403
FT /note="A -> L (in Ref. 1; CAA55175)"
FT /evidence="ECO:0000305"
FT CONFLICT 420
FT /note="I -> M (in Ref. 1; CAA55175)"
FT /evidence="ECO:0000305"
FT CONFLICT 498..502
FT /note="SSIQQ -> ELNSE (in Ref. 4; AAA73986)"
FT /evidence="ECO:0000305"
FT STRAND 2..4
FT /evidence="ECO:0007829|PDB:5OL4"
FT HELIX 5..12
FT /evidence="ECO:0007829|PDB:5OL4"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:5OL4"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:5OL4"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:1UBP"
FT TURN 53..55
FT /evidence="ECO:0007829|PDB:5OL4"
FT TURN 62..65
FT /evidence="ECO:0007829|PDB:5OL4"
FT STRAND 68..78
FT /evidence="ECO:0007829|PDB:5OL4"
FT STRAND 81..90
FT /evidence="ECO:0007829|PDB:5OL4"
FT STRAND 93..98
FT /evidence="ECO:0007829|PDB:5OL4"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:5OL4"
FT STRAND 120..123
FT /evidence="ECO:0007829|PDB:5OL4"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:5OL4"
FT STRAND 133..139
FT /evidence="ECO:0007829|PDB:5OL4"
FT HELIX 145..151
FT /evidence="ECO:0007829|PDB:5OL4"
FT STRAND 154..160
FT /evidence="ECO:0007829|PDB:5OL4"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:5OL4"
FT HELIX 166..170
FT /evidence="ECO:0007829|PDB:5OL4"
FT HELIX 176..187
FT /evidence="ECO:0007829|PDB:5OL4"
FT STRAND 191..199
FT /evidence="ECO:0007829|PDB:5OL4"
FT HELIX 205..214
FT /evidence="ECO:0007829|PDB:5OL4"
FT STRAND 218..222
FT /evidence="ECO:0007829|PDB:5OL4"
FT HELIX 223..225
FT /evidence="ECO:0007829|PDB:5OL4"
FT HELIX 229..242
FT /evidence="ECO:0007829|PDB:5OL4"
FT STRAND 245..249
FT /evidence="ECO:0007829|PDB:5OL4"
FT HELIX 259..266
FT /evidence="ECO:0007829|PDB:5OL4"
FT STRAND 271..275
FT /evidence="ECO:0007829|PDB:5OL4"
FT STRAND 281..283
FT /evidence="ECO:0007829|PDB:4AC7"
FT TURN 284..286
FT /evidence="ECO:0007829|PDB:5OL4"
FT HELIX 287..292
FT /evidence="ECO:0007829|PDB:5OL4"
FT STRAND 296..300
FT /evidence="ECO:0007829|PDB:5OL4"
FT HELIX 302..304
FT /evidence="ECO:0007829|PDB:4AC7"
FT HELIX 311..322
FT /evidence="ECO:0007829|PDB:5OL4"
FT HELIX 330..338
FT /evidence="ECO:0007829|PDB:5OL4"
FT HELIX 342..353
FT /evidence="ECO:0007829|PDB:5OL4"
FT STRAND 366..368
FT /evidence="ECO:0007829|PDB:5OL4"
FT HELIX 373..388
FT /evidence="ECO:0007829|PDB:5OL4"
FT HELIX 400..410
FT /evidence="ECO:0007829|PDB:5OL4"
FT HELIX 412..418
FT /evidence="ECO:0007829|PDB:5OL4"
FT TURN 421..423
FT /evidence="ECO:0007829|PDB:5OL4"
FT STRAND 424..426
FT /evidence="ECO:0007829|PDB:5OL4"
FT STRAND 435..438
FT /evidence="ECO:0007829|PDB:5OL4"
FT HELIX 440..442
FT /evidence="ECO:0007829|PDB:5OL4"
FT TURN 443..445
FT /evidence="ECO:0007829|PDB:5OL4"
FT STRAND 448..452
FT /evidence="ECO:0007829|PDB:5OL4"
FT STRAND 455..461
FT /evidence="ECO:0007829|PDB:5OL4"
FT STRAND 466..469
FT /evidence="ECO:0007829|PDB:5OL4"
FT STRAND 475..478
FT /evidence="ECO:0007829|PDB:5OL4"
FT HELIX 480..482
FT /evidence="ECO:0007829|PDB:5OL4"
FT HELIX 486..489
FT /evidence="ECO:0007829|PDB:5OL4"
FT STRAND 492..495
FT /evidence="ECO:0007829|PDB:5OL4"
FT HELIX 497..501
FT /evidence="ECO:0007829|PDB:5OL4"
FT HELIX 504..508
FT /evidence="ECO:0007829|PDB:5OL4"
FT STRAND 512..516
FT /evidence="ECO:0007829|PDB:5OL4"
FT HELIX 525..527
FT /evidence="ECO:0007829|PDB:5OL4"
FT STRAND 537..539
FT /evidence="ECO:0007829|PDB:5OL4"
FT TURN 541..543
FT /evidence="ECO:0007829|PDB:5OL4"
FT STRAND 546..548
FT /evidence="ECO:0007829|PDB:5OL4"
FT STRAND 551..553
FT /evidence="ECO:0007829|PDB:6G48"
FT STRAND 562..564
FT /evidence="ECO:0007829|PDB:5OL4"
FT TURN 565..567
FT /evidence="ECO:0007829|PDB:5OL4"
SQ SEQUENCE 570 AA; 61400 MW; 4F6DC7E2703A7568 CRC64;
MKINRQQYAE SYGPTVGDQV RLADTDLWIE VEKDTTYGDE AVNFGGGKVL REGMGENGTY
TRTENVLDLL LTNALILDYT GIYKADIGVK DGYIVGIGKG GNPDIMDGVT PNMIVGTATE
VIAAEGKIVT AGGIDTHVHF INPDQVDVAL ANGITTLFGG GTGPAEGSKA TTVTPGPWNI
EKMLKSTEGL PINVGILGKG HGSSIAPIME QIDAGAAGLK IHEDWGATPA SIDRSLTVAD
EADVQVAIHS DTLNEAGFLE DTLRAINGRV IHSFHVEGAG GGHAPDIMAM AGHPNVLPSS
TNPTRPFTVN TIDEHLDMLM VCHHLKQNIP EDVAFADSRI RPETIAAEDI LHDLGIISMM
STDALAMGRA GEMVLRTWQT ADKMKKQRGP LAEEKNGSDN FRAKRYVSKY TINPAIAQGI
AHEVGSIEEG KFADLVLWEP KFFGVKADRV IKGGIIAYAQ IGDPSASIPT PQPVMGRRMY
GTVGDLIHDT NITFMSKSSI QQGVPAKLGL KRRIGTVKNC RNIGKKDMKW NDVTTDIDIN
PETYEVKVDG EVLTCEPVKE LPMAQRYFLF
