ID MURE_ECOLI Reviewed; 495 AA.
AC P22188; O07101;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 27-MAR-2024, entry version 202.
DE RecName: Full=UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase;
DE EC=6.3.2.13 {ECO:0000269|PubMed:11124264, ECO:0000269|PubMed:2269304};
DE AltName: Full=Meso-A2pm-adding enzyme;
DE AltName: Full=Meso-diaminopimelate-adding enzyme;
DE AltName: Full=UDP-MurNAc-L-Ala-D-Glu:meso-diaminopimelate ligase;
DE AltName: Full=UDP-MurNAc-tripeptide synthetase;
DE AltName: Full=UDP-N-acetylmuramyl-tripeptide synthetase;
GN Name=murE; OrderedLocusNames=b0085, JW0083;
OS Escherichia coli (strain K12).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2692800; DOI=10.1139/m89-175;
RA Tao J.-S., Ishiguro E.E.;
RT "Nucleotide sequence of the murE gene of Escherichia coli.";
RL Can. J. Microbiol. 35:1051-1054(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1630901; DOI=10.1093/nar/20.13.3305;
RA Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K.,
RA Mizobuchi K., Nakata A.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 0-
RT 2.4 min region.";
RL Nucleic Acids Res. 20:3305-3308(1992).
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 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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTANT MURE1.
RC STRAIN=CGSC 5989;
RX PubMed=9166795; DOI=10.1021/bi9701078;
RA Eveland S.S., Pompliano D.L., Anderson M.S.;
RT "Conditionally lethal Escherichia coli murein mutants contain point defects
RT that map to regions conserved among murein and folyl poly-gamma-glutamate
RT ligases: identification of a ligase superfamily.";
RL Biochemistry 36:6223-6229(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-124, PROTEIN SEQUENCE OF 2-19, AND
RP SEQUENCE REVISION.
RX PubMed=2198024; DOI=10.1042/bj2690277;
RA Michaud C., Parquet C., Flouret B., Blanot D., van Heijenoort J.;
RT "Revised interpretation of the sequence containing the murE gene encoding
RT the UDP-N-acetylmuramyl-tripeptide synthetase of Escherichia coli.";
RL Biochem. J. 269:277-278(1990).
RN [7]
RP PROTEIN SEQUENCE OF 2-19, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, ACTIVITY REGULATION, AND SUBSTRATE SPECIFICITY.
RX PubMed=2269304; DOI=10.1111/j.1432-1033.1990.tb19479.x;
RA Michaud C., Mengin-Lecreulx D., van Heijenoort J., Blanot D.;
RT "Over-production, purification and properties of the uridine-diphosphate-N-
RT acetylmuramoyl-L-alanyl-D-glutamate: meso-2,6-diaminopimelate ligase from
RT Escherichia coli.";
RL Eur. J. Biochem. 194:853-861(1990).
RN [8]
RP FUNCTION, AND SUBSTRATE SPECIFICITY.
RX PubMed=3905407; DOI=10.1111/j.1432-1033.1985.tb09269.x;
RA Abo-Ghalia M., Michaud C., Blanot D., van Heijenoort J.;
RT "Specificity of the uridine-diphosphate-N-acetylmuramyl-L-alanyl-D-
RT glutamate:meso-2,6-diaminopimelate synthetase from Escherichia coli.";
RL Eur. J. Biochem. 153:81-87(1985).
RN [9]
RP KINETIC PARAMETERS, AND SUBSTRATE SPECIFICITY.
RX PubMed=8021219; DOI=10.1128/jb.176.14.4321-4327.1994;
RA Mengin-Lecreulx D., Blanot D., van Heijenoort J.;
RT "Replacement of diaminopimelic acid by cystathionine or lanthionine in the
RT peptidoglycan of Escherichia coli.";
RL J. Bacteriol. 176:4321-4327(1994).
RN [10]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH PRODUCT, FUNCTION,
RP CATALYTIC ACTIVITY, AND CARBOXYLATION AT LYS-225.
RX PubMed=11124264; DOI=10.1074/jbc.m009835200;
RA Gordon E., Flouret B., Chantalat L., van Heijenoort J., Mengin-Lecreulx D.,
RA Dideberg O.;
RT "Crystal structure of UDP-N-acetylmuramoyl-L-alanyl-D-glutamate: meso-
RT diaminopimelate ligase from Escherichia coli.";
RL J. Biol. Chem. 276:10999-11006(2001).
CC -!- FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to the
CC nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG)
CC in the biosynthesis of bacterial cell-wall peptidoglycan. Is also able
CC to use many meso-diaminopimelate analogs as substrates, although much
CC less efficiently, but not L-lysine. {ECO:0000269|PubMed:11124264,
CC ECO:0000269|PubMed:2269304, ECO:0000269|PubMed:3905407}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + meso-2,6-diaminoheptanedioate + UDP-N-acetyl-alpha-D-
CC muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-
CC acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-
CC diaminoheptanedioate; Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57791,
CC ChEBI:CHEBI:83900, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216;
CC EC=6.3.2.13; Evidence={ECO:0000269|PubMed:11124264,
CC ECO:0000269|PubMed:2269304};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00208};
CC -!- ACTIVITY REGULATION: Activated by potassium phosphate.
CC {ECO:0000269|PubMed:2269304}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=76 uM for UDP-N-acetylmuramoyl-L-Ala-D-Glu
CC {ECO:0000269|PubMed:2269304, ECO:0000269|PubMed:8021219};
CC KM=36 uM for meso-diaminopimelate {ECO:0000269|PubMed:2269304,
CC ECO:0000269|PubMed:8021219};
CC KM=1500 uM for meso-lanthionine {ECO:0000269|PubMed:2269304,
CC ECO:0000269|PubMed:8021219};
CC KM=3900 uM for L-allo-cystathionine {ECO:0000269|PubMed:2269304,
CC ECO:0000269|PubMed:8021219};
CC KM=10000 uM for D-allo-cystathionine {ECO:0000269|PubMed:2269304,
CC ECO:0000269|PubMed:8021219};
CC KM=620 uM for ATP {ECO:0000269|PubMed:2269304,
CC ECO:0000269|PubMed:8021219};
CC Vmax=32 nmol/min/mg enzyme with meso-diaminopimelate as substrate
CC {ECO:0000269|PubMed:2269304, ECO:0000269|PubMed:8021219};
CC Vmax=23 nmol/min/mg enzyme with meso-lanthionine as substrate
CC {ECO:0000269|PubMed:2269304, ECO:0000269|PubMed:8021219};
CC Vmax=19 nmol/min/mg enzyme with L-allo-cystathionine as substrate
CC {ECO:0000269|PubMed:2269304, ECO:0000269|PubMed:8021219};
CC Vmax=23 nmol/min/mg enzyme with L-allo-cystathionine as substrate
CC {ECO:0000269|PubMed:2269304, ECO:0000269|PubMed:8021219};
CC pH dependence:
CC Optimum pH is about 8. {ECO:0000269|PubMed:2269304};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC -!- INTERACTION:
CC P22188; P0A6F1: carA; NbExp=2; IntAct=EBI-553061, EBI-546107;
CC P22188; P76069: ydaY; NbExp=3; IntAct=EBI-553061, EBI-545264;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- PTM: Carboxylation is probably crucial for Mg(2+) binding and,
CC consequently, for the gamma-phosphate positioning of ATP.
CC {ECO:0000269|PubMed:11124264}.
CC -!- SIMILARITY: Belongs to the MurCDEF family. MurE subfamily.
CC {ECO:0000305}.
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DR EMBL; X55814; CAA39334.1; -; Genomic_DNA.
DR EMBL; X55034; CAA38862.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73196.1; -; Genomic_DNA.
DR EMBL; AP009048; BAB96653.1; -; Genomic_DNA.
DR EMBL; U67894; AAB60789.1; -; Genomic_DNA.
DR PIR; S14384; S14384.
DR RefSeq; NP_414627.1; NC_000913.3.
DR RefSeq; WP_000775093.1; NZ_LN832404.1.
DR PDB; 1E8C; X-ray; 2.00 A; A/B=2-495.
DR PDB; 7B53; X-ray; 1.75 A; A/B=1-495.
DR PDB; 7B60; X-ray; 1.91 A; A/B=1-495.
DR PDB; 7B61; X-ray; 1.65 A; A/B=1-495.
DR PDB; 7B68; X-ray; 1.89 A; A/B=1-495.
DR PDB; 7B6I; X-ray; 2.07 A; A/B=1-495.
DR PDB; 7B6J; X-ray; 2.09 A; A/B=1-495.
DR PDB; 7B6K; X-ray; 1.84 A; A/B=1-495.
DR PDB; 7B6L; X-ray; 2.08 A; A/B=1-495.
DR PDB; 7B6M; X-ray; 1.67 A; A/B=1-495.
DR PDB; 7B6N; X-ray; 1.79 A; A/B=1-495.
DR PDB; 7B6O; X-ray; 1.86 A; A/B=1-495.
DR PDB; 7B6P; X-ray; 1.68 A; A/B=1-495.
DR PDB; 7B6Q; X-ray; 1.82 A; A/B=1-495.
DR PDB; 7B9E; X-ray; 2.12 A; A/B=1-495.
DR PDB; 7B9W; X-ray; 1.82 A; AAA/BBB=1-495.
DR PDBsum; 1E8C; -.
DR PDBsum; 7B53; -.
DR PDBsum; 7B60; -.
DR PDBsum; 7B61; -.
DR PDBsum; 7B68; -.
DR PDBsum; 7B6I; -.
DR PDBsum; 7B6J; -.
DR PDBsum; 7B6K; -.
DR PDBsum; 7B6L; -.
DR PDBsum; 7B6M; -.
DR PDBsum; 7B6N; -.
DR PDBsum; 7B6O; -.
DR PDBsum; 7B6P; -.
DR PDBsum; 7B6Q; -.
DR PDBsum; 7B9E; -.
DR PDBsum; 7B9W; -.
DR AlphaFoldDB; P22188; -.
DR SMR; P22188; -.
DR BioGRID; 4261641; 527.
DR BioGRID; 849192; 4.
DR DIP; DIP-10280N; -.
DR IntAct; P22188; 20.
DR STRING; 511145.b0085; -.
DR BindingDB; P22188; -.
DR ChEMBL; CHEMBL3309032; -.
DR DrugBank; DB03590; 2,6-Diaminopimelic Acid.
DR DrugBank; DB03801; Lysine Nz-Carboxylic Acid.
DR DrugBank; DB02314; Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine-D-Glutamate.
DR SWISS-2DPAGE; P22188; -.
DR jPOST; P22188; -.
DR PaxDb; 511145-b0085; -.
DR EnsemblBacteria; AAC73196; AAC73196; b0085.
DR GeneID; 944791; -.
DR KEGG; ecj:JW0083; -.
DR KEGG; eco:b0085; -.
DR PATRIC; fig|1411691.4.peg.2195; -.
DR EchoBASE; EB0616; -.
DR eggNOG; COG0769; Bacteria.
DR HOGENOM; CLU_022291_3_2_6; -.
DR InParanoid; P22188; -.
DR OMA; EYFIMEV; -.
DR OrthoDB; 9800958at2; -.
DR PhylomeDB; P22188; -.
DR BioCyc; EcoCyc:UDP-NACMURALGLDAPLIG-MONOMER; -.
DR BioCyc; MetaCyc:UDP-NACMURALGLDAPLIG-MONOMER; -.
DR BRENDA; 6.3.2.13; 2026.
DR UniPathway; UPA00219; -.
DR EvolutionaryTrace; P22188; -.
DR PRO; PR:P22188; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008765; F:UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate ligase activity; IDA:EcoCyc.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IMP:EcoCyc.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR Gene3D; 3.90.190.20; Mur ligase, C-terminal domain; 1.
DR Gene3D; 3.40.1190.10; Mur-like, catalytic domain; 1.
DR Gene3D; 3.40.1390.10; MurE/MurF, N-terminal domain; 1.
DR HAMAP; MF_00208; MurE; 1.
DR InterPro; IPR036565; Mur-like_cat_sf.
DR InterPro; IPR004101; Mur_ligase_C.
DR InterPro; IPR036615; Mur_ligase_C_dom_sf.
DR InterPro; IPR013221; Mur_ligase_cen.
DR InterPro; IPR000713; Mur_ligase_N.
DR InterPro; IPR035911; MurE/MurF_N.
DR InterPro; IPR005761; UDP-N-AcMur-Glu-dNH2Pim_ligase.
DR NCBIfam; TIGR01085; murE; 1.
DR PANTHER; PTHR23135; MUR LIGASE FAMILY MEMBER; 1.
DR PANTHER; PTHR23135:SF4; UDP-N-ACETYLMURAMOYL-L-ALANYL-D-GLUTAMATE--2,6-DIAMINOPIMELATE LIGASE MURE HOMOLOG, CHLOROPLASTIC; 1.
DR Pfam; PF01225; Mur_ligase; 1.
DR Pfam; PF02875; Mur_ligase_C; 1.
DR Pfam; PF08245; Mur_ligase_M; 1.
DR SUPFAM; SSF53623; MurD-like peptide ligases, catalytic domain; 1.
DR SUPFAM; SSF53244; MurD-like peptide ligases, peptide-binding domain; 1.
DR SUPFAM; SSF63418; MurE/MurF N-terminal domain; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell cycle; Cell division; Cell shape;
KW Cell wall biogenesis/degradation; Cytoplasm; Direct protein sequencing;
KW Ligase; Magnesium; Nucleotide-binding; Peptidoglycan synthesis;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2198024,
FT ECO:0000269|PubMed:2269304"
FT CHAIN 2..495
FT /note="UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-
FT diaminopimelate ligase"
FT /id="PRO_0000101893"
FT MOTIF 414..417
FT /note="Meso-diaminopimelate recognition motif"
FT BINDING 27
FT /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-
FT glutamate"
FT /ligand_id="ChEBI:CHEBI:83900"
FT BINDING 29
FT /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-
FT glutamate"
FT /ligand_id="ChEBI:CHEBI:83900"
FT BINDING 44..46
FT /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-
FT glutamate"
FT /ligand_id="ChEBI:CHEBI:83900"
FT BINDING 116..122
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 157
FT /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-
FT glutamate"
FT /ligand_id="ChEBI:CHEBI:83900"
FT BINDING 158..159
FT /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-
FT glutamate"
FT /ligand_id="ChEBI:CHEBI:83900"
FT BINDING 185
FT /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-
FT glutamate"
FT /ligand_id="ChEBI:CHEBI:83900"
FT BINDING 191
FT /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-
FT glutamate"
FT /ligand_id="ChEBI:CHEBI:83900"
FT BINDING 193
FT /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-
FT glutamate"
FT /ligand_id="ChEBI:CHEBI:83900"
FT BINDING 390
FT /ligand="meso-2,6-diaminoheptanedioate"
FT /ligand_id="ChEBI:CHEBI:57791"
FT BINDING 414..417
FT /ligand="meso-2,6-diaminoheptanedioate"
FT /ligand_id="ChEBI:CHEBI:57791"
FT BINDING 465
FT /ligand="meso-2,6-diaminoheptanedioate"
FT /ligand_id="ChEBI:CHEBI:57791"
FT BINDING 469
FT /ligand="meso-2,6-diaminoheptanedioate"
FT /ligand_id="ChEBI:CHEBI:57791"
FT MOD_RES 225
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000269|PubMed:11124264"
FT VARIANT 344
FT /note="E -> K (in murE1)"
FT VARIANT 495
FT /note="A -> S (in murE1)"
FT HELIX 6..10
FT /evidence="ECO:0007829|PDB:7B61"
FT TURN 11..13
FT /evidence="ECO:0007829|PDB:7B61"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:7B61"
FT TURN 29..31
FT /evidence="ECO:0007829|PDB:7B61"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:7B61"
FT HELIX 48..51
FT /evidence="ECO:0007829|PDB:7B61"
FT HELIX 52..57
FT /evidence="ECO:0007829|PDB:7B61"
FT STRAND 61..66
FT /evidence="ECO:0007829|PDB:7B61"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:7B61"
FT STRAND 75..79
FT /evidence="ECO:0007829|PDB:7B61"
FT STRAND 82..87
FT /evidence="ECO:0007829|PDB:7B61"
FT HELIX 90..101
FT /evidence="ECO:0007829|PDB:7B61"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:7B61"
FT STRAND 108..119
FT /evidence="ECO:0007829|PDB:7B61"
FT HELIX 120..133
FT /evidence="ECO:0007829|PDB:7B61"
FT STRAND 138..142
FT /evidence="ECO:0007829|PDB:7B61"
FT STRAND 145..148
FT /evidence="ECO:0007829|PDB:7B61"
FT STRAND 156..159
FT /evidence="ECO:0007829|PDB:1E8C"
FT HELIX 162..174
FT /evidence="ECO:0007829|PDB:7B61"
FT STRAND 178..183
FT /evidence="ECO:0007829|PDB:7B61"
FT HELIX 186..190
FT /evidence="ECO:0007829|PDB:7B61"
FT TURN 191..196
FT /evidence="ECO:0007829|PDB:7B61"
FT STRAND 200..204
FT /evidence="ECO:0007829|PDB:7B61"
FT HELIX 212..215
FT /evidence="ECO:0007829|PDB:1E8C"
FT HELIX 217..231
FT /evidence="ECO:0007829|PDB:7B61"
FT STRAND 236..240
FT /evidence="ECO:0007829|PDB:7B61"
FT HELIX 244..252
FT /evidence="ECO:0007829|PDB:7B61"
FT STRAND 256..263
FT /evidence="ECO:0007829|PDB:7B61"
FT HELIX 267..269
FT /evidence="ECO:0007829|PDB:7B61"
FT STRAND 272..282
FT /evidence="ECO:0007829|PDB:7B61"
FT STRAND 285..292
FT /evidence="ECO:0007829|PDB:7B61"
FT STRAND 297..301
FT /evidence="ECO:0007829|PDB:7B61"
FT HELIX 306..321
FT /evidence="ECO:0007829|PDB:7B61"
FT HELIX 326..332
FT /evidence="ECO:0007829|PDB:7B61"
FT HELIX 333..335
FT /evidence="ECO:0007829|PDB:7B61"
FT STRAND 342..346
FT /evidence="ECO:0007829|PDB:7B61"
FT STRAND 353..357
FT /evidence="ECO:0007829|PDB:7B61"
FT HELIX 362..374
FT /evidence="ECO:0007829|PDB:7B61"
FT STRAND 380..384
FT /evidence="ECO:0007829|PDB:7B61"
FT STRAND 388..390
FT /evidence="ECO:0007829|PDB:7B61"
FT HELIX 394..405
FT /evidence="ECO:0007829|PDB:7B61"
FT STRAND 407..411
FT /evidence="ECO:0007829|PDB:7B61"
FT HELIX 421..430
FT /evidence="ECO:0007829|PDB:7B61"
FT HELIX 435..437
FT /evidence="ECO:0007829|PDB:7B61"
FT STRAND 438..440
FT /evidence="ECO:0007829|PDB:7B61"
FT HELIX 444..454
FT /evidence="ECO:0007829|PDB:7B61"
FT STRAND 460..465
FT /evidence="ECO:0007829|PDB:7B61"
FT STRAND 471..474
FT /evidence="ECO:0007829|PDB:7B61"
FT STRAND 477..480
FT /evidence="ECO:0007829|PDB:7B61"
FT HELIX 483..491
FT /evidence="ECO:0007829|PDB:7B61"
SQ SEQUENCE 495 AA; 53344 MW; D4A7A3E56D6C7E49 CRC64;
MADRNLRDLL APWVPDAPSR ALREMTLDSR VAAAGDLFVA VVGHQADGRR YIPQAIAQGV
AAIIAEAKDE ATDGEIREMH GVPVIYLSQL NERLSALAGR FYHEPSDNLR LVGVTGTNGK
TTTTQLLAQW SQLLGEISAV MGTVGNGLLG KVIPTENTTG SAVDVQHELA GLVDQGATFC
AMEVSSHGLV QHRVAALKFA ASVFTNLSRD HLDYHGDMEH YEAAKWLLYS EHHCGQAIIN
ADDEVGRRWL AKLPDAVAVS MEDHINPNCH GRWLKATEVN YHDSGATIRF SSSWGDGEIE
SHLMGAFNVS NLLLALATLL ALGYPLADLL KTAARLQPVC GRMEVFTAPG KPTVVVDYAH
TPDALEKALQ AARLHCAGKL WCVFGCGGDR DKGKRPLMGA IAEEFADVAV VTDDNPRTEE
PRAIINDILA GMLDAGHAKV MEGRAEAVTC AVMQAKENDV VLVAGKGHED YQIVGNQRLD
YSDRVTVARL LGVIA
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