NAT_SACS2
ID NAT_SACS2 Reviewed; 167 AA.
AC Q980R9;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 2.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=N-alpha-acetyltransferase {ECO:0000303|PubMed:17511810};
DE Short=NAT {ECO:0000303|PubMed:17511810};
DE EC=2.3.1.255 {ECO:0000269|PubMed:17511810, ECO:0000269|PubMed:23959863, ECO:0000269|PubMed:25728374};
DE EC=2.3.1.258 {ECO:0000269|PubMed:17511810, ECO:0000269|PubMed:23959863};
DE AltName: Full=Amino-terminal acetyltransferase {ECO:0000303|PubMed:17511810};
DE AltName: Full=N-terminal acetyltransferase {ECO:0000303|PubMed:17511810};
GN Name=ard1 {ECO:0000303|PubMed:17511810}; OrderedLocusNames=SSO0209;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RX PubMed=17511810; DOI=10.1111/j.1365-2958.2007.05752.x;
RA Mackay D.T., Botting C.H., Taylor G.L., White M.F.;
RT "An acetylase with relaxed specificity catalyses protein N-terminal
RT acetylation in Sulfolobus solfataricus.";
RL Mol. Microbiol. 64:1540-1548(2007).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG.
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=20419351; DOI=10.1007/s10969-010-9090-y;
RA Oke M., Carter L.G., Johnson K.A., Liu H., McMahon S.A., Yan X., Kerou M.,
RA Weikart N.D., Kadi N., Sheikh M.A., Schmelz S., Dorward M., Zawadzki M.,
RA Cozens C., Falconer H., Powers H., Overton I.M., van Niekerk C.A., Peng X.,
RA Patel P., Garrett R.A., Prangishvili D., Botting C.H., Coote P.J.,
RA Dryden D.T., Barton G.J., Schwarz-Linek U., Challis G.L., Taylor G.L.,
RA White M.F., Naismith J.H.;
RT "The Scottish Structural Proteomics Facility: targets, methods and
RT outputs.";
RL J. Struct. Funct. Genomics 11:167-180(2010).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) IN COMPLEX WITH ZINC ION AND
RP ACETYL-COA, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP MUTAGENESIS OF LEU-33; PRO-34; GLU-35; TYR-37; HIS-88; TYR-125; GLU-127;
RP ARG-129 AND TYR-154, AND SUBSTRATE SPECIFICITY.
RX PubMed=23959863; DOI=10.1073/pnas.1310365110;
RA Liszczak G., Marmorstein R.;
RT "Implications for the evolution of eukaryotic amino-terminal
RT acetyltransferase (NAT) enzymes from the structure of an archaeal
RT ortholog.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:14652-14657(2013).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS,
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF
RP GLU-35; ARG-100; THR-105 AND ASN-132, AND SUBSTRATE SPECIFICITY.
RX PubMed=25728374; DOI=10.1038/srep08673;
RA Chang Y.Y., Hsu C.H.;
RT "Structural basis for substrate-specific acetylation of Nalpha-
RT acetyltransferase Ard1 from Sulfolobus solfataricus.";
RL Sci. Rep. 5:8673-8673(2015).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG,
RP MUTAGENESIS OF SER-75 AND SER-82, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBUNIT.
RX PubMed=26593285; DOI=10.1002/cbic.201500568;
RA Chang Y.Y., Hsu C.H.;
RT "Multiple conformations of the loop region confers heat-resistance on
RT ssArd1, a Thermophilic NatA.";
RL ChemBioChem 17:214-217(2016).
CC -!- FUNCTION: Displays alpha (N-terminal) acetyltransferase activity.
CC Catalyzes the covalent attachment of an acetyl moiety from acetyl-CoA
CC to the free alpha-amino group at the N-terminus of a protein
CC (PubMed:17511810, PubMed:23959863, PubMed:25728374). NAT is able to
CC acetylate the alpha-amino group of methionine, alanine and serine N-
CC terminal residue substrates, however it has a preference for Ser-N-
CC terminal substrates (PubMed:17511810, PubMed:23959863,
CC PubMed:25728374). {ECO:0000269|PubMed:17511810,
CC ECO:0000269|PubMed:23959863, ECO:0000269|PubMed:25728374}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-alanyl-[protein] = CoA + H(+) + N-
CC terminal N(alpha)-acetyl-L-alanyl-[protein]; Xref=Rhea:RHEA:50500,
CC Rhea:RHEA-COMP:12701, Rhea:RHEA-COMP:12702, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64718,
CC ChEBI:CHEBI:83683; EC=2.3.1.255;
CC Evidence={ECO:0000269|PubMed:17511810, ECO:0000269|PubMed:25728374};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-seryl-[protein] = CoA + H(+) + N-
CC terminal N(alpha)-acetyl-L-seryl-[protein]; Xref=Rhea:RHEA:50504,
CC Rhea:RHEA-COMP:12703, Rhea:RHEA-COMP:12704, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64738,
CC ChEBI:CHEBI:83690; EC=2.3.1.255;
CC Evidence={ECO:0000269|PubMed:17511810, ECO:0000269|PubMed:23959863,
CC ECO:0000269|PubMed:25728374};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-leucyl-[protein] = CoA +
CC H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-leucyl-[protein];
CC Xref=Rhea:RHEA:50520, Rhea:RHEA-COMP:12711, Rhea:RHEA-COMP:12712,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:133377, ChEBI:CHEBI:133378; EC=2.3.1.258;
CC Evidence={ECO:0000269|PubMed:17511810, ECO:0000269|PubMed:23959863};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-glutamyl-[protein] = CoA
CC + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-glutamyl-[protein];
CC Xref=Rhea:RHEA:50488, Rhea:RHEA-COMP:12696, Rhea:RHEA-COMP:12697,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:133359, ChEBI:CHEBI:133360;
CC Evidence={ECO:0000269|PubMed:17511810};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=54 uM for Ser-N-terminal peptide {ECO:0000269|PubMed:23959863};
CC KM=67.17 uM for acetyl-CoA (at 65 degrees Celsius with Ser-N-terminal
CC peptide (Alba)) {ECO:0000269|PubMed:25728374};
CC KM=400 uM for Met-N-terminal peptide {ECO:0000269|PubMed:23959863};
CC Note=kcat is 33.57 min(-1) for acetyltransferase activity with
CC acetyl-CoA (at 65 degrees Celsius with Ser-N-terminal peptide (Alba))
CC (PubMed:25728374). kcat is 3.3 min(-1) for acetyltransferase activity
CC with Ser-N-terminal peptide (PubMed:23959863). kcat is 0.73 min(-1)
CC for acetyltransferase activity with Met-N-terminal peptide
CC (PubMed:23959863). {ECO:0000269|PubMed:23959863,
CC ECO:0000269|PubMed:25728374};
CC Temperature dependence:
CC Thermostable. {ECO:0000269|PubMed:26593285};
CC -!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:26593285}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- MISCELLANEOUS: NAT does not require a binding partner for activity.
CC {ECO:0000269|PubMed:17511810, ECO:0000269|PubMed:23959863}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. ARD1 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK40554.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE006641; AAK40554.1; ALT_INIT; Genomic_DNA.
DR PIR; C90162; C90162.
DR PDB; 2X7B; X-ray; 1.95 A; A=1-167.
DR PDB; 4LX9; X-ray; 1.98 A; A=1-167.
DR PDB; 4R3K; X-ray; 2.13 A; A=1-167.
DR PDB; 4R3L; X-ray; 1.84 A; A=1-167.
DR PDB; 5C88; X-ray; 2.49 A; A/B=1-167.
DR PDB; 6AG4; X-ray; 2.26 A; A=1-167.
DR PDB; 6AG5; X-ray; 2.32 A; A=1-167.
DR PDBsum; 2X7B; -.
DR PDBsum; 4LX9; -.
DR PDBsum; 4R3K; -.
DR PDBsum; 4R3L; -.
DR PDBsum; 5C88; -.
DR PDBsum; 6AG4; -.
DR PDBsum; 6AG5; -.
DR AlphaFoldDB; Q980R9; -.
DR SMR; Q980R9; -.
DR STRING; 273057.SSO0209; -.
DR DNASU; 1455364; -.
DR EnsemblBacteria; AAK40554; AAK40554; SSO0209.
DR KEGG; sso:SSO0209; -.
DR PATRIC; fig|273057.12.peg.208; -.
DR eggNOG; arCOG00833; Archaea.
DR HOGENOM; CLU_013985_23_0_2; -.
DR InParanoid; Q980R9; -.
DR OMA; SGEIMGY; -.
DR PhylomeDB; Q980R9; -.
DR BRENDA; 2.3.1.255; 6163.
DR EvolutionaryTrace; Q980R9; -.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0031415; C:NatA complex; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004596; F:peptide alpha-N-acetyltransferase activity; IDA:UniProtKB.
DR GO; GO:0006474; P:N-terminal protein amino acid acetylation; IEA:InterPro.
DR InterPro; IPR006464; AcTrfase_RimI/Ard1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR045047; Ard1-like.
DR InterPro; IPR000182; GNAT_dom.
DR PANTHER; PTHR23091; PTHR23091; 1.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR TIGRFAMs; TIGR01575; rimI; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Cytoplasm; Metal-binding;
KW Reference proteome; Transferase; Zinc.
FT CHAIN 1..167
FT /note="N-alpha-acetyltransferase"
FT /id="PRO_0000281644"
FT DOMAIN 12..167
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT BINDING 37
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:25728374,
FT ECO:0007744|PDB:4R3L"
FT BINDING 88
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:23959863,
FT ECO:0007744|PDB:4LX9"
FT BINDING 92..94
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|PubMed:20419351,
FT ECO:0000269|PubMed:23959863, ECO:0000269|PubMed:25728374,
FT ECO:0000269|PubMed:26593285, ECO:0007744|PDB:2X7B,
FT ECO:0007744|PDB:4LX9, ECO:0007744|PDB:4R3K,
FT ECO:0007744|PDB:4R3L, ECO:0007744|PDB:5C88"
FT BINDING 100..105
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|PubMed:20419351,
FT ECO:0000269|PubMed:23959863, ECO:0000269|PubMed:25728374,
FT ECO:0000269|PubMed:26593285, ECO:0007744|PDB:2X7B,
FT ECO:0007744|PDB:4LX9, ECO:0007744|PDB:4R3K,
FT ECO:0007744|PDB:4R3L, ECO:0007744|PDB:5C88"
FT BINDING 127
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:23959863,
FT ECO:0007744|PDB:4LX9"
FT BINDING 132
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|PubMed:20419351,
FT ECO:0000269|PubMed:23959863, ECO:0000269|PubMed:25728374,
FT ECO:0007744|PDB:2X7B, ECO:0007744|PDB:4LX9,
FT ECO:0007744|PDB:4R3K, ECO:0007744|PDB:4R3L"
FT BINDING 139..141
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|PubMed:20419351,
FT ECO:0000269|PubMed:23959863, ECO:0000269|PubMed:25728374,
FT ECO:0007744|PDB:2X7B, ECO:0007744|PDB:4LX9,
FT ECO:0007744|PDB:4R3K, ECO:0007744|PDB:4R3L"
FT BINDING 154
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:25728374,
FT ECO:0007744|PDB:4R3L"
FT SITE 35
FT /note="Plays an important role in substrate specificity"
FT /evidence="ECO:0000269|PubMed:25728374"
FT SITE 75
FT /note="Plays an important role in modulating multiple
FT conformations of loop regions and contributes to protein
FT thermostability"
FT /evidence="ECO:0000269|PubMed:26593285"
FT SITE 82
FT /note="Plays an important role in modulating multiple
FT conformations of loop regions and contributes to protein
FT thermostability"
FT /evidence="ECO:0000269|PubMed:26593285"
FT MUTAGEN 33
FT /note="L->A: 20- and 2-fold decrease of the catalytic
FT efficiency and affinity for Ser-N-terminal peptide. 11-fold
FT decrease of the catalytic efficiency for Met-N-terminal
FT peptide, but almost same affinity compared to the wild-
FT type."
FT /evidence="ECO:0000269|PubMed:23959863"
FT MUTAGEN 34
FT /note="P->A: 20-fold decrease of the catalytic efficiency
FT for Ser-N-terminal peptide, but almost same affinity
FT compared to the wild-type. 18-fold decrease of the
FT catalytic efficiency for Met-N-terminal peptide, but almost
FT same affinity compared to the wild-type."
FT /evidence="ECO:0000269|PubMed:23959863,
FT ECO:0000269|PubMed:25728374"
FT MUTAGEN 35
FT /note="E->A: Slight increase of the catalytic efficiency
FT for Ser-N-terminal peptide, but 4-fold decrease of the
FT affinity compared to the wild-type. 6-fold increase of the
FT catalytic efficiency for Met-N-terminal peptide and slight
FT decrease of the affinity compared to the wild-type."
FT /evidence="ECO:0000269|PubMed:23959863,
FT ECO:0000269|PubMed:25728374"
FT MUTAGEN 35
FT /note="E->F: Strong decrease of the acetyltransferase
FT activity with Ser-N-terminal peptide such as Alba. 2-fold
FT increase of acetyltransferase activity for Ala-N-terminal
FT peptide such as Hjc compared to the wild-type."
FT /evidence="ECO:0000269|PubMed:25728374"
FT MUTAGEN 35
FT /note="E->Q: Loss of acetyltransferase activity for Ser and
FT Met-N-terminal peptide; when associated with Gln-127."
FT /evidence="ECO:0000269|PubMed:23959863"
FT MUTAGEN 35
FT /note="E->V: Alters the N-terminal substrate specificity
FT and allows large N-terminal end residue of the substrate to
FT be accommodated in a substrate-binding pocket. 4-fold
FT increase of the acetyltransferase activity with Met-N-
FT terminal peptide such as SSB compared to the wild-type. 2-
FT fold increase of acetyltransferase activity with Ala-N-
FT terminal peptide such as Hjc."
FT /evidence="ECO:0000269|PubMed:25728374"
FT MUTAGEN 35
FT /note="E->W: Low acetyltransferase activity with Ala-,
FT Met- and Ser-N-terminal peptide."
FT /evidence="ECO:0000269|PubMed:25728374"
FT MUTAGEN 37
FT /note="Y->A: 34-fold decrease of the catalytic efficiency
FT for Ser-N-terminal peptide and slight decrease of the
FT affinity compared to the wild-type. Loss of
FT acetyltransferase activity for Met-N-terminal peptide."
FT /evidence="ECO:0000269|PubMed:23959863"
FT MUTAGEN 37
FT /note="Y->F: Same catalytic efficiency and slight decrease
FT of the affinity for Ser-N-terminal peptide compared to the
FT wild-type. 3-fold decrease of the catalytic efficiency and
FT 1.3-fold increase of the affinity for Met-N-terminal
FT peptide compared to the wild-type."
FT /evidence="ECO:0000269|PubMed:23959863"
FT MUTAGEN 75
FT /note="S->A: Has a melting temperature about 3 degrees
FT Celsius lower than that of the wild-type."
FT /evidence="ECO:0000269|PubMed:26593285"
FT MUTAGEN 82
FT /note="S->A: Has a melting temperature about 3 degrees
FT Celsius lower than that of the wild-type."
FT /evidence="ECO:0000269|PubMed:26593285"
FT MUTAGEN 88
FT /note="H->A: 2.5- and 1.5-fold decrease of the catalytic
FT efficiency and affinity for Ser-N-terminal peptide compared
FT to the wild-type, respectively. Loss of acetyltransferase
FT activity for Met-N-terminal peptide."
FT /evidence="ECO:0000269|PubMed:23959863"
FT MUTAGEN 88
FT /note="H->F: 2.5-fold decrease of the catalytic efficiency
FT for Ser-N-terminal peptide, but almost same affinity
FT compared to the wild-type. Loss of acetyltransferase
FT activity for Met-N-terminal peptide."
FT /evidence="ECO:0000269|PubMed:23959863"
FT MUTAGEN 88
FT /note="H->Q: 2.5-fold decrease of the catalytic efficiency
FT for Ser-N-terminal peptide, but 1.5-fold increase of the
FT affinity compared to the wild-type. Loss of
FT acetyltransferase activity for Met-N-terminal peptide."
FT /evidence="ECO:0000269|PubMed:23959863"
FT MUTAGEN 100
FT /note="R->A: 7-fold decrease of the affinity, with no
FT significant difference in the catalytic efficiency. Same
FT fold compared to the wild-type."
FT /evidence="ECO:0000269|PubMed:25728374"
FT MUTAGEN 105
FT /note="T->A: 3-fold decrease of the affinity, with no
FT significant difference in the catalytic efficiency. Same
FT fold compared to the wild-type."
FT /evidence="ECO:0000269|PubMed:25728374"
FT MUTAGEN 125
FT /note="Y->A: Same catalytic efficiency and 1.7-fold
FT decrease of the affinity for Ser-N-terminal peptide
FT compared to the wild-type. 1.5- and 2.5-fold decrease of
FT the catalytic efficiency and affinity for Met-N-terminal
FT peptide compared to the wild-type, respectively."
FT /evidence="ECO:0000269|PubMed:23959863"
FT MUTAGEN 127
FT /note="E->A: Same catalytic efficiency and slight decrease
FT of the affinity for Ser-N-terminal peptide compared to the
FT wild-type. Loss of acetyltransferase activity for Met-N-
FT terminal peptide."
FT /evidence="ECO:0000269|PubMed:23959863"
FT MUTAGEN 127
FT /note="E->H: 1.3-fold decrease of the catalytic efficiency
FT for Ser-N-terminal peptide, but almost same affinity
FT compared to the wild-type. 1.7-fold decrease of the
FT catalytic efficiency and 1.3-fold increase of the affinity
FT for Met-N-terminal peptide compared to the wild-type."
FT /evidence="ECO:0000269|PubMed:23959863"
FT MUTAGEN 127
FT /note="E->Q: 2.3-fold decrease of the catalytic efficiency
FT and 1.3-fold increase of the affinity for Ser-N-terminal
FT peptide compared to the wild-type. 5-fold decrease of the
FT catalytic efficiency and slight decrease of the affinity
FT for Met-N-terminal peptide compared to the wild-type. Loss
FT of acetyltransferase activity for Ser and Met-N-terminal
FT peptide; when associated with Gln-35."
FT /evidence="ECO:0000269|PubMed:23959863"
FT MUTAGEN 129
FT /note="R->A: Slight decrease of the catalytic efficiency
FT and of the affinity for Ser-N-terminal peptide compared to
FT teh wild-type. 2.5-fold increase of the catalytic
FT efficiency and almost the same affinity for Met-N-terminal
FT peptide compared to the wild-type."
FT /evidence="ECO:0000269|PubMed:23959863"
FT MUTAGEN 132
FT /note="N->A: 4.5-fold decrease of the affinity, with no
FT significant difference in the catalytic efficiency. Same
FT fold compared to the wild-type."
FT /evidence="ECO:0000269|PubMed:25728374"
FT MUTAGEN 154
FT /note="Y->A: 1.3-fold decrease of the catalytic efficiency
FT for Ser-N-terminal peptide, but same affinity compared to
FT the wild-type. 6.5-fold decrease of the catalytic
FT efficiency for Met-N-terminal peptide, but same affinity
FT compared to the wild-type."
FT /evidence="ECO:0000269|PubMed:23959863"
FT MUTAGEN 154
FT /note="Y->F: Almost same catalytic efficiency for Ser-N-
FT terminal peptide and slight decrease of the affinity
FT compared to the wild-type. 5-fold decrease of the catalytic
FT efficiency for Met-N-terminal peptide and 1.5-fold decrease
FT of the affinity compared to the wild-type."
FT /evidence="ECO:0000269|PubMed:23959863"
FT STRAND 13..16
FT /evidence="ECO:0007829|PDB:4R3L"
FT HELIX 19..21
FT /evidence="ECO:0007829|PDB:4R3L"
FT HELIX 22..32
FT /evidence="ECO:0007829|PDB:4R3L"
FT HELIX 39..49
FT /evidence="ECO:0007829|PDB:4R3L"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:4R3L"
FT STRAND 54..58
FT /evidence="ECO:0007829|PDB:4R3L"
FT STRAND 61..74
FT /evidence="ECO:0007829|PDB:4R3L"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:4R3K"
FT STRAND 83..94
FT /evidence="ECO:0007829|PDB:4R3L"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:4R3L"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:4R3L"
FT HELIX 103..119
FT /evidence="ECO:0007829|PDB:4R3L"
FT STRAND 122..129
FT /evidence="ECO:0007829|PDB:4R3L"
FT HELIX 133..141
FT /evidence="ECO:0007829|PDB:4R3L"
FT STRAND 145..150
FT /evidence="ECO:0007829|PDB:4R3L"
FT STRAND 154..157
FT /evidence="ECO:0007829|PDB:5C88"
FT STRAND 160..166
FT /evidence="ECO:0007829|PDB:4R3L"
SQ SEQUENCE 167 AA; 19448 MW; 410D4CA4F7CEA60E CRC64;
MELAEKDKGR DFTLRNARMD DIDQIIKINR LTLPENYPYY FFVEHLKEYG LAFFVAIVDN
SVVGYIMPRI EWGFSNIKQL PSLVRKGHVV SIAVLEEYRR KGIATTLLEA SMKSMKNDYN
AEEIYLEVRV SNYPAIALYE KLNFKKVKVL KGYYADGEDA YLMARPL
