GLNK_ECOLI
ID GLNK_ECOLI Reviewed; 112 AA.
AC P0AC55; P38504; P77118; Q2MBX6;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Nitrogen regulatory protein GlnK {ECO:0000305};
DE AltName: Full=Nitrogen regulatory protein P-II 2;
DE AltName: Full=PII-like protein {ECO:0000303|PubMed:7590157};
GN Name=glnK {ECO:0000303|PubMed:8843440}; Synonyms=ybaI;
GN OrderedLocusNames=b0450, JW0440;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=7590157; DOI=10.1111/j.1574-6968.1995.tb07825.x;
RA Vanheeswijk W.C., Stegeman B., Hoving S., Molenaar D., Kahn D.,
RA Westerhoff H.V.;
RT "An additional PII in Escherichia coli: a new regulatory protein in the
RT glutamine synthetase cascade.";
RL FEMS Microbiol. Lett. 132:153-157(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
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 PROTEIN SEQUENCE OF 1-7, FUNCTION, ACTIVITY REGULATION, INTERACTION WITH
RP AMTB, SUBCELLULAR LOCATION, AND URIDYLYLATION.
RX PubMed=16864585; DOI=10.1074/jbc.m602477200;
RA Durand A., Merrick M.;
RT "In vitro analysis of the Escherichia coli AmtB-GlnK complex reveals a
RT stoichiometric interaction and sensitivity to ATP and 2-oxoglutarate.";
RL J. Biol. Chem. 281:29558-29567(2006).
RN [6]
RP IDENTIFICATION.
RX PubMed=7904973; DOI=10.1016/0378-1119(93)90470-n;
RA Allikmets R., Gerrard B.C., Court D., Dean M.C.;
RT "Cloning and organization of the abc and mdl genes of Escherichia coli:
RT relationship to eukaryotic multidrug resistance.";
RL Gene 136:231-236(1993).
RN [7]
RP FUNCTION, INDUCTION, AND URIDYLYLATION.
RX PubMed=8843440; DOI=10.1046/j.1365-2958.1996.6281349.x;
RA van Heeswijk W.C., Hoving S., Molenaar D., Stegeman B., Kahn D.,
RA Westerhoff H.V.;
RT "An alternative PII protein in the regulation of glutamine synthetase in
RT Escherichia coli.";
RL Mol. Microbiol. 21:133-146(1996).
RN [8]
RP FUNCTION, SUBUNIT, AND INTERACTION WITH GLNB.
RX PubMed=10760266; DOI=10.1073/pnas.97.8.3942;
RA van Heeswijk W.C., Wen D., Clancy P., Jaggi R., Ollis D.L.,
RA Westerhoff H.V., Vasudevan S.G.;
RT "The Escherichia coli signal transducers PII (GlnB) and GlnK form
RT heterotrimers in vivo: fine tuning the nitrogen signal cascade.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:3942-3947(2000).
RN [9]
RP FUNCTION, ACTIVITY REGULATION, INTERACTION WITH AMTB, SUBCELLULAR LOCATION,
RP AND URIDYLYLATION.
RX PubMed=11847102; DOI=10.1093/emboj/21.4.536;
RA Coutts G., Thomas G., Blakey D., Merrick M.;
RT "Membrane sequestration of the signal transduction protein GlnK by the
RT ammonium transporter AmtB.";
RL EMBO J. 21:536-545(2002).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12366843; DOI=10.1046/j.1365-2958.2002.03153.x;
RA Blauwkamp T.A., Ninfa A.J.;
RT "Physiological role of the GlnK signal transduction protein of Escherichia
RT coli: survival of nitrogen starvation.";
RL Mol. Microbiol. 46:203-214(2002).
RN [11]
RP FUNCTION, ACTIVITY REGULATION, INTERACTION WITH AMTB, SUBCELLULAR LOCATION,
RP AND MUTAGENESIS OF TYR-51.
RX PubMed=14668330; DOI=10.1074/jbc.m312399200;
RA Javelle A., Severi E., Thornton J., Merrick M.;
RT "Ammonium sensing in Escherichia coli. Role of the ammonium transporter
RT AmtB and AmtB-GlnK complex formation.";
RL J. Biol. Chem. 279:8530-8538(2004).
RN [12]
RP ACTIVITY REGULATION, INTERACTION WITH AMTB, AND URIDYLYLATION.
RX PubMed=20639578; DOI=10.1074/jbc.m110.153908;
RA Radchenko M.V., Thornton J., Merrick M.;
RT "Control of AmtB-GlnK complex formation by intracellular levels of ATP,
RT ADP, and 2-oxoglutarate.";
RL J. Biol. Chem. 285:31037-31045(2010).
RN [13]
RP ACTIVITY REGULATION, AND MUTAGENESIS OF ARG-47 AND TYR-51.
RX PubMed=25566239; DOI=10.3389/fmicb.2014.00731;
RA Radchenko M.V., Thornton J., Merrick M.;
RT "Association and dissociation of the GlnK-AmtB complex in response to
RT cellular nitrogen status can occur in the absence of GlnK post-
RT translational modification.";
RL Front. Microbiol. 5:731-731(2014).
RN [14]
RP FUNCTION.
RX PubMed=28538158; DOI=10.1016/j.bpj.2017.04.012;
RA Gosztolai A., Schumacher J., Behrends V., Bundy J.G., Heydenreich F.,
RA Bennett M.H., Buck M., Barahona M.;
RT "GlnK facilitates the dynamic regulation of bacterial nitrogen
RT assimilation.";
RL Biophys. J. 112:2219-2230(2017).
RN [15] {ECO:0007744|PDB:1GNK, ECO:0007744|PDB:2GNK}
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH ATP, AND SUBUNIT.
RX PubMed=9733647; DOI=10.1006/jmbi.1998.1979;
RA Xu Y., Cheah E., Carr P.D., van Heeswijk W.C., Westerhoff H.V.,
RA Vasudevan S.G., Ollis D.L.;
RT "GlnK, a PII-homologue: structure reveals ATP binding site and indicates
RT how the T-loops may be involved in molecular recognition.";
RL J. Mol. Biol. 282:149-165(1998).
RN [16] {ECO:0007744|PDB:2NUU}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH ADP AND AMTB,
RP SUBUNIT, INTERACTION WITH AMTB, AND DOMAIN.
RX PubMed=17220269; DOI=10.1073/pnas.0610348104;
RA Conroy M.J., Durand A., Lupo D., Li X.D., Bullough P.A., Winkler F.K.,
RA Merrick M.;
RT "The crystal structure of the Escherichia coli AmtB-GlnK complex reveals
RT how GlnK regulates the ammonia channel.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1213-1218(2007).
RN [17] {ECO:0007744|PDB:2NS1}
RP X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) IN COMPLEX WITH ADP AND AMTB,
RP ACTIVITY REGULATION, INTERACTION WITH AMTB, AND DOMAIN.
RX PubMed=17190799; DOI=10.1073/pnas.0609796104;
RA Gruswitz F., O'Connell J. III, Stroud R.M.;
RT "Inhibitory complex of the transmembrane ammonia channel, AmtB, and the
RT cytosolic regulatory protein, GlnK, at 1.96 A.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:42-47(2007).
CC -!- FUNCTION: Involved in the regulation of nitrogen metabolism
CC (PubMed:8843440, PubMed:10760266, PubMed:11847102, PubMed:12366843,
CC PubMed:14668330, PubMed:28538158). Regulates the activity of its
CC targets by protein-protein interaction in response to the nitrogen
CC status of the cell (PubMed:8843440, PubMed:10760266, PubMed:11847102,
CC PubMed:14668330). Involved in the regulation of the ammonium
CC transporter AmtB so as to optimize ammonium uptake under all growth
CC conditions (PubMed:11847102, PubMed:14668330, PubMed:16864585). In
CC nitrogen-limited conditions, GlnK does not interact with AmtB, which
CC remains active and imports ammonium. When extracellular ammonium
CC increases, GlnK associates tightly with AmtB in the inner membrane,
CC thereby inhibiting the transporter activity (PubMed:11847102,
CC PubMed:14668330, PubMed:16864585). Also involved in the regulation of
CC the glutamine synthetase adenylyltransferase/adenylyl-removing (AT/AR)
CC enzyme GlnE and the glutamine synthetase GlnA (PubMed:8843440,
CC PubMed:10760266, PubMed:28538158). In nitrogen-limited conditions,
CC formation of uridylylated GlnB(PII)/GlnK heterotrimers may fine-
CC regulate the activation of GlnA: uridylylated heterotrimers stimulate
CC the deadenylation and the activation of GlnA whereas uridylylated GlnK
CC homotrimers do not stimulate, or hardly stimulate, the deadenylation of
CC GlnA (PubMed:10760266). In addition, regulates the expression of Ntr
CC genes during nitrogen starvation, probably via the control of the
CC levels of phosphorylated NRI during different stages of the response to
CC nitrogen limitation (PubMed:12366843). {ECO:0000269|PubMed:10760266,
CC ECO:0000269|PubMed:11847102, ECO:0000269|PubMed:12366843,
CC ECO:0000269|PubMed:14668330, ECO:0000269|PubMed:16864585,
CC ECO:0000269|PubMed:28538158, ECO:0000269|PubMed:8843440}.
CC -!- ACTIVITY REGULATION: Formation of the GlnK-AmtB complex is influenced
CC by intracellular pools of the effector molecules ATP, ADP, Mg(2+) and
CC 2-oxoglutarate (PubMed:16864585, PubMed:20639578). The rapid drop in
CC the 2-oxoglutarate pool upon ammonium influx and a simultaneous, but
CC transient, change in the ATP/ADP ratio promotes AmtB-GlnK complex
CC formation (PubMed:20639578). ADP orients the surface of GlnK for AmtB
CC blockade (PubMed:17190799). The GlnK-AmtB interaction is also
CC controlled by the level of intracellular glutamine and the
CC uridylylation status of GlnK (PubMed:11847102, PubMed:14668330,
CC PubMed:16864585). The uridylylation state of GlnK influences the
CC dynamics of its interaction with AmtB, but association and dissociation
CC of the complex in response to cellular nitrogen status can occur in the
CC absence of GlnK post-translational modification (PubMed:25566239).
CC {ECO:0000269|PubMed:11847102, ECO:0000269|PubMed:14668330,
CC ECO:0000269|PubMed:16864585, ECO:0000269|PubMed:17190799,
CC ECO:0000269|PubMed:20639578, ECO:0000269|PubMed:25566239}.
CC -!- SUBUNIT: Homotrimer (PubMed:10760266, PubMed:9733647, PubMed:17220269).
CC In response to elevation of the extracellular ammonium concentration,
CC interacts and forms a complex with AmtB (PubMed:11847102,
CC PubMed:14668330, PubMed:17220269, PubMed:17190799, PubMed:16864585,
CC PubMed:20639578). Binds to the cytoplasmic face of AmtB with a
CC stoichiometry of AmtB(3):GlnK(3) (PubMed:17220269, PubMed:17190799).
CC Sequestration by AmtB is reversible (PubMed:14668330). In nitrogen-poor
CC medium, can form heterotrimers with GlnB (PII protein)
CC (PubMed:10760266). {ECO:0000269|PubMed:10760266,
CC ECO:0000269|PubMed:11847102, ECO:0000269|PubMed:14668330,
CC ECO:0000269|PubMed:16864585, ECO:0000269|PubMed:17190799,
CC ECO:0000269|PubMed:17220269, ECO:0000269|PubMed:20639578,
CC ECO:0000269|PubMed:9733647}.
CC -!- INTERACTION:
CC P0AC55; P69681: amtB; NbExp=3; IntAct=EBI-559503, EBI-9137905;
CC P0AC55; P0A9Z1: glnB; NbExp=3; IntAct=EBI-559503, EBI-551053;
CC P0AC55; P27249: glnD; NbExp=3; IntAct=EBI-559503, EBI-552032;
CC P0AC55; P0AC55: glnK; NbExp=3; IntAct=EBI-559503, EBI-559503;
CC P0AC55; P0AFB5: glnL; NbExp=5; IntAct=EBI-559503, EBI-701156;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11847102,
CC ECO:0000269|PubMed:14668330, ECO:0000269|PubMed:16864585}. Cell inner
CC membrane {ECO:0000269|PubMed:11847102, ECO:0000269|PubMed:14668330,
CC ECO:0000269|PubMed:16864585}. Note=During nitrogen limitation, GlnK is
CC predominantly in its fully uridylylated state in the cytoplasmic
CC fraction. In response to nitrogen shock, GlnK is deuridylylated rapidly
CC and associates tightly with AmtB in the inner membrane.
CC {ECO:0000269|PubMed:11847102, ECO:0000269|PubMed:14668330,
CC ECO:0000269|PubMed:16864585}.
CC -!- INDUCTION: Expression is regulated by the nitrogen status
CC (PubMed:8843440). May be regulated through the NRI/NRII two-component
CC regulatory system (PubMed:8843440). {ECO:0000269|PubMed:8843440}.
CC -!- DOMAIN: Interacts with AmtB almost exclusively via a long surface loop
CC containing Tyr-51 (T-loop), the tip of which inserts deeply into the
CC cytoplasmic pore exit, blocking ammonia conduction (PubMed:17220269,
CC PubMed:17190799). Uridylylation probably sterically blocks the T-loop
CC region from interacting with AmtB (PubMed:17190799).
CC {ECO:0000269|PubMed:17190799, ECO:0000269|PubMed:17220269}.
CC -!- PTM: Uridylylated/deuridylylated by GlnD (PubMed:8843440,
CC PubMed:11847102). Fully uridylylated in nitrogen-limited conditions and
CC deuridylylated when extracellular ammonium increases (PubMed:11847102,
CC PubMed:20639578). Uridylylation abrogates binding to AmtB
CC (PubMed:11847102, PubMed:16864585). {ECO:0000269|PubMed:11847102,
CC ECO:0000269|PubMed:16864585, ECO:0000269|PubMed:20639578,
CC ECO:0000269|PubMed:8843440}.
CC -!- DISRUPTION PHENOTYPE: Mutant lacking this gene shows very high
CC expression of the glnK and nac promoters in nitrogen-starved cells, and
CC has a severe defect in the growth rate recovery in ammonia after
CC nitrogen starvation. {ECO:0000269|PubMed:12366843}.
CC -!- SIMILARITY: Belongs to the P(II) protein family. {ECO:0000255|PROSITE-
CC ProRule:PRU00675}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB40206.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U40429; AAD14836.1; -; Genomic_DNA.
DR EMBL; S79842; AAA87955.1; -; Genomic_DNA.
DR EMBL; U82664; AAB40206.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC73553.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76230.1; -; Genomic_DNA.
DR PIR; B64775; B64775.
DR RefSeq; NP_414984.1; NC_000913.3.
DR RefSeq; WP_000780338.1; NZ_STEB01000007.1.
DR PDB; 1GNK; X-ray; 2.00 A; A/B=1-112.
DR PDB; 2GNK; X-ray; 2.00 A; A=1-112.
DR PDB; 2NS1; X-ray; 1.96 A; B=1-112.
DR PDB; 2NUU; X-ray; 2.50 A; G/H/I/J/K/L=1-112.
DR PDBsum; 1GNK; -.
DR PDBsum; 2GNK; -.
DR PDBsum; 2NS1; -.
DR PDBsum; 2NUU; -.
DR AlphaFoldDB; P0AC55; -.
DR SMR; P0AC55; -.
DR BioGRID; 4263149; 10.
DR BioGRID; 849476; 6.
DR DIP; DIP-35006N; -.
DR IntAct; P0AC55; 14.
DR STRING; 511145.b0450; -.
DR SWISS-2DPAGE; P0AC55; -.
DR jPOST; P0AC55; -.
DR PaxDb; P0AC55; -.
DR PRIDE; P0AC55; -.
DR EnsemblBacteria; AAC73553; AAC73553; b0450.
DR EnsemblBacteria; BAE76230; BAE76230; BAE76230.
DR GeneID; 67416475; -.
DR GeneID; 945087; -.
DR KEGG; ecj:JW0440; -.
DR KEGG; eco:b0450; -.
DR PATRIC; fig|1411691.4.peg.1825; -.
DR EchoBASE; EB2108; -.
DR eggNOG; COG0347; Bacteria.
DR HOGENOM; CLU_082268_0_0_6; -.
DR InParanoid; P0AC55; -.
DR OMA; YRGTEHV; -.
DR PhylomeDB; P0AC55; -.
DR BioCyc; EcoCyc:PROTEIN-PII2; -.
DR BioCyc; MetaCyc:PROTEIN-PII2; -.
DR EvolutionaryTrace; P0AC55; -.
DR PRO; PR:P0AC55; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0030234; F:enzyme regulator activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0006808; P:regulation of nitrogen utilization; IBA:GO_Central.
DR Gene3D; 3.30.70.120; -; 1.
DR InterPro; IPR002187; N-reg_PII.
DR InterPro; IPR011322; N-reg_PII-like_a/b.
DR InterPro; IPR015867; N-reg_PII/ATP_PRibTrfase_C.
DR InterPro; IPR017918; N-reg_PII_CS.
DR InterPro; IPR002332; N-reg_PII_urydylation_site.
DR PANTHER; PTHR30115; PTHR30115; 1.
DR Pfam; PF00543; P-II; 1.
DR PIRSF; PIRSF039144; GlnB; 1.
DR PRINTS; PR00340; PIIGLNB.
DR SMART; SM00938; P-II; 1.
DR SUPFAM; SSF54913; SSF54913; 1.
DR PROSITE; PS00638; PII_GLNB_CTER; 1.
DR PROSITE; PS51343; PII_GLNB_DOM; 1.
DR PROSITE; PS00496; PII_GLNB_UMP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell inner membrane; Cell membrane; Cytoplasm;
KW Direct protein sequencing; Membrane; Nucleotide-binding; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..112
FT /note="Nitrogen regulatory protein GlnK"
FT /id="PRO_0000139772"
FT BINDING 29
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000269|PubMed:17220269,
FT ECO:0007744|PDB:2NUU"
FT BINDING 37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:9733647,
FT ECO:0007744|PDB:2GNK"
FT BINDING 38..39
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000269|PubMed:17190799,
FT ECO:0000269|PubMed:17220269, ECO:0007744|PDB:2NS1,
FT ECO:0007744|PDB:2NUU"
FT BINDING 64
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000269|PubMed:17220269,
FT ECO:0007744|PDB:2NUU"
FT BINDING 64
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:9733647,
FT ECO:0007744|PDB:2GNK"
FT BINDING 87..90
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000269|PubMed:17190799,
FT ECO:0000269|PubMed:17220269, ECO:0007744|PDB:2NS1,
FT ECO:0007744|PDB:2NUU"
FT BINDING 87..90
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:9733647,
FT ECO:0007744|PDB:2GNK"
FT BINDING 101..103
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000269|PubMed:17220269,
FT ECO:0007744|PDB:2NUU"
FT BINDING 101..103
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:9733647,
FT ECO:0007744|PDB:2GNK"
FT MOD_RES 51
FT /note="O-UMP-tyrosine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00675"
FT MUTAGEN 47
FT /note="R->A: Shows an identical membrane sequestration
FT profile to the wild-type. Reuridylylation is slightly
FT longer."
FT /evidence="ECO:0000269|PubMed:25566239"
FT MUTAGEN 51
FT /note="Y->A: Fully deuridylylated regardless of the N-
FT status of the cell. Still responds to ammonium shock by
FT becoming rapidly sequestered to the membrane. Sequestration
FT rate is significantly more rapid."
FT /evidence="ECO:0000269|PubMed:25566239"
FT MUTAGEN 51
FT /note="Y->F: Leads to complete inhibition of AmtB
FT activity."
FT /evidence="ECO:0000269|PubMed:14668330"
FT STRAND 1..8
FT /evidence="ECO:0007829|PDB:2NS1"
FT HELIX 10..12
FT /evidence="ECO:0007829|PDB:2NS1"
FT HELIX 13..22
FT /evidence="ECO:0007829|PDB:2NS1"
FT STRAND 29..35
FT /evidence="ECO:0007829|PDB:2NS1"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:2NS1"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:2NS1"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:2NS1"
FT STRAND 56..66
FT /evidence="ECO:0007829|PDB:2NS1"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:2NS1"
FT HELIX 70..81
FT /evidence="ECO:0007829|PDB:2NS1"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:2GNK"
FT STRAND 90..97
FT /evidence="ECO:0007829|PDB:2NS1"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:2NS1"
FT HELIX 108..111
FT /evidence="ECO:0007829|PDB:2NS1"
SQ SEQUENCE 112 AA; 12259 MW; 1875CD92C162B537 CRC64;
MKLVTVIIKP FKLEDVREAL SSIGIQGLTV TEVKGFGRQK GHAELYRGAE YSVNFLPKVK
IDVAIADDQL DEVIDIVSKA AYTGKIGDGK IFVAELQRVI RIRTGEADEA AL
