AMTB_ECOLI
ID AMTB_ECOLI Reviewed; 428 AA.
AC P69681; P37905; Q2MBX5;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Ammonium transporter AmtB {ECO:0000303|PubMed:11847102, ECO:0000303|PubMed:12023896};
DE AltName: Full=Ammonia channel AmtB {ECO:0000303|PubMed:16910683, ECO:0000303|PubMed:17040913};
DE AltName: Full=Ammonium channel AmtB {ECO:0000303|PubMed:15876187};
DE Flags: Precursor;
GN Name=amtB {ECO:0000303|PubMed:8843440}; Synonyms=ybaG;
GN OrderedLocusNames=b0451, JW0441;
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=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 [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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 377-428.
RC STRAIN=K12;
RX PubMed=1645722; DOI=10.1016/s0021-9258(18)99125-8;
RA Naggert J., Narasimhan M.L., Deveaux L., Cho H., Randhawa Z.I.,
RA Cronan J.E. Jr., Green B.N., Smith S.;
RT "Cloning, sequencing, and characterization of Escherichia coli thioesterase
RT II.";
RL J. Biol. Chem. 266:11044-11050(1991).
RN [6]
RP IDENTIFICATION.
RX PubMed=7984428; DOI=10.1093/nar/22.22.4756;
RA Borodovsky M., Rudd K.E., Koonin E.V.;
RT "Intrinsic and extrinsic approaches for detecting genes in a bacterial
RT genome.";
RL Nucleic Acids Res. 22:4756-4767(1994).
RN [7]
RP TOPOLOGY.
RX PubMed=10931328; DOI=10.1046/j.1365-2958.2000.01994.x;
RA Thomas G.H., Mullins J.G., Merrick M.;
RT "Membrane topology of the Mep/Amt family of ammonium transporters.";
RL Mol. Microbiol. 37:331-344(2000).
RN [8]
RP POSSIBLE INTERACTION WITH GLNK.
RX PubMed=10637624; DOI=10.1016/s0168-9525(99)01887-9;
RA Thomas G.H., Coutts G., Merrick M.;
RT "The glnKamtB operon. A conserved gene pair in prokaryotes.";
RL Trends Genet. 16:11-14(2000).
RN [9]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=12023896; DOI=10.1042/bj20011761;
RA Blakey D., Leech A., Thomas G.H., Coutts G., Findlay K., Merrick M.;
RT "Purification of the Escherichia coli ammonium transporter AmtB reveals a
RT trimeric stoichiometry.";
RL Biochem. J. 364:527-535(2002).
RN [10]
RP FUNCTION, ACTIVITY REGULATION, INTERACTION WITH GLNK, SUBCELLULAR LOCATION,
RP DOMAIN, AND MUTAGENESIS OF 404-GLY--ALA-428.
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 [11]
RP FUNCTION, ACTIVITY REGULATION, INTERACTION WITH GLNK, AND MUTAGENESIS OF
RP ASP-182.
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 FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=15876187; DOI=10.1042/bj20042094;
RA Javelle A., Thomas G., Marini A.M., Kraemer R., Merrick M.;
RT "In vivo functional characterization of the Escherichia coli ammonium
RT channel AmtB: evidence for metabolic coupling of AmtB to glutamine
RT synthetase.";
RL Biochem. J. 390:215-222(2005).
RN [13]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [14]
RP FUNCTION, AND MOLECULAR DYNAMICS SIMULATIONS.
RX PubMed=16910683; DOI=10.1021/ja0631549;
RA Lin Y., Cao Z., Mo Y.;
RT "Molecular dynamics simulations on the Escherichia coli ammonia channel
RT protein AmtB: mechanism of ammonia/ammonium transport.";
RL J. Am. Chem. Soc. 128:10876-10884(2006).
RN [15]
RP ACTIVITY REGULATION, AND INTERACTION WITH GLNK.
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 [16]
RP DOMAIN, AND MUTAGENESIS OF 405-LEU--ALA-428; ARG-406; GLY-415;
RP 421-HIS--ALA-428; 426-TYR--ALA-428; TYR-426; 427-ASN-ALA-428; ASN-427 AND
RP ALA-428.
RX PubMed=17453422; DOI=10.1080/09687860601129420;
RA Severi E., Javelle A., Merrick M.;
RT "The conserved carboxy-terminal region of the ammonia channel AmtB plays a
RT critical role in channel function.";
RL Mol. Membr. Biol. 24:161-171(2007).
RN [17]
RP FUNCTION, AND MUTAGENESIS OF TRP-170.
RX PubMed=17998534; DOI=10.1073/pnas.0709267104;
RA Fong R.N., Kim K.S., Yoshihara C., Inwood W.B., Kustu S.;
RT "The W148L substitution in the Escherichia coli ammonium channel AmtB
RT increases flux and indicates that the substrate is an ion.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:18706-18711(2007).
RN [18]
RP FUNCTION, DEPROTONATION MECHANISM, AND MOLECULAR DYNAMICS SIMULATIONS ON
RP WILD-TYPE AND ALA-182 MUTANT.
RX PubMed=19278252; DOI=10.1021/jp810651m;
RA Lin Y., Cao Z., Mo Y.;
RT "Functional role of Asp160 and the deprotonation mechanism of ammonium in
RT the Escherichia coli ammonia channel protein AmtB.";
RL J. Phys. Chem. B 113:4922-4929(2009).
RN [19]
RP ACTIVITY REGULATION, AND INTERACTION WITH GLNK.
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 [20]
RP MUTAGENESIS OF HIS-190 AND HIS-340.
RX PubMed=23667517; DOI=10.1371/journal.pone.0062745;
RA Wang J., Fulford T., Shao Q., Javelle A., Yang H., Zhu W., Merrick M.;
RT "Ammonium transport proteins with changes in one of the conserved pore
RT histidines have different performance in ammonia and methylamine
RT conduction.";
RL PLoS ONE 8:e62745-e62745(2013).
RN [21]
RP INTERACTION WITH LIPIDS.
RX PubMed=24899312; DOI=10.1038/nature13419;
RA Laganowsky A., Reading E., Allison T.M., Ulmschneider M.B., Degiacomi M.T.,
RA Baldwin A.J., Robinson C.V.;
RT "Membrane proteins bind lipids selectively to modulate their structure and
RT function.";
RL Nature 510:172-175(2014).
RN [22]
RP FUNCTION, AND INTERACTION WITH LIPIDS.
RX PubMed=30211659; DOI=10.1096/fj.201800782r;
RA Mirandela G.D., Tamburrino G., Hoskisson P.A., Zachariae U., Javelle A.;
RT "The lipid environment determines the activity of the Escherichia coli
RT ammonium transporter AmtB.";
RL FASEB J. 33:1989-1999(2019).
RN [23]
RP FUNCTION, TRANSPORT MECHANISM, AND MUTAGENESIS OF ASP-182; HIS-190 AND
RP HIS-340.
RX PubMed=32662768; DOI=10.7554/elife.57183;
RA Williamson G., Tamburrino G., Bizior A., Boeckstaens M., Dias Mirandela G.,
RA Bage M.G., Pisliakov A., Ives C.M., Terras E., Hoskisson P.A., Marini A.M.,
RA Zachariae U., Javelle A.;
RT "A two-lane mechanism for selective biological ammonium transport.";
RL Elife 9:0-0(2020).
RN [24] {ECO:0007744|PDB:1XQE, ECO:0007744|PDB:1XQF}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 23-428, FUNCTION, SUBUNIT,
RP SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=15563598; DOI=10.1073/pnas.0406475101;
RA Zheng L., Kostrewa D., Berneche S., Winkler F.K., Li X.-D.;
RT "The mechanism of ammonia transport based on the crystal structure of AmtB
RT of Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:17090-17095(2004).
RN [25] {ECO:0007744|PDB:1U77, ECO:0007744|PDB:1U7C, ECO:0007744|PDB:1U7G}
RP X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 23-407 IN COMPLEXES WITH AMMONIA;
RP AMMONIUM AND METHYLAMINE, PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION,
RP SUBUNIT, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=15361618; DOI=10.1126/science.1101952;
RA Khademi S., O'Connell J.D. III, Remis J., Robles-Colmenares Y.,
RA Miercke L.J., Stroud R.M.;
RT "Mechanism of ammonia transport by Amt/MEP/Rh: structure of AmtB at 1.35
RT A.";
RL Science 305:1587-1594(2004).
RN [26] {ECO:0007744|PDB:2NMR, ECO:0007744|PDB:2NOP, ECO:0007744|PDB:2NOW, ECO:0007744|PDB:2NPC, ECO:0007744|PDB:2NPD, ECO:0007744|PDB:2NPE, ECO:0007744|PDB:2NPG, ECO:0007744|PDB:2NPJ, ECO:0007744|PDB:2NPK}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 23-428 OF WILD-TYPE AND HISTIDINE
RP MUTANTS, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, AND MUTAGENESIS OF
RP HIS-190 AND HIS-340.
RX PubMed=17040913; DOI=10.1074/jbc.m608325200;
RA Javelle A., Lupo D., Zheng L., Li X.D., Winkler F.K., Merrick M.;
RT "An unusual twin-his arrangement in the pore of ammonia channels is
RT essential for substrate conductance.";
RL J. Biol. Chem. 281:39492-39498(2006).
RN [27] {ECO:0007744|PDB:2NUU}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 25-428 IN COMPLEX WITH GLNK,
RP SUBUNIT, AND INTERACTION WITH GLNK.
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 [28] {ECO:0007744|PDB:2NS1}
RP X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) OF 23-428 IN COMPLEX WITH GLNK,
RP INTERACTION WITH GLNK, 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).
RN [29] {ECO:0007744|PDB:3C1G, ECO:0007744|PDB:3C1H, ECO:0007744|PDB:3C1I, ECO:0007744|PDB:3C1J}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 23-428 OF WILD-TYPE AND MUTANTS
RP PHE-129; PHE-237 AND PHE-129/PHE-237, FUNCTION, ACTIVITY REGULATION, AND
RP MUTAGENESIS OF PHE-129; TRP-170; TRP-234; PHE-237 AND SER-241.
RX PubMed=18362341; DOI=10.1073/pnas.0711742105;
RA Javelle A., Lupo D., Ripoche P., Fulford T., Merrick M., Winkler F.K.;
RT "Substrate binding, deprotonation, and selectivity at the periplasmic
RT entrance of the Escherichia coli ammonia channel AmtB.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:5040-5045(2008).
RN [30] {ECO:0007744|PDB:6B21}
RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 26-428 IN COMPLEX WITH
RP CARDIOLIPIN, INTERACTION WITH LIPIDS, AND MUTAGENESIS OF HIS-178.
RX PubMed=29507234; DOI=10.1073/pnas.1719813115;
RA Patrick J.W., Boone C.D., Liu W., Conover G.M., Liu Y., Cong X.,
RA Laganowsky A.;
RT "Allostery revealed within lipid binding events to membrane proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:2976-2981(2018).
CC -!- FUNCTION: Involved in the uptake of ammonium/ammonia (NH(4)(+)/NH(3))
CC (PubMed:14668330, PubMed:15876187, PubMed:15563598, PubMed:15361618,
CC PubMed:16910683, PubMed:30211659, PubMed:32662768). Transport is
CC electrogenic (PubMed:30211659, PubMed:32662768). Following
CC sequestration of NH(4)(+) at the periplasmic face, NH(4)(+) is
CC deprotonated and neutral NH(3) is transported into the cytoplasm
CC (PubMed:15876187, PubMed:16910683, PubMed:18362341, PubMed:19278252,
CC PubMed:32662768). Neutral NH(3) and charged H(+) are carried separately
CC across the membrane on a unique two-lane pathway, before recombining to
CC NH(4)(+) inside the cell (PubMed:32662768). In vitro can also transport
CC the larger analogs methylamine and methylammonium (PubMed:11847102,
CC PubMed:14668330, PubMed:12023896, PubMed:15876187, PubMed:17998534,
CC PubMed:18362341). Also acts as a sensor of the extracellular ammonium
CC concentration (PubMed:14668330). {ECO:0000269|PubMed:11847102,
CC ECO:0000269|PubMed:12023896, ECO:0000269|PubMed:14668330,
CC ECO:0000269|PubMed:15361618, ECO:0000269|PubMed:15563598,
CC ECO:0000269|PubMed:15876187, ECO:0000269|PubMed:16910683,
CC ECO:0000269|PubMed:17998534, ECO:0000269|PubMed:18362341,
CC ECO:0000269|PubMed:19278252, ECO:0000269|PubMed:30211659,
CC ECO:0000269|PubMed:32662768}.
CC -!- ACTIVITY REGULATION: In the presence of high extracellular ammonium
CC concentrations, transport activity is inhibited by interaction with the
CC regulatory protein GlnK (PubMed:11847102, PubMed:14668330,
CC PubMed:16864585). Ammonium transport through AmtB is required for GlnK
CC sequestration (PubMed:14668330). Formation of the GlnK-AmtB complex is
CC influenced by intracellular pools of the effector molecules ATP, ADP,
CC Mg(2+) and 2-oxoglutarate (PubMed:16864585, PubMed:20639578). The rapid
CC drop in the 2-oxoglutarate pool upon ammonium influx and a
CC simultaneous, but transient, change in the ATP/ADP ratio promotes AmtB-
CC GlnK complex formation (PubMed:20639578). The GlnK-AmtB interaction is
CC also controlled by the level of intracellular glutamine and the
CC uridylylation status of GlnK (PubMed:14668330). Inhibited by imidazole
CC and thallium, which likely act by competitive binding to the
CC periplasmic ammonium binding site (PubMed:18362341). Transport activity
CC is independent of the membrane potential and of ATP hydrolysis
CC (PubMed:15876187). {ECO:0000269|PubMed:11847102,
CC ECO:0000269|PubMed:14668330, ECO:0000269|PubMed:15876187,
CC ECO:0000269|PubMed:16864585, ECO:0000269|PubMed:18362341,
CC ECO:0000269|PubMed:20639578}.
CC -!- SUBUNIT: Homotrimer (PubMed:12023896, PubMed:15563598, PubMed:15361618,
CC PubMed:17040913). In response to elevation of the extracellular
CC ammonium concentration, interacts and forms a complex with GlnK
CC (PubMed:10637624, PubMed:11847102, PubMed:14668330, PubMed:17220269,
CC PubMed:17190799, PubMed:16864585, PubMed:20639578). Interacts with GlnK
CC with a stoichiometry of AmtB(3):GlnK(3) (PubMed:17220269,
CC PubMed:17190799). Sequestration of GlnK is reversible
CC (PubMed:14668330). {ECO:0000269|PubMed:10637624,
CC ECO:0000269|PubMed:11847102, ECO:0000269|PubMed:12023896,
CC ECO:0000269|PubMed:14668330, ECO:0000269|PubMed:15361618,
CC ECO:0000269|PubMed:15563598, ECO:0000269|PubMed:16864585,
CC ECO:0000269|PubMed:17040913, ECO:0000269|PubMed:17190799,
CC ECO:0000269|PubMed:17220269, ECO:0000269|PubMed:20639578}.
CC -!- INTERACTION:
CC P69681; P69681: amtB; NbExp=4; IntAct=EBI-9137905, EBI-9137905;
CC P69681; P0AC55: glnK; NbExp=3; IntAct=EBI-9137905, EBI-559503;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:11847102,
CC ECO:0000269|PubMed:12023896, ECO:0000269|PubMed:15361618,
CC ECO:0000269|PubMed:15563598, ECO:0000269|PubMed:17040913}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:15361618,
CC ECO:0000269|PubMed:15563598, ECO:0000269|PubMed:17040913}.
CC -!- DOMAIN: The C-terminal cytoplasmic domain plays a significant role in
CC normal function and it might also mediate co-operativity between the
CC three subunits (PubMed:17453422). The C-terminal cytoplasmic domain is
CC also required for interaction with the T-loop of GlnK (PubMed:11847102,
CC PubMed:17190799). {ECO:0000269|PubMed:11847102,
CC ECO:0000269|PubMed:17190799, ECO:0000269|PubMed:17453422}.
CC -!- MISCELLANEOUS: Specifically binds 1-palmitoyl-2-oleoyl
CC phosphatidylglycerol (POPG), which increases protein stability
CC (PubMed:24899312). POPG is an essential cofactor for transport activity
CC and, in the absence of POPG, AmtB cannot complete the full
CC translocation cycle (PubMed:30211659). Can also bind
CC phosphatidylethanolamine and cardiolipin-like molecules, leading to
CC positive allosteric modulation (PubMed:29507234).
CC {ECO:0000269|PubMed:24899312, ECO:0000269|PubMed:29507234,
CC ECO:0000269|PubMed:30211659}.
CC -!- SIMILARITY: Belongs to the ammonia transporter channel (TC 1.A.11.2)
CC family. {ECO:0000305}.
CC -!- CAUTION: Methylammonium (MeA) has been widely used to measure ammonium
CC transport activity because the radioactive tracer [14C]MeA is
CC commercially available. However, MeA is a poor substrate analog for
CC AmtB, not well suited to elucidate the mechanistic details of AmtB
CC activity. {ECO:0000305|PubMed:30211659}.
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DR EMBL; U40429; AAD14837.1; -; Genomic_DNA.
DR EMBL; U82664; AAB40207.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73554.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76231.1; -; Genomic_DNA.
DR EMBL; M63308; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A90692; A90692.
DR PIR; C64775; C64775.
DR PIR; E85542; E85542.
DR RefSeq; NP_414985.1; NC_000913.3.
DR RefSeq; WP_000685029.1; NZ_STEB01000007.1.
DR PDB; 1U77; X-ray; 2.00 A; A=23-407.
DR PDB; 1U7C; X-ray; 1.85 A; A=23-407.
DR PDB; 1U7G; X-ray; 1.40 A; A=23-407.
DR PDB; 1XQE; X-ray; 2.10 A; A=23-428.
DR PDB; 1XQF; X-ray; 1.80 A; A=23-428.
DR PDB; 2NMR; X-ray; 2.10 A; A=23-428.
DR PDB; 2NOP; X-ray; 2.00 A; A=23-428.
DR PDB; 2NOW; X-ray; 2.20 A; A=23-428.
DR PDB; 2NPC; X-ray; 2.10 A; A=23-428.
DR PDB; 2NPD; X-ray; 2.10 A; A=23-428.
DR PDB; 2NPE; X-ray; 2.10 A; A=23-428.
DR PDB; 2NPG; X-ray; 2.00 A; A=23-428.
DR PDB; 2NPJ; X-ray; 2.00 A; A=23-428.
DR PDB; 2NPK; X-ray; 2.00 A; A=23-428.
DR PDB; 2NS1; X-ray; 1.96 A; A=23-428.
DR PDB; 2NUU; X-ray; 2.50 A; A/B/C/D/E/F=25-428.
DR PDB; 3C1G; X-ray; 2.30 A; A=23-428.
DR PDB; 3C1H; X-ray; 2.20 A; A=23-428.
DR PDB; 3C1I; X-ray; 2.30 A; A=23-428.
DR PDB; 3C1J; X-ray; 2.00 A; A=23-428.
DR PDB; 6B21; X-ray; 2.45 A; A=26-428.
DR PDBsum; 1U77; -.
DR PDBsum; 1U7C; -.
DR PDBsum; 1U7G; -.
DR PDBsum; 1XQE; -.
DR PDBsum; 1XQF; -.
DR PDBsum; 2NMR; -.
DR PDBsum; 2NOP; -.
DR PDBsum; 2NOW; -.
DR PDBsum; 2NPC; -.
DR PDBsum; 2NPD; -.
DR PDBsum; 2NPE; -.
DR PDBsum; 2NPG; -.
DR PDBsum; 2NPJ; -.
DR PDBsum; 2NPK; -.
DR PDBsum; 2NS1; -.
DR PDBsum; 2NUU; -.
DR PDBsum; 3C1G; -.
DR PDBsum; 3C1H; -.
DR PDBsum; 3C1I; -.
DR PDBsum; 3C1J; -.
DR PDBsum; 6B21; -.
DR AlphaFoldDB; P69681; -.
DR PCDDB; P69681; -.
DR SMR; P69681; -.
DR BioGRID; 4259856; 9.
DR BioGRID; 849473; 3.
DR DIP; DIP-29874N; -.
DR IntAct; P69681; 3.
DR STRING; 511145.b0451; -.
DR DrugBank; DB04147; Dodecyldimethylamine N-oxide.
DR DrugBank; DB01828; Methylamine.
DR TCDB; 1.A.11.1.1; the ammonium transporter channel (amt) family.
DR jPOST; P69681; -.
DR PaxDb; P69681; -.
DR PRIDE; P69681; -.
DR EnsemblBacteria; AAC73554; AAC73554; b0451.
DR EnsemblBacteria; BAE76231; BAE76231; BAE76231.
DR GeneID; 67416474; -.
DR GeneID; 945084; -.
DR KEGG; ecj:JW0441; -.
DR KEGG; eco:b0451; -.
DR PATRIC; fig|1411691.4.peg.1824; -.
DR EchoBASE; EB1768; -.
DR eggNOG; COG0004; Bacteria.
DR HOGENOM; CLU_000445_33_0_6; -.
DR InParanoid; P69681; -.
DR OMA; MACWNSN; -.
DR PhylomeDB; P69681; -.
DR BioCyc; EcoCyc:AMTB-MON; -.
DR BioCyc; MetaCyc:AMTB-MON; -.
DR EvolutionaryTrace; P69681; -.
DR PRO; PR:P69681; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0008519; F:ammonium transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0072488; P:ammonium transmembrane transport; IDA:UniProtKB.
DR GO; GO:0015670; P:carbon dioxide transport; IDA:UniProtKB.
DR Gene3D; 1.10.3430.10; -; 1.
DR InterPro; IPR029020; Ammonium/urea_transptr.
DR InterPro; IPR001905; Ammonium_transpt.
DR InterPro; IPR018047; Ammonium_transpt_CS.
DR InterPro; IPR024041; NH4_transpt_AmtB-like_dom.
DR PANTHER; PTHR43029; PTHR43029; 1.
DR Pfam; PF00909; Ammonium_transp; 1.
DR TIGRFAMs; TIGR00836; amt; 1.
DR PROSITE; PS01219; AMMONIUM_TRANSP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Ammonia transport; Cell inner membrane; Cell membrane;
KW Direct protein sequencing; Membrane; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:15361618"
FT CHAIN 23..428
FT /note="Ammonium transporter AmtB"
FT /id="PRO_0000001307"
FT TOPO_DOM 23..32
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:15361618,
FT ECO:0000269|PubMed:15563598, ECO:0000269|PubMed:17040913"
FT TRANSMEM 33..54
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:15361618,
FT ECO:0000269|PubMed:15563598, ECO:0000269|PubMed:17040913"
FT TOPO_DOM 55..65
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15361618,
FT ECO:0000269|PubMed:15563598, ECO:0000269|PubMed:17040913"
FT TRANSMEM 66..90
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:15361618,
FT ECO:0000269|PubMed:15563598, ECO:0000269|PubMed:17040913"
FT TOPO_DOM 91..119
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:15361618,
FT ECO:0000269|PubMed:15563598, ECO:0000269|PubMed:17040913"
FT TRANSMEM 120..142
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:15361618,
FT ECO:0000269|PubMed:15563598, ECO:0000269|PubMed:17040913"
FT TOPO_DOM 143..146
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15361618,
FT ECO:0000269|PubMed:15563598, ECO:0000269|PubMed:17040913"
FT TRANSMEM 147..171
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:15361618,
FT ECO:0000269|PubMed:15563598, ECO:0000269|PubMed:17040913"
FT TOPO_DOM 172..185
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:15361618,
FT ECO:0000269|PubMed:15563598, ECO:0000269|PubMed:17040913"
FT TRANSMEM 186..201
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:15361618,
FT ECO:0000269|PubMed:15563598, ECO:0000269|PubMed:17040913"
FT TOPO_DOM 202..221
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15361618,
FT ECO:0000269|PubMed:15563598, ECO:0000269|PubMed:17040913"
FT TRANSMEM 222..241
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:15361618,
FT ECO:0000269|PubMed:15563598, ECO:0000269|PubMed:17040913"
FT TOPO_DOM 242..248
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:15361618,
FT ECO:0000269|PubMed:15563598, ECO:0000269|PubMed:17040913"
FT TRANSMEM 249..273
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:15361618,
FT ECO:0000269|PubMed:15563598, ECO:0000269|PubMed:17040913"
FT TOPO_DOM 274..279
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15361618,
FT ECO:0000269|PubMed:15563598, ECO:0000269|PubMed:17040913"
FT TRANSMEM 280..300
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:15361618,
FT ECO:0000269|PubMed:15563598, ECO:0000269|PubMed:17040913"
FT TOPO_DOM 301..302
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:15361618,
FT ECO:0000269|PubMed:15563598, ECO:0000269|PubMed:17040913"
FT TRANSMEM 303..321
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:15361618,
FT ECO:0000269|PubMed:15563598, ECO:0000269|PubMed:17040913"
FT TOPO_DOM 322..333
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15361618,
FT ECO:0000269|PubMed:15563598, ECO:0000269|PubMed:17040913"
FT TRANSMEM 334..355
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:15361618,
FT ECO:0000269|PubMed:15563598, ECO:0000269|PubMed:17040913"
FT TOPO_DOM 356..370
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:15361618,
FT ECO:0000269|PubMed:15563598, ECO:0000269|PubMed:17040913"
FT TRANSMEM 371..399
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:15361618,
FT ECO:0000269|PubMed:15563598, ECO:0000269|PubMed:17040913"
FT TOPO_DOM 400..428
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15361618,
FT ECO:0000269|PubMed:15563598, ECO:0000269|PubMed:15919996,
FT ECO:0000269|PubMed:17040913"
FT BINDING 241
FT /ligand="NH4(+)"
FT /ligand_id="ChEBI:CHEBI:28938"
FT /evidence="ECO:0000269|PubMed:15361618"
FT SITE 182
FT /note="Important for the deprotonation of the ammonium
FT cation"
FT /evidence="ECO:0000269|PubMed:19278252"
FT SITE 190
FT /note="Twin-His motif. Important for optimum substrate
FT conductance"
FT /evidence="ECO:0000305|PubMed:17040913,
FT ECO:0000305|PubMed:23667517, ECO:0000305|PubMed:32662768"
FT SITE 237
FT /note="Important for optimum substrate conductance"
FT /evidence="ECO:0000305|PubMed:18362341"
FT SITE 340
FT /note="Twin-His motif. Important for optimum substrate
FT conductance"
FT /evidence="ECO:0000305|PubMed:17040913,
FT ECO:0000305|PubMed:23667517, ECO:0000305|PubMed:32662768"
FT MUTAGEN 129
FT /note="F->A: 1.4-fold increase in transport activity with
FT methylammonium as substrate. Shows 80% inhibition by
FT thallium."
FT /evidence="ECO:0000269|PubMed:18362341"
FT MUTAGEN 170
FT /note="W->A: 2.5-fold increase in transport activity with
FT methylammonium as substrate. Shows 80% inhibition by
FT thallium."
FT /evidence="ECO:0000269|PubMed:18362341"
FT MUTAGEN 170
FT /note="W->L: 5-fold increase in transport activity with
FT methylammonium as substrate."
FT /evidence="ECO:0000269|PubMed:17998534"
FT MUTAGEN 178
FT /note="H->A: Abolishes the positive allosteric modulation
FT observed for binding phosphatidylethanolamine and
FT cardiolipin-like molecules."
FT /evidence="ECO:0000269|PubMed:29507234"
FT MUTAGEN 182
FT /note="D->A: Impairs ammonium transport. Loss of activity
FT with methylammonium as substrate. GlnK remains fully
FT uridylylated and localizes to the cytoplasm during a
FT transient increase in extracellular ammonium."
FT /evidence="ECO:0000269|PubMed:14668330,
FT ECO:0000269|PubMed:32662768"
FT MUTAGEN 182
FT /note="D->E: Impairs ammonium transport. Retains 71% of
FT wild-type activity with methylammonium as substrate. Allows
FT some complex formation with GlnK during a transient
FT increase in extracellular ammonium."
FT /evidence="ECO:0000269|PubMed:14668330,
FT ECO:0000269|PubMed:32662768"
FT MUTAGEN 190
FT /note="H->A: Does not prevent transport of ammonia. Loss of
FT transport activity with methylammonium and methylamine.
FT Shows normal GlnK-AmtB complex formation after ammonium
FT shock. Loss of both methylamine and ammonia transport; when
FT associated with A-340."
FT /evidence="ECO:0000269|PubMed:17040913,
FT ECO:0000269|PubMed:23667517, ECO:0000269|PubMed:32662768"
FT MUTAGEN 190
FT /note="H->D,F,N,Q: Loss of transport activity with
FT methylammonium as substrate. Shows normal GlnK-AmtB complex
FT formation after ammonium shock."
FT /evidence="ECO:0000269|PubMed:17040913"
FT MUTAGEN 190
FT /note="H->E: Retains 25% of transport activity with
FT methylammonium as substrate. Shows normal GlnK-AmtB complex
FT formation after ammonium shock."
FT /evidence="ECO:0000269|PubMed:17040913"
FT MUTAGEN 190
FT /note="H->K: Loss of transport activity with methylammonium
FT as substrate."
FT /evidence="ECO:0000269|PubMed:17040913"
FT MUTAGEN 190
FT /note="H->T: Loss of transport activity with methylammonium
FT as substrate. Cannot form GlnK-AmtB complex after ammonium
FT shock."
FT /evidence="ECO:0000269|PubMed:17040913"
FT MUTAGEN 234
FT /note="W->A: Loss of transport activity with methylammonium
FT as substrate."
FT /evidence="ECO:0000269|PubMed:18362341"
FT MUTAGEN 234
FT /note="W->F: Retains 80% of transport activity with
FT methylammonium as substrate."
FT /evidence="ECO:0000269|PubMed:18362341"
FT MUTAGEN 237
FT /note="F->A,H,L,Q,S,W: Loss of transport activity with
FT methylammonium as substrate."
FT /evidence="ECO:0000269|PubMed:18362341"
FT MUTAGEN 241
FT /note="S->A: 4-fold increase in transport activity with
FT methylammonium as substrate. Shows 80% inhibition by
FT thallium."
FT /evidence="ECO:0000269|PubMed:18362341"
FT MUTAGEN 340
FT /note="H->A: Does not prevent transport of ammonia. Loss of
FT transport activity with methylammonium and methylamine.
FT Shows normal GlnK-AmtB complex formation after ammonium
FT shock. Loss of both methylamine and ammonia transport; when
FT associated with A-190."
FT /evidence="ECO:0000269|PubMed:17040913,
FT ECO:0000269|PubMed:23667517, ECO:0000269|PubMed:32662768"
FT MUTAGEN 340
FT /note="H->E,F: Loss of transport activity with
FT methylammonium as substrate. Shows normal GlnK-AmtB complex
FT formation after ammonium shock."
FT /evidence="ECO:0000269|PubMed:17040913"
FT MUTAGEN 340
FT /note="H->T: Loss of transport activity with methylammonium
FT as substrate."
FT /evidence="ECO:0000269|PubMed:17040913"
FT MUTAGEN 404..428
FT /note="Missing: Reduced methylamine transport activity.
FT Cannot interact with GlnK."
FT /evidence="ECO:0000269|PubMed:11847102"
FT MUTAGEN 405..428
FT /note="Missing: Retains 27% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:17453422"
FT MUTAGEN 406
FT /note="R->A: Almost loss of activity."
FT /evidence="ECO:0000269|PubMed:17453422"
FT MUTAGEN 415
FT /note="G->A,D,E,N,R: Almost loss of activity."
FT /evidence="ECO:0000269|PubMed:17453422"
FT MUTAGEN 421..428
FT /note="Missing: Retains 43% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:17453422"
FT MUTAGEN 426..428
FT /note="Missing: Retains 21% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:17453422"
FT MUTAGEN 426
FT /note="Y->G: Retains 11% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:17453422"
FT MUTAGEN 427..428
FT /note="Missing: Retains 12% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:17453422"
FT MUTAGEN 427
FT /note="N->A: Retains 33% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:17453422"
FT MUTAGEN 427
FT /note="N->D: No change in activity."
FT /evidence="ECO:0000269|PubMed:17453422"
FT MUTAGEN 427
FT /note="N->Q: Retains 28% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:17453422"
FT MUTAGEN 428
FT /note="Missing: No change in activity."
FT /evidence="ECO:0000269|PubMed:17453422"
FT CONFLICT 377..382
FT /note="QLESIA -> SWKASP (in Ref. 5; M63308)"
FT /evidence="ECO:0000305"
FT HELIX 29..46
FT /evidence="ECO:0007829|PDB:1U7G"
FT HELIX 49..55
FT /evidence="ECO:0007829|PDB:1U7G"
FT HELIX 60..83
FT /evidence="ECO:0007829|PDB:1U7G"
FT HELIX 85..90
FT /evidence="ECO:0007829|PDB:1U7G"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:1U7G"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:3C1J"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:1U7G"
FT HELIX 119..141
FT /evidence="ECO:0007829|PDB:1U7G"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:1U7G"
FT HELIX 147..160
FT /evidence="ECO:0007829|PDB:1U7G"
FT HELIX 162..170
FT /evidence="ECO:0007829|PDB:1U7G"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:1XQF"
FT HELIX 174..178
FT /evidence="ECO:0007829|PDB:1U7G"
FT TURN 186..189
FT /evidence="ECO:0007829|PDB:1U7G"
FT HELIX 190..203
FT /evidence="ECO:0007829|PDB:1U7G"
FT TURN 208..212
FT /evidence="ECO:0007829|PDB:2NS1"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:1U7G"
FT HELIX 220..239
FT /evidence="ECO:0007829|PDB:1U7G"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:1U7G"
FT STRAND 243..246
FT /evidence="ECO:0007829|PDB:1U7G"
FT HELIX 247..275
FT /evidence="ECO:0007829|PDB:1U7G"
FT HELIX 280..294
FT /evidence="ECO:0007829|PDB:1U7G"
FT TURN 295..300
FT /evidence="ECO:0007829|PDB:1U7G"
FT HELIX 303..328
FT /evidence="ECO:0007829|PDB:1U7G"
FT HELIX 333..335
FT /evidence="ECO:0007829|PDB:1U7G"
FT HELIX 336..354
FT /evidence="ECO:0007829|PDB:1U7G"
FT HELIX 357..359
FT /evidence="ECO:0007829|PDB:1U7G"
FT HELIX 370..402
FT /evidence="ECO:0007829|PDB:1U7G"
FT HELIX 409..414
FT /evidence="ECO:0007829|PDB:2NS1"
FT HELIX 416..421
FT /evidence="ECO:0007829|PDB:2NS1"
SQ SEQUENCE 428 AA; 44515 MW; B4AC96F0E5AE2B59 CRC64;
MKIATIKTGL ASLAMLPGLV MAAPAVADKA DNAFMMICTA LVLFMTIPGI ALFYGGLIRG
KNVLSMLTQV TVTFALVCIL WVVYGYSLAF GEGNNFFGNI NWLMLKNIEL TAVMGSIYQY
IHVAFQGSFA CITVGLIVGA LAERIRFSAV LIFVVVWLTL SYIPIAHMVW GGGLLASHGA
LDFAGGTVVH INAAIAGLVG AYLIGKRVGF GKEAFKPHNL PMVFTGTAIL YIGWFGFNAG
SAGTANEIAA LAFVNTVVAT AAAILGWIFG EWALRGKPSL LGACSGAIAG LVGVTPACGY
IGVGGALIIG VVAGLAGLWG VTMLKRLLRV DDPCDVFGVH GVCGIVGCIM TGIFAASSLG
GVGFAEGVTM GHQLLVQLES IAITIVWSGV VAFIGYKLAD LTVGLRVPEE QEREGLDVNS
HGENAYNA
