AMTB_ECO57
ID AMTB_ECO57 Reviewed; 428 AA.
AC P69680; P37905;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Ammonium transporter AmtB {ECO:0000250|UniProtKB:P69681};
DE AltName: Full=Ammonia channel AmtB {ECO:0000250|UniProtKB:P69681};
DE AltName: Full=Ammonium channel AmtB {ECO:0000250|UniProtKB:P69681};
DE Flags: Precursor;
GN Name=amtB; OrderedLocusNames=Z0563, ECs0505;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
CC -!- FUNCTION: Involved in the uptake of ammonium/ammonia (NH(4)(+)/NH(3)).
CC Transport is electrogenic. Following sequestration of NH(4)(+) at the
CC periplasmic face, NH(4)(+) is deprotonated and neutral NH(3) is
CC transported into the cytoplasm. Neutral NH(3) and charged H(+) are
CC carried separately across the membrane on a unique two-lane pathway,
CC before recombining to NH(4)(+) inside the cell.
CC {ECO:0000250|UniProtKB:P69681}.
CC -!- ACTIVITY REGULATION: In the presence of high extracellular ammonium
CC concentrations, transport activity is inhibited by interaction with the
CC regulatory protein GlnK. Formation of the GlnK-AmtB complex is
CC influenced by intracellular pools of the effector molecules ATP, ADP,
CC Mg(2+) and 2-oxoglutarate. The GlnK-AmtB interaction is also controlled
CC by the level of intracellular glutamine and the uridylylation status of
CC GlnK. {ECO:0000250|UniProtKB:P69681}.
CC -!- SUBUNIT: Homotrimer (By similarity). In response to elevation of the
CC extracellular ammonium concentration, interacts and forms a complex
CC with GlnK (By similarity). {ECO:0000250|UniProtKB:P69681}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:P69681}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P69681}.
CC -!- SIMILARITY: Belongs to the ammonia transporter channel (TC 1.A.11.2)
CC family. {ECO:0000305}.
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DR EMBL; AE005174; AAG54801.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB33928.1; -; Genomic_DNA.
DR PIR; C64775; C64775.
DR PIR; E85542; E85542.
DR RefSeq; NP_308532.1; NC_002695.1.
DR RefSeq; WP_000685029.1; NZ_SWKA01000005.1.
DR PDB; 4NH2; X-ray; 2.30 A; A/B/C/D/E/F=26-428.
DR PDBsum; 4NH2; -.
DR AlphaFoldDB; P69680; -.
DR SMR; P69680; -.
DR STRING; 155864.EDL933_0526; -.
DR EnsemblBacteria; AAG54801; AAG54801; Z0563.
DR EnsemblBacteria; BAB33928; BAB33928; ECs_0505.
DR GeneID; 67416474; -.
DR GeneID; 914608; -.
DR KEGG; ece:Z0563; -.
DR KEGG; ecs:ECs_0505; -.
DR PATRIC; fig|386585.9.peg.610; -.
DR eggNOG; COG0004; Bacteria.
DR HOGENOM; CLU_000445_33_0_6; -.
DR OMA; MACWNSN; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008519; F:ammonium transmembrane transporter activity; IEA:InterPro.
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 Membrane; Reference proteome; Signal; Transmembrane; Transmembrane helix;
KW Transport.
FT SIGNAL 1..22
FT /evidence="ECO:0000250|UniProtKB:P69681"
FT CHAIN 23..428
FT /note="Ammonium transporter AmtB"
FT /id="PRO_0000001308"
FT TOPO_DOM 23..32
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P69681"
FT TRANSMEM 33..54
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P69681"
FT TOPO_DOM 55..65
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P69681"
FT TRANSMEM 66..90
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P69681"
FT TOPO_DOM 91..119
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P69681"
FT TRANSMEM 120..142
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P69681"
FT TOPO_DOM 143..146
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P69681"
FT TRANSMEM 147..171
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P69681"
FT TOPO_DOM 172..185
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P69681"
FT TRANSMEM 186..201
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P69681"
FT TOPO_DOM 202..221
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P69681"
FT TRANSMEM 222..241
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P69681"
FT TOPO_DOM 242..248
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P69681"
FT TRANSMEM 249..273
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P69681"
FT TOPO_DOM 274..279
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P69681"
FT TRANSMEM 280..300
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P69681"
FT TOPO_DOM 301..302
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P69681"
FT TRANSMEM 303..321
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P69681"
FT TOPO_DOM 322..333
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P69681"
FT TRANSMEM 334..355
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P69681"
FT TOPO_DOM 356..370
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P69681"
FT TRANSMEM 371..399
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P69681"
FT TOPO_DOM 400..428
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P69681"
FT BINDING 241
FT /ligand="NH4(+)"
FT /ligand_id="ChEBI:CHEBI:28938"
FT /evidence="ECO:0000250|UniProtKB:P69681"
FT SITE 182
FT /note="Important for the deprotonation of the ammonium
FT cation"
FT /evidence="ECO:0000250|UniProtKB:P69681"
FT SITE 190
FT /note="Twin-His motif. Important for optimum substrate
FT conductance"
FT /evidence="ECO:0000250|UniProtKB:P69681"
FT SITE 237
FT /note="Important for optimum substrate conductance"
FT /evidence="ECO:0000250|UniProtKB:P69681"
FT SITE 340
FT /note="Twin-His motif. Important for optimum substrate
FT conductance"
FT /evidence="ECO:0000250|UniProtKB:P69681"
FT HELIX 29..46
FT /evidence="ECO:0007829|PDB:4NH2"
FT HELIX 49..55
FT /evidence="ECO:0007829|PDB:4NH2"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:4NH2"
FT HELIX 63..83
FT /evidence="ECO:0007829|PDB:4NH2"
FT HELIX 85..90
FT /evidence="ECO:0007829|PDB:4NH2"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:4NH2"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:4NH2"
FT TURN 104..107
FT /evidence="ECO:0007829|PDB:4NH2"
FT HELIX 119..141
FT /evidence="ECO:0007829|PDB:4NH2"
FT HELIX 147..160
FT /evidence="ECO:0007829|PDB:4NH2"
FT HELIX 162..170
FT /evidence="ECO:0007829|PDB:4NH2"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:4NH2"
FT HELIX 174..177
FT /evidence="ECO:0007829|PDB:4NH2"
FT TURN 186..189
FT /evidence="ECO:0007829|PDB:4NH2"
FT HELIX 190..202
FT /evidence="ECO:0007829|PDB:4NH2"
FT HELIX 220..239
FT /evidence="ECO:0007829|PDB:4NH2"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:4NH2"
FT STRAND 243..246
FT /evidence="ECO:0007829|PDB:4NH2"
FT HELIX 247..275
FT /evidence="ECO:0007829|PDB:4NH2"
FT HELIX 280..294
FT /evidence="ECO:0007829|PDB:4NH2"
FT TURN 295..300
FT /evidence="ECO:0007829|PDB:4NH2"
FT HELIX 303..322
FT /evidence="ECO:0007829|PDB:4NH2"
FT HELIX 335..354
FT /evidence="ECO:0007829|PDB:4NH2"
FT HELIX 357..359
FT /evidence="ECO:0007829|PDB:4NH2"
FT HELIX 370..402
FT /evidence="ECO:0007829|PDB:4NH2"
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
