ID   AMT2_METJA              Reviewed;         420 AA.
AC   Q58739;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Ammonium transporter Amt2 {ECO:0000250|UniProtKB:Q60366};
GN   Name=amt2 {ECO:0000305}; OrderedLocusNames=MJ1343;
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS   10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=243232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA   Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA   Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA   Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA   Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA   Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA   Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA   Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA   Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT   "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT   jannaschii.";
RL   Science 273:1058-1073(1996).
CC   -!- FUNCTION: Involved in the uptake of ammonium/ammonia (NH(4)(+)/NH(3))
CC       (By similarity). Transport is electrogenic (By similarity).
CC       {ECO:0000250|UniProtKB:O29285}.
CC   -!- SUBUNIT: Homotrimer (By similarity). Interacts and forms a complex with
CC       GlnK2 (By similarity). {ECO:0000250|UniProtKB:Q60366}.
CC   -!- INTERACTION:
CC       Q58739; Q60381: glnK1; NbExp=2; IntAct=EBI-7201308, EBI-7201321;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the ammonia transporter channel (TC 1.A.11.2)
CC       family. {ECO:0000305}.
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DR   EMBL; L77117; AAB99352.1; -; Genomic_DNA.
DR   PIR; F64467; F64467.
DR   AlphaFoldDB; Q58739; -.
DR   SMR; Q58739; -.
DR   IntAct; Q58739; 1.
DR   MINT; Q58739; -.
DR   STRING; 243232.MJ_1343; -.
DR   EnsemblBacteria; AAB99352; AAB99352; MJ_1343.
DR   KEGG; mja:MJ_1343; -.
DR   eggNOG; arCOG04397; Archaea.
DR   HOGENOM; CLU_000445_33_1_2; -.
DR   InParanoid; Q58739; -.
DR   OMA; IWLSIMS; -.
DR   PhylomeDB; Q58739; -.
DR   Proteomes; UP000000805; 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   GO; GO:0097272; P:ammonium homeostasis; IBA:GO_Central.
DR   GO; GO:0072488; P:ammonium transmembrane transport; IBA:GO_Central.
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   Pfam; PF00909; Ammonium_transp; 1.
DR   TIGRFAMs; TIGR00836; amt; 1.
DR   PROSITE; PS01219; AMMONIUM_TRANSP; 1.
PE   1: Evidence at protein level;
KW   Ammonia transport; Cell membrane; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..420
FT                   /note="Ammonium transporter Amt2"
FT                   /id="PRO_0000139765"
FT   TRANSMEM        34..54
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        71..91
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        120..140
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        149..169
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        180..200
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        220..240
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        250..270
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        273..293
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        295..315
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        339..359
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        365..385
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   SITE            186
FT                   /note="Twin-His motif. Important for optimum substrate
FT                   conductance"
FT                   /evidence="ECO:0000250|UniProtKB:P69681"
FT   SITE            334
FT                   /note="Twin-His motif. Important for optimum substrate
FT                   conductance"
FT                   /evidence="ECO:0000250|UniProtKB:P69681"
SQ   SEQUENCE   420 AA;  43786 MW;  F7AE2554D19DACA2 CRC64;
     MWGENIATAD LFANATDIHS IVQALTTLAN ASDVFFLVVM GVLVFMMQWG FAMLEGGQVR
     KKNVNNVMMK NMVDWLIGCV AWLFIGGILC SKGFDLSAFI DWWKQILGTN WPNNGLDLAS
     WFFGLVFCAT AATIVSGGVA ERIKFSAYVL ISLIITGLLY PLFVYLGPWG ASIVPWHDYA
     GSLVVHGLGG FLALGAIAAL GPRIGRFVDG RPVPILGHNI PMAVFGAFAL AIGWYGFNVG
     SSLALGDISG LVCATTTMAM AGGGIGALIA SRNDVLFTAN GIVAGLVAIC SGTDVVSPIG
     GLIIGLIAGL QVPIVYKLVE KAGLDDVCGV VPVHGTAGVI GAILTGILGL KIFGGAGGVS
     LIDQIIGAVF CIIYGTGLGY ILAKIVGIAL GGLRVSEEEE KMGLDMAEHK MPAYPEETVI