AMTB_BACSU
ID AMTB_BACSU Reviewed; 404 AA.
AC Q07429;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Ammonium transporter {ECO:0000303|PubMed:14600241};
DE AltName: Full=Membrane protein NrgA {ECO:0000303|PubMed:8282685};
DE AltName: Full=Protein AmtB {ECO:0000303|PubMed:14600241};
GN Name=nrgA {ECO:0000303|PubMed:8282685};
GN Synonyms=amtB {ECO:0000303|PubMed:14600241}; OrderedLocusNames=BSU36510;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBCELLULAR LOCATION.
RX PubMed=8282685; DOI=10.1128/jb.176.1.108-114.1994;
RA Wray L.V. Jr., Atkinson M.R., Fisher S.H.;
RT "The nitrogen-regulated Bacillus subtilis nrgAB operon encodes a membrane
RT protein and a protein highly similar to the Escherichia coli glnB-encoded
RT PII protein.";
RL J. Bacteriol. 176:108-114(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9353933; DOI=10.1099/00221287-143-10-3313;
RA Presecan E., Moszer I., Boursier L., Cruz Ramos H., De La Fuente V.,
RA Hullo M.-F., Lelong C., Schleich S., Sekowska A., Song B.H., Villani G.,
RA Kunst F., Danchin A., Glaser P.;
RT "The Bacillus subtilis genome from gerBC (311 degrees) to licR (334
RT degrees).";
RL Microbiology 143:3313-3328(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP INDUCTION BY TNRA.
RC STRAIN=168;
RX PubMed=10864496; DOI=10.1006/jmbi.2000.3846;
RA Wray L.V. Jr., Zalieckas J.M., Fisher S.H.;
RT "Purification and in vitro activities of the Bacillus subtilis TnrA
RT transcription factor.";
RL J. Mol. Biol. 300:29-40(2000).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, INDUCTION, AND SUBUNIT.
RC STRAIN=168;
RX PubMed=14600241; DOI=10.1099/mic.0.26512-0;
RA Detsch C., Stuelke J.;
RT "Ammonium utilization in Bacillus subtilis: transport and regulatory
RT functions of NrgA and NrgB.";
RL Microbiology 149:3289-3297(2003).
RN [6]
RP INDUCTION BY TNRA.
RX PubMed=12823818; DOI=10.1046/j.1365-2958.2003.03567.x;
RA Yoshida K., Yamaguchi H., Kinehara M., Ohki Y.-H., Nakaura Y., Fujita Y.;
RT "Identification of additional TnrA-regulated genes of Bacillus subtilis
RT associated with a TnrA box.";
RL Mol. Microbiol. 49:157-165(2003).
RN [7]
RP FUNCTION, INTERACTION WITH GLNK AND TNRA, AND DISRUPTION PHENOTYPE.
RX PubMed=17001076; DOI=10.1074/jbc.m607582200;
RA Heinrich A., Woyda K., Brauburger K., Meiss G., Detsch C., Stuelke J.,
RA Forchhammer K.;
RT "Interaction of the membrane-bound GlnK-AmtB complex with the master
RT regulator of nitrogen metabolism TnrA in Bacillus subtilis.";
RL J. Biol. Chem. 281:34909-34917(2006).
RN [8]
RP FUNCTION, INTERACTION WITH GLNK AND TNRA, AND DISRUPTION PHENOTYPE.
RX PubMed=21435182; DOI=10.1111/j.1742-4658.2011.08102.x;
RA Kayumov A., Heinrich A., Fedorova K., Ilinskaya O., Forchhammer K.;
RT "Interaction of the general transcription factor TnrA with the PII-like
RT protein GlnK and glutamine synthetase in Bacillus subtilis.";
RL FEBS J. 278:1779-1789(2011).
CC -!- FUNCTION: Functions as an ammonium and methylammonium transporter in
CC the absence of glutamine (PubMed:14600241). Required for ammonium
CC utilization at low concentrations or at low pH values, when ammonium is
CC the single nitrogen source (PubMed:14600241). Required for binding of
CC NrgB to the membrane (PubMed:14600241). Interaction between GlnK-AmtB
CC complex and TnrA protects TnrA from proteolytic degradation
CC (PubMed:17001076, PubMed:21435182). {ECO:0000269|PubMed:14600241,
CC ECO:0000269|PubMed:17001076, ECO:0000269|PubMed:21435182}.
CC -!- SUBUNIT: Interacts with NrgB for a correct localization of the latter.
CC GlnK-AmtB complex interacts with TnrA. {ECO:0000269|PubMed:17001076,
CC ECO:0000269|PubMed:21435182, ECO:0000305|PubMed:14600241}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:8282685};
CC Multi-pass membrane protein {ECO:0000305|PubMed:8282685}.
CC -!- INDUCTION: The nrgAB operon is activated by TnrA (PubMed:12823818).
CC NrgB is required for full induction of the operon under conditions of
CC ammonium limitation (PubMed:14600241, PubMed:10864496).
CC {ECO:0000269|PubMed:10864496, ECO:0000269|PubMed:12823818,
CC ECO:0000269|PubMed:14600241}.
CC -!- DISRUPTION PHENOTYPE: Cells grow poorly at pH 5.5 and not at all at pH
CC 5.0 with ammonium as their sole nitrogen source (PubMed:14600241). They
CC are unable to transport the ammonium analog methylammonium, and thus
CC probably also ammonium (PubMed:14600241). In the absence of nitrogen
CC source, cells lacking this gene do not show degradation of TnrA, which
CC is entirely soluble (PubMed:17001076, PubMed:21435182).
CC {ECO:0000269|PubMed:14600241, ECO:0000269|PubMed:17001076,
CC ECO:0000269|PubMed:21435182}.
CC -!- SIMILARITY: Belongs to the ammonia transporter channel (TC 1.A.11.2)
CC family. {ECO:0000305}.
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DR EMBL; L03216; AAA17399.1; -; Unassigned_DNA.
DR EMBL; Z82987; CAB05374.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15668.1; -; Genomic_DNA.
DR PIR; A36865; A36865.
DR RefSeq; NP_391532.1; NC_000964.3.
DR RefSeq; WP_003227757.1; NZ_JNCM01000034.1.
DR AlphaFoldDB; Q07429; -.
DR SMR; Q07429; -.
DR STRING; 224308.BSU36510; -.
DR PaxDb; Q07429; -.
DR EnsemblBacteria; CAB15668; CAB15668; BSU_36510.
DR GeneID; 936933; -.
DR KEGG; bsu:BSU36510; -.
DR PATRIC; fig|224308.179.peg.3951; -.
DR eggNOG; COG0004; Bacteria.
DR InParanoid; Q07429; -.
DR OMA; MACWNSN; -.
DR PhylomeDB; Q07429; -.
DR BioCyc; BSUB:BSU36510-MON; -.
DR Proteomes; UP000001570; 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; 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 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 Ammonia transport; Cell membrane; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..404
FT /note="Ammonium transporter"
FT /id="PRO_0000139760"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 44..64
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 227..247
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 254..274
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 277..297
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 352..372
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 404 AA; 42733 MW; 93A8C960ECAD2B9C CRC64;
MQMGDTVFMF FCALLVWLMT PGLALFYGGM VKSKNVLSTA MHSFSSIAIV SIVWVLFGYT
LAFAPGNSII GGLEWAGLKG VGFDPGDYSD TIPHSLFMMF QMTFAVLTTA IISGAFAERM
RFGAFLLFSV LWASLVYTPV AHWVWGGGWI GQLGALDFAG GNVVHISSGV AGLVLAIVLG
KRKDGTASSP HNLIYTFLGG ALIWFGWFGF NVGSALTLDG VAMYAFINTN TAAAAGIAGW
ILVEWIINKK PTMLGAVSGA IAGLVAITPA AGFVTPFASI IIGIIGGAVC FWGVFSLKKK
FGYDDALDAF GLHGIGGTWG GIATGLFATT SVNSAGADGL FYGDASLIWK QIVAIAATYV
FVFIVTFVII KIVSLFLPLR ATEEEESLGL DLTMHGEKAY QDSM
