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Entry version 135 (23 Feb 2022)
Sequence version 1 (29 Mar 2005)
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Protein

Ammonium transporter AmtB

Gene

amtB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Involved in the uptake of ammonium/ammonia (NH4+/NH3) (PubMed:14668330, PubMed:15876187, PubMed:15563598, PubMed:15361618, PubMed:16910683, PubMed:30211659, PubMed:32662768).

Transport is electrogenic (PubMed:30211659, PubMed:32662768).

Following sequestration of NH4+ at the periplasmic face, NH4+ is deprotonated and neutral NH3 is transported into the cytoplasm (PubMed:15876187, PubMed:16910683, PubMed:18362341, PubMed:19278252, PubMed:32662768).

Neutral NH3 and charged H+ are carried separately across the membrane on a unique two-lane pathway, before recombining to NH4+ inside the cell (PubMed:32662768).

In vitro can also transport the larger analogs methylamine and methylammonium (PubMed:11847102, PubMed:14668330, PubMed:12023896, PubMed:15876187, PubMed:17998534, PubMed:18362341).

Also acts as a sensor of the extracellular ammonium concentration (PubMed:14668330).

12 Publications

Miscellaneous

Specifically binds 1-palmitoyl-2-oleoyl phosphatidylglycerol (POPG), which increases protein stability (PubMed:24899312). POPG is an essential cofactor for transport activity and, in the absence of POPG, AmtB cannot complete the full translocation cycle (PubMed:30211659). Can also bind phosphatidylethanolamine and cardiolipin-like molecules, leading to positive allosteric modulation (PubMed:29507234).3 Publications

Caution

Methylammonium (MeA) has been widely used to measure ammonium transport activity because the radioactive tracer [14C]MeA is commercially available. However, MeA is a poor substrate analog for AmtB, not well suited to elucidate the mechanistic details of AmtB activity.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

In the presence of high extracellular ammonium concentrations, transport activity is inhibited by interaction with the regulatory protein GlnK (PubMed:11847102, PubMed:14668330, PubMed:16864585). Ammonium transport through AmtB is required for GlnK sequestration (PubMed:14668330). Formation of the GlnK-AmtB complex is influenced by intracellular pools of the effector molecules ATP, ADP, Mg2+ and 2-oxoglutarate (PubMed:16864585, PubMed:20639578). The rapid drop in the 2-oxoglutarate pool upon ammonium influx and a simultaneous, but transient, change in the ATP/ADP ratio promotes AmtB-GlnK complex formation (PubMed:20639578). The GlnK-AmtB interaction is also controlled by the level of intracellular glutamine and the uridylylation status of GlnK (PubMed:14668330). Inhibited by imidazole and thallium, which likely act by competitive binding to the periplasmic ammonium binding site (PubMed:18362341). Transport activity is independent of the membrane potential and of ATP hydrolysis (PubMed:15876187).6 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei182Important for the deprotonation of the ammonium cation1 Publication1
Sitei190Twin-His motif. Important for optimum substrate conductance3 Publications1
Sitei237Important for optimum substrate conductance1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei241Ammonium1 Publication1
Sitei340Twin-His motif. Important for optimum substrate conductance3 Publications1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Biological processAmmonia transport, Transport

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:AMTB-MONOMER

Protein family/group databases

Transport Classification Database

More...
TCDBi
1.A.11.1.1, the ammonium transporter channel (amt) family

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Ammonium transporter AmtB2 Publications
Alternative name(s):
Ammonia channel AmtB2 Publications
Ammonium channel AmtB1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:amtB1 Publication
Synonyms:ybaG
Ordered Locus Names:b0451, JW0441
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini23 – 32Periplasmic3 Publications10
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei33 – 54Helical3 PublicationsAdd BLAST22
Topological domaini55 – 65Cytoplasmic3 PublicationsAdd BLAST11
Transmembranei66 – 90Helical3 PublicationsAdd BLAST25
Topological domaini91 – 119Periplasmic3 PublicationsAdd BLAST29
Transmembranei120 – 142Helical3 PublicationsAdd BLAST23
Topological domaini143 – 146Cytoplasmic3 Publications4
Transmembranei147 – 171Helical3 PublicationsAdd BLAST25
Topological domaini172 – 185Periplasmic3 PublicationsAdd BLAST14
Transmembranei186 – 201Helical3 PublicationsAdd BLAST16
Topological domaini202 – 221Cytoplasmic3 PublicationsAdd BLAST20
Transmembranei222 – 241Helical3 PublicationsAdd BLAST20
Topological domaini242 – 248Periplasmic3 Publications7
Transmembranei249 – 273Helical3 PublicationsAdd BLAST25
Topological domaini274 – 279Cytoplasmic3 Publications6
Transmembranei280 – 300Helical3 PublicationsAdd BLAST21
Topological domaini301 – 302Periplasmic3 Publications2
Transmembranei303 – 321Helical3 PublicationsAdd BLAST19
Topological domaini322 – 333Cytoplasmic3 PublicationsAdd BLAST12
Transmembranei334 – 355Helical3 PublicationsAdd BLAST22
Topological domaini356 – 370Periplasmic3 PublicationsAdd BLAST15
Transmembranei371 – 399Helical3 PublicationsAdd BLAST29
Topological domaini400 – 428Cytoplasmic4 PublicationsAdd BLAST29

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi129F → A: 1.4-fold increase in transport activity with methylammonium as substrate. Shows 80% inhibition by thallium. 1 Publication1
Mutagenesisi170W → A: 2.5-fold increase in transport activity with methylammonium as substrate. Shows 80% inhibition by thallium. 1 Publication1
Mutagenesisi170W → L: 5-fold increase in transport activity with methylammonium as substrate. 1 Publication1
Mutagenesisi178H → A: Abolishes the positive allosteric modulation observed for binding phosphatidylethanolamine and cardiolipin-like molecules. 1 Publication1
Mutagenesisi182D → A: Impairs ammonium transport. Loss of activity with methylammonium as substrate. GlnK remains fully uridylylated and localizes to the cytoplasm during a transient increase in extracellular ammonium. 2 Publications1
Mutagenesisi182D → E: Impairs ammonium transport. Retains 71% of wild-type activity with methylammonium as substrate. Allows some complex formation with GlnK during a transient increase in extracellular ammonium. 2 Publications1
Mutagenesisi190H → A: Does not prevent transport of ammonia. Loss of transport activity with methylammonium and methylamine. Shows normal GlnK-AmtB complex formation after ammonium shock. Loss of both methylamine and ammonia transport; when associated with A-340. 3 Publications1
Mutagenesisi190H → D, F, N or Q: Loss of transport activity with methylammonium as substrate. Shows normal GlnK-AmtB complex formation after ammonium shock. 1 Publication1
Mutagenesisi190H → E: Retains 25% of transport activity with methylammonium as substrate. Shows normal GlnK-AmtB complex formation after ammonium shock. 1 Publication1
Mutagenesisi190H → K: Loss of transport activity with methylammonium as substrate. 1 Publication1
Mutagenesisi190H → T: Loss of transport activity with methylammonium as substrate. Cannot form GlnK-AmtB complex after ammonium shock. 1 Publication1
Mutagenesisi234W → A: Loss of transport activity with methylammonium as substrate. 1 Publication1
Mutagenesisi234W → F: Retains 80% of transport activity with methylammonium as substrate. 1 Publication1
Mutagenesisi237F → A, H, L, Q, S or W: Loss of transport activity with methylammonium as substrate. 1 Publication1
Mutagenesisi241S → A: 4-fold increase in transport activity with methylammonium as substrate. Shows 80% inhibition by thallium. 1 Publication1
Mutagenesisi340H → A: Does not prevent transport of ammonia. Loss of transport activity with methylammonium and methylamine. Shows normal GlnK-AmtB complex formation after ammonium shock. Loss of both methylamine and ammonia transport; when associated with A-190. 3 Publications1
Mutagenesisi340H → E or F: Loss of transport activity with methylammonium as substrate. Shows normal GlnK-AmtB complex formation after ammonium shock. 1 Publication1
Mutagenesisi340H → T: Loss of transport activity with methylammonium as substrate. 1 Publication1
Mutagenesisi404 – 428Missing : Reduced methylamine transport activity. Cannot interact with GlnK. 1 PublicationAdd BLAST25
Mutagenesisi405 – 428Missing : Retains 27% of wild-type activity. 1 PublicationAdd BLAST24
Mutagenesisi406R → A: Almost loss of activity. 1 Publication1
Mutagenesisi415G → A, D, E, N or R: Almost loss of activity. 1 Publication1
Mutagenesisi421 – 428Missing : Retains 43% of wild-type activity. 1 Publication8
Mutagenesisi426 – 428Missing : Retains 21% of wild-type activity. 1 Publication3
Mutagenesisi426Y → G: Retains 11% of wild-type activity. 1 Publication1
Mutagenesisi427 – 428Missing : Retains 12% of wild-type activity. 1 Publication2
Mutagenesisi427N → A: Retains 33% of wild-type activity. 1 Publication1
Mutagenesisi427N → D: No change in activity. 1 Publication1
Mutagenesisi427N → Q: Retains 28% of wild-type activity. 1 Publication1
Mutagenesisi428Missing : No change in activity. 1 Publication1

Chemistry databases

Drug and drug target database

More...
DrugBanki
DB04147, Dodecyldimethylamine N-oxide
DB01828, Methylamine

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 221 PublicationAdd BLAST22
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000000130723 – 428Ammonium transporter AmtBAdd BLAST406

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P69681

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P69681

PRoteomics IDEntifications database

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PRIDEi
P69681

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homotrimer (PubMed:12023896, PubMed:15563598, PubMed:15361618, PubMed:17040913). In response to elevation of the extracellular ammonium concentration, interacts and forms a complex with GlnK (PubMed:10637624, PubMed:11847102, PubMed:14668330, PubMed:17220269, PubMed:17190799, PubMed:16864585, PubMed:20639578).

Interacts with GlnK with a stoichiometry of AmtB3:GlnK3 (PubMed:17220269, PubMed:17190799). Sequestration of GlnK is reversible (PubMed:14668330).

11 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

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BioGRIDi
4259856, 9 interactors
849473, 3 interactors

Database of interacting proteins

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DIPi
DIP-29874N

Protein interaction database and analysis system

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IntActi
P69681, 3 interactors

STRING: functional protein association networks

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STRINGi
511145.b0451

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1428
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

The Protein Circular Dichroism Data Bank

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PCDDBi
P69681

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P69681

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P69681

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The C-terminal cytoplasmic domain plays a significant role in normal function and it might also mediate co-operativity between the three subunits (PubMed:17453422). The C-terminal cytoplasmic domain is also required for interaction with the T-loop of GlnK (PubMed:11847102, PubMed:17190799).3 Publications

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
COG0004, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_000445_33_0_6

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P69681

Database for complete collections of gene phylogenies

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PhylomeDBi
P69681

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.10.3430.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR029020, Ammonium/urea_transptr
IPR001905, Ammonium_transpt
IPR018047, Ammonium_transpt_CS
IPR024041, NH4_transpt_AmtB-like_dom

The PANTHER Classification System

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PANTHERi
PTHR43029, PTHR43029, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF00909, Ammonium_transp, 1 hit

TIGRFAMs; a protein family database

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TIGRFAMsi
TIGR00836, amt, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS01219, AMMONIUM_TRANSP, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P69681-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKIATIKTGL ASLAMLPGLV MAAPAVADKA DNAFMMICTA LVLFMTIPGI
60 70 80 90 100
ALFYGGLIRG KNVLSMLTQV TVTFALVCIL WVVYGYSLAF GEGNNFFGNI
110 120 130 140 150
NWLMLKNIEL TAVMGSIYQY IHVAFQGSFA CITVGLIVGA LAERIRFSAV
160 170 180 190 200
LIFVVVWLTL SYIPIAHMVW GGGLLASHGA LDFAGGTVVH INAAIAGLVG
210 220 230 240 250
AYLIGKRVGF GKEAFKPHNL PMVFTGTAIL YIGWFGFNAG SAGTANEIAA
260 270 280 290 300
LAFVNTVVAT AAAILGWIFG EWALRGKPSL LGACSGAIAG LVGVTPACGY
310 320 330 340 350
IGVGGALIIG VVAGLAGLWG VTMLKRLLRV DDPCDVFGVH GVCGIVGCIM
360 370 380 390 400
TGIFAASSLG GVGFAEGVTM GHQLLVQLES IAITIVWSGV VAFIGYKLAD
410 420
LTVGLRVPEE QEREGLDVNS HGENAYNA
Length:428
Mass (Da):44,515
Last modified:March 29, 2005 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iB4AC96F0E5AE2B59
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti377 – 382QLESIA → SWKASP in M63308 (PubMed:1645722).Curated6

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
U40429 Genomic DNA Translation: AAD14837.1
U82664 Genomic DNA Translation: AAB40207.1
U00096 Genomic DNA Translation: AAC73554.1
AP009048 Genomic DNA Translation: BAE76231.1
M63308 Genomic DNA No translation available.

Protein sequence database of the Protein Information Resource

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PIRi
A90692
C64775
E85542

NCBI Reference Sequences

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RefSeqi
NP_414985.1, NC_000913.3
WP_000685029.1, NZ_STEB01000007.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

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EnsemblBacteriai
AAC73554; AAC73554; b0451
BAE76231; BAE76231; BAE76231

Database of genes from NCBI RefSeq genomes

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GeneIDi
67416474
945084

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
ecj:JW0441
eco:b0451

Pathosystems Resource Integration Center (PATRIC)

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PATRICi
fig|1411691.4.peg.1824

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U40429 Genomic DNA Translation: AAD14837.1
U82664 Genomic DNA Translation: AAB40207.1
U00096 Genomic DNA Translation: AAC73554.1
AP009048 Genomic DNA Translation: BAE76231.1
M63308 Genomic DNA No translation available.
PIRiA90692
C64775
E85542
RefSeqiNP_414985.1, NC_000913.3
WP_000685029.1, NZ_STEB01000007.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1U77X-ray2.00A23-407[»]
1U7CX-ray1.85A23-407[»]
1U7GX-ray1.40A23-407[»]
1XQEX-ray2.10A23-428[»]
1XQFX-ray1.80A23-428[»]
2NMRX-ray2.10A23-428[»]
2NOPX-ray2.00A23-428[»]
2NOWX-ray2.20A23-428[»]
2NPCX-ray2.10A23-428[»]
2NPDX-ray2.10A23-428[»]
2NPEX-ray2.10A23-428[»]
2NPGX-ray2.00A23-428[»]
2NPJX-ray2.00A23-428[»]
2NPKX-ray2.00A23-428[»]
2NS1X-ray1.96A23-428[»]
2NUUX-ray2.50A/B/C/D/E/F25-428[»]
3C1GX-ray2.30A23-428[»]
3C1HX-ray2.20A23-428[»]
3C1IX-ray2.30A23-428[»]
3C1JX-ray2.00A23-428[»]
6B21X-ray2.45A26-428[»]
PCDDBiP69681
SMRiP69681
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4259856, 9 interactors
849473, 3 interactors
DIPiDIP-29874N
IntActiP69681, 3 interactors
STRINGi511145.b0451

Chemistry databases

DrugBankiDB04147, Dodecyldimethylamine N-oxide
DB01828, Methylamine

Protein family/group databases

TCDBi1.A.11.1.1, the ammonium transporter channel (amt) family

Proteomic databases

jPOSTiP69681
PaxDbiP69681
PRIDEiP69681

Genome annotation databases

EnsemblBacteriaiAAC73554; AAC73554; b0451
BAE76231; BAE76231; BAE76231
GeneIDi67416474
945084
KEGGiecj:JW0441
eco:b0451
PATRICifig|1411691.4.peg.1824

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

More...
EchoBASEi
EB1768

Phylogenomic databases

eggNOGiCOG0004, Bacteria
HOGENOMiCLU_000445_33_0_6
InParanoidiP69681
PhylomeDBiP69681

Enzyme and pathway databases

BioCyciEcoCyc:AMTB-MONOMER

Miscellaneous databases

EvolutionaryTraceiP69681

Protein Ontology

More...
PROi
PR:P69681

Family and domain databases

Gene3Di1.10.3430.10, 1 hit
InterProiView protein in InterPro
IPR029020, Ammonium/urea_transptr
IPR001905, Ammonium_transpt
IPR018047, Ammonium_transpt_CS
IPR024041, NH4_transpt_AmtB-like_dom
PANTHERiPTHR43029, PTHR43029, 1 hit
PfamiView protein in Pfam
PF00909, Ammonium_transp, 1 hit
TIGRFAMsiTIGR00836, amt, 1 hit
PROSITEiView protein in PROSITE
PS01219, AMMONIUM_TRANSP, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiAMTB_ECOLI
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P69681
Secondary accession number(s): P37905, Q2MBX5
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: March 29, 2005
Last modified: February 23, 2022
This is version 135 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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