P69681 (AMTB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ammonia channel

Alternative name(s):
Ammonia transporter

Gene names

Name:	amtB
Synonyms:	ybaG
Ordered Locus Names:	b0451, JW0441

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	428 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in the uptake of ammonia.
Subunit structure	Homotrimer. May interact with GlnK. Ref.9
Subcellular location	Cell inner membrane; Multi-pass membrane protein.
Sequence similarities	Belongs to the ammonia transporter channel (TC 1.A.11.2) family. [View classification]

Ontologies

Keywords
Biological process	Ammonia transport Transport
Cellular component	Cell inner membrane Cell membrane Membrane
Domain	Signal Transmembrane Transmembrane helix
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	ammonium transport Inferred from direct assay PubMed 19273840. Source: UniProtKB carbon dioxide transport Inferred from direct assay PubMed 19273840. Source: UniProtKB
Cellular_component	integral to plasma membrane Inferred from direct assay PubMed 16630265. Source: EcoCyc
Molecular_function	ammonia transmembrane transporter activity Inferred from direct assay PubMed 19273840. Source: UniProtKB ammonium transmembrane transporter activity Inferred from electronic annotation. Source: InterPro uniporter activity Inferred from mutant phenotype PubMed 9618533. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 22

22

Ref.12

Chain

23 – 428

406

Ammonia channel

PRO_0000001307

Regions

Topological domain

23 – 28

6

Periplasmic Ref.7 Ref.10

Transmembrane

29 – 55

27

Helical; Name=1

Topological domain

56 – 59

4

Cytoplasmic Ref.7 Ref.10

Transmembrane

60 – 90

31

Helical; Name=2

Topological domain

91 – 118

28

Periplasmic Ref.7 Ref.10

Transmembrane

119 – 141

23

Helical; Name=3

Topological domain

142 – 146

5

Cytoplasmic Ref.7 Ref.10

Transmembrane

147 – 170

24

Helical; Name=4

Topological domain

171 – 184

14

Periplasmic Ref.7 Ref.10

Transmembrane

185 – 203

19

Helical; Name=5

Topological domain

204 – 215

12

Cytoplasmic Ref.7 Ref.10

Transmembrane

216 – 242

27

Helical; Name=6

Topological domain

243 – 245

3

Periplasmic Ref.7 Ref.10

Transmembrane

246 – 275

30

Helical; Name=7

Topological domain

276 – 279

4

Cytoplasmic Ref.7 Ref.10

Transmembrane

280 – 294

15

Helical; Name=8

Topological domain

295 – 302

8

Periplasmic Ref.7 Ref.10

Transmembrane

303 – 328

26

Helical; Name=9

Topological domain

329 – 332

4

Cytoplasmic Ref.7 Ref.10

Transmembrane

333 – 354

22

Helical; Name=10

Topological domain

355 – 369

15

Periplasmic Ref.7 Ref.10

Transmembrane

370 – 402

33

Helical; Name=11

Topological domain

403 – 428

26

Cytoplasmic Ref.7 Ref.10

Experimental info

Sequence conflict

377 – 382

6

QLESIA → SWKASP in M63308. Ref.5

Secondary structure

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428

Helix Strand Turn

Details...

Helix

29 – 46

18

Helix

49 – 55

7

Helix

60 – 83

24

Helix

85 – 90

6

Beta strand

94 – 96

3

Beta strand

100 – 102

3

Helix

103 – 105

3

Helix

119 – 141

23

Helix

142 – 144

3

Helix

147 – 160

14

Helix

162 – 170

9

Beta strand

171 – 173

3

Helix

174 – 178

5

Turn

186 – 189

4

Helix

190 – 203

14

Turn

208 – 212

5

Helix

217 – 219

3

Helix

220 – 239

20

Helix

240 – 242

3

Beta strand

243 – 246

4

Helix

247 – 275

29

Helix

280 – 294

15

Turn

295 – 300

6

Helix

303 – 328

26

Helix

333 – 335

3

Helix

336 – 354

19

Helix

357 – 359

3

Helix

370 – 402

33

Helix

409 – 414

6

Helix

416 – 421

6

Sequences

	Sequence		Length	Mass (Da)
	P69681 [UniParc]. Last modified March 29, 2005. Version 1. Checksum: B4AC96F0E5AE2B59	FASTA	428	44,515
	10 20 30 40 50 60 MKIATIKTGL ASLAMLPGLV MAAPAVADKA DNAFMMICTA LVLFMTIPGI ALFYGGLIRG 70 80 90 100 110 120 KNVLSMLTQV TVTFALVCIL WVVYGYSLAF GEGNNFFGNI NWLMLKNIEL TAVMGSIYQY 130 140 150 160 170 180 IHVAFQGSFA CITVGLIVGA LAERIRFSAV LIFVVVWLTL SYIPIAHMVW GGGLLASHGA 190 200 210 220 230 240 LDFAGGTVVH INAAIAGLVG AYLIGKRVGF GKEAFKPHNL PMVFTGTAIL YIGWFGFNAG 250 260 270 280 290 300 SAGTANEIAA LAFVNTVVAT AAAILGWIFG EWALRGKPSL LGACSGAIAG LVGVTPACGY 310 320 330 340 350 360 IGVGGALIIG VVAGLAGLWG VTMLKRLLRV DDPCDVFGVH GVCGIVGCIM TGIFAASSLG 370 380 390 400 410 420 GVGFAEGVTM GHQLLVQLES IAITIVWSGV VAFIGYKLAD LTVGLRVPEE QEREGLDVNS HGENAYNA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"An alternative PII protein in the regulation of glutamine synthetase in Escherichia coli." van Heeswijk W.C., Hoving S., Molenaar D., Stegeman B., Kahn D., Westerhoff H.V. Mol. Microbiol. 21:133-146(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]	"Sequence of minutes 4-25 of Escherichia coli." Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W. Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"Cloning, sequencing, and characterization of Escherichia coli thioesterase II." Naggert J., Narasimhan M.L., Deveaux L., Cho H., Randhawa Z.I., Cronan J.E. Jr., Green B.N., Smith S. J. Biol. Chem. 266:11044-11050(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 377-428. Strain: K12.
[6]	"Intrinsic and extrinsic approaches for detecting genes in a bacterial genome." Borodovsky M., Rudd K.E., Koonin E.V. Nucleic Acids Res. 22:4756-4767(1994) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION.
[7]	"Membrane topology of the Mep/Amt family of ammonium transporters." Thomas G.H., Mullins J.G., Merrick M. Mol. Microbiol. 37:331-344(2000) [PubMed] [Europe PMC] [Abstract] Cited for: TOPOLOGY.
[8]	"The glnKamtB operon. A conserved gene pair in prokaryotes." Thomas G.H., Coutts G., Merrick M. Trends Genet. 16:11-14(2000) [PubMed] [Europe PMC] [Abstract] Cited for: POSSIBLE INTERACTION WITH GLNK.
[9]	"Purification of the Escherichia coli ammonium transporter AmtB reveals a trimeric stoichiometry." Blakey D., Leech A., Thomas G.H., Coutts G., Findlay K., Merrick M. Biochem. J. 364:527-535(2002) [PubMed] [Europe PMC] [Abstract] Cited for: SUBUNIT.
[10]	"Global topology analysis of the Escherichia coli inner membrane proteome." Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G. Science 308:1321-1323(2005) [PubMed] [Europe PMC] [Abstract] Cited for: TOPOLOGY [LARGE SCALE ANALYSIS]. Strain: K12 / MG1655 / ATCC 47076.
[11]	"The mechanism of ammonia transport based on the crystal structure of AmtB of Escherichia coli." Zheng L., Kostrewa D., Berneche S., Winkler F.K., Li X.-D. Proc. Natl. Acad. Sci. U.S.A. 101:17090-17095(2004) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
[12]	"Mechanism of ammonia transport by Amt/MEP/Rh: structure of AmtB at 1.35 A." Khademi S., O'Connell J.D. III, Remis J., Robles-Colmenares Y., Miercke L.J., Stroud R.M. Science 305:1587-1594(2004) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS), PROTEIN SEQUENCE OF N-TERMINUS.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

PIR

A90692.
C64775.
E85542.

RefSeq

NP_414985.1. NC_000913.2.
YP_488743.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1U77	X-ray	2.00	A	23-407	[»]
1U7C	X-ray	1.85	A	23-407	[»]
1U7G	X-ray	1.40	A	23-407	[»]
1XQE	X-ray	2.10	A	23-428	[»]
1XQF	X-ray	1.80	A	23-428	[»]
2NMR	X-ray	2.10	A	23-428	[»]
2NOP	X-ray	2.00	A	23-428	[»]
2NOW	X-ray	2.20	A	23-428	[»]
2NPC	X-ray	2.10	A	23-428	[»]
2NPD	X-ray	2.10	A	23-428	[»]
2NPE	X-ray	2.10	A	23-428	[»]
2NPG	X-ray	2.00	A	23-428	[»]
2NPJ	X-ray	2.00	A	23-428	[»]
2NPK	X-ray	2.00	A	23-428	[»]
2NS1	X-ray	1.96	A	23-428	[»]
2NUU	X-ray	2.50	A/B/C/D/E/F	25-428	[»]
3C1G	X-ray	2.30	A	23-428	[»]
3C1H	X-ray	2.20	A	23-428	[»]
3C1I	X-ray	2.30	A	23-428	[»]
3C1J	X-ray	2.00	A	23-428	[»]

ProteinModelPortal

P69681.

SMR

P69681. Positions 25-428.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29874N.

STRING

511145.b0451.

Protein family/group databases

TCDB

1.A.11.1.1. ammonia transporter channel (Amt) family.

Proteomic databases

PaxDb

P69681.

PRIDE

P69681.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC73554; AAC73554; b0451.
BAE76231; BAE76231; BAE76231.

GeneID

12930862.
945084.

KEGG

ecj:Y75_p0439.
eco:b0451.

PATRIC

32116057. VBIEscCol129921_0470.

Organism-specific databases

EchoBASE

EB1768.

EcoGene

EG11821. amtB.

Phylogenomic databases

eggNOG

COG0004.

HOGENOM

HOG000017736.

KO

K03320.

OMA

FAMITPA.

ProtClustDB

PRK10666.

Enzyme and pathway databases

BioCyc

EcoCyc:AMTB-MONOMER.
ECOL316407:JW0441-MONOMER.

Gene expression databases

Genevestigator

P69681.

Family and domain databases

InterPro

IPR001905. Ammonium_transpt.
IPR018047. Ammonium_transpt_CS.
IPR024041. NH4_transpt_AmtB-like_dom.
[Graphical view]

PANTHER

PTHR11730. PTHR11730. 1 hit.

Pfam

PF00909. Ammonium_transp. 1 hit.
[Graphical view]

SUPFAM

SSF111352. RH_like_transpt. 1 hit.

TIGRFAMs

TIGR00836. amt. 1 hit.

PROSITE

PS01219. AMMONIUM_TRANSP. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P69681.

Entry information

Entry name

AMTB_ECOLI

Accession

Primary (citable) accession number: P69681
Secondary accession number(s): P37905, Q2MBX5

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 29, 2005
Last sequence update:	March 29, 2005
Last modified:	May 1, 2013
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program