Magnesium-transporting ATPase, P-type 1 - Escherichia coli (strain K12)

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P0ABB8 (ATMA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 74. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Magnesium-transporting ATPase, P-type 1
EC=3.6.3.2

Alternative name(s):
Mg(2+) transport ATPase, P-type 1

Gene names

Name:	mgtA
Synonyms:	corB, mgt
Ordered Locus Names:	b4242, JW4201

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	898 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Mediates magnesium influx to the cytosol.
Catalytic activity	ATP + H₂O + Mg²⁺(Out) = ADP + phosphate + Mg²⁺(In).
Subcellular location	Cell inner membrane; Multi-pass membrane protein Ref.5.
Induction	Induced by low levels of proline and by osmotic shock. The leader of mgtA mRNA functions as a riboswitch, favoring transcription under low Mg²⁺ conditions. Under limiting proline levels the MgtL peptide encoded within the mgtA leader cannot be translated, thereby favoring the transcription of the mgtA ORF. Induction by osmotic shock also depends on translational regulation by MgtL Probable. Induced by low extracellular levels of Mg²⁺ via the PhoQ/PhoP two-component regulatory system. Ref.4
Sequence similarities	Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIIB subfamily. [View classification]

Ontologies

Keywords
Cellular component	Cell inner membrane Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW magnesium-importing ATPase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 898

898

Magnesium-transporting ATPase, P-type 1

PRO_0000046182

Regions

Topological domain

1 – 94

Cytoplasmic Potential

Transmembrane

95 – 115

Helical; Name=1; Potential

Topological domain

116

Extracellular Potential

Transmembrane

117 – 137

Helical; Name=2; Potential

Topological domain

138 – 287

150

Cytoplasmic Potential

Transmembrane

288 – 308

Helical; Name=3; Potential

Topological domain

309 – 317

Extracellular Potential

Transmembrane

318 – 335

Helical; Name=4; Potential

Topological domain

336 – 695

360

Cytoplasmic Potential

Transmembrane

696 – 715

Helical; Name=5; Potential

Topological domain

716 – 724

Extracellular Potential

Transmembrane

725 – 744

Helical; Name=6; Potential

Topological domain

745 – 766

Cytoplasmic Potential

Transmembrane

767 – 790

Helical; Name=7; Potential

Topological domain

791 – 799

Extracellular Potential

Transmembrane

800 – 818

Helical; Name=8; Potential

Topological domain

819 – 831

Cytoplasmic Potential

Transmembrane

832 – 851

Helical; Name=9; Potential

Topological domain

852 – 866

Extracellular Potential

Transmembrane

867 – 886

Helical; Name=10; Potential

Topological domain

887 – 898

Cytoplasmic Potential

Sites

Active site

373

4-aspartylphosphate intermediate By similarity

Metal binding

331

Magnesium Potential

Metal binding

641

Magnesium By similarity

Metal binding

645

Magnesium By similarity

Metal binding

709

Magnesium Potential

Metal binding

734

Magnesium Potential

Metal binding

738

Magnesium Potential

Experimental info

Sequence conflict

301 – 317

PVVLL…DWWEA → AGGAVNQWLHQRRLVGS in AAA97139. Ref.1

Secondary structure

898

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0ABB8 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: 2B097D67E3FFA956
Show »

FASTA

898

99,466

        10         20         30         40         50         60 
MFKEIFTRLI RHLPSRLVHR DPLPGAQQTV NTVVPPSLSA HCLKMAVMPE EELWKTFDTH 

        70         80         90        100        110        120 
PEGLNQAEVE SAREQHGENK LPAQQPSPWW VHLWVCYRNP FNILLTILGA ISYATEDLFA 

       130        140        150        160        170        180 
AGVIALMVAI STLLNFIQEA RSTKAADALK AMVSNTATVL RVINDKGENG WLEIPIDQLV 

       190        200        210        220        230        240 
PGDIIKLAAG DMIPADLRIL QARDLFVAQA SLTGESLPVE KAATTRQPEH SNPLECDTLC 

       250        260        270        280        290        300 
FMGTTVVSGT AQAMVIATGA NTWFGQLAGR VSEQESEPNA FQQGISRVSM LLIRFMLVMA 

       310        320        330        340        350        360 
PVVLLINGYT KGDWWEAALF ALSVAVGLTP EMLPMIVTST LARGAVKLSK QKVIVKHLDA 

       370        380        390        400        410        420 
IQNFGAMDIL CTDKTGTLTQ DKIVLENHTD ISGKTSERVL HSAWLNSHYQ TGLKNLLDTA 

       430        440        450        460        470        480 
VLEGTDEESA RSLASRWQKI DEIPFDFERR RMSVVVAENT EHHQLVCKGA LQEILNVCSQ 

       490        500        510        520        530        540 
VRHNGEIVPL DDIMLRKIKR VTDTLNRQGL RVVAVATKYL PAREGDYQRA DESDLILEGY 

       550        560        570        580        590        600 
IAFLDPPKET TAPALKALKA SGITVKILTG DSELVAAKVC HEVGLDAGEV VIGSDIETLS 

       610        620        630        640        650        660 
DDELANLAQR TTLFARLTPM HKERIVTLLK REGHVVGFMG DGINDAPALR AADIGISVDG 

       670        680        690        700        710        720 
AVDIAREAAD IILLEKSLMV LEEGVIEGRR TFANMLKYIK MTASSNFGNV FSVLVASAFL 

       730        740        750        760        770        780 
PFLPMLPLHL LIQNLLYDVS QVAIPFDNVD DEQIQKPQRW NPADLGRFMI FFGPISSIFD 

       790        800        810        820        830        840 
ILTFCLMWWV FHANTPETQT LFQSGWFVVG LLSQTLIVHM IRTRRVPFIQ SCASWPLMIM 

       850        860        870        880        890 
TVIVMIVGIA LPFSPLASYL QLQALPLSYF PWLVAILAGY MTLTQLVKGF YSRRYGWQ

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes." Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R. Nucleic Acids Res. 23:2105-2119(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[2]	"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], SEQUENCE REVISION TO 301-317. Strain: K12 / MG1655 / ATCC 47076.
[3]	"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.
[4]	"Identification and molecular characterization of the Mg2+ stimulon of Escherichia coli." Minagawa S., Ogasawara H., Kato A., Yamamoto K., Eguchi Y., Oshima T., Mori H., Ishihama A., Utsumi R. J. Bacteriol. 185:3696-3702(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION. Strain: K12.
[5]	"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: SUBCELLULAR LOCATION. Strain: K12 / MG1655 / ATCC 47076.
[6]	"The structure of Mg-ATPase nucleotide-binding domain at 1.6 A resolution reveals a unique ATP-binding motif." Hakansson K.O. Acta Crystallogr. D 65:1181-1186(2009) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 383-545.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U14003 Genomic DNA. Translation: AAA97139.1.
U00096 Genomic DNA. Translation: AAC77199.1.
AP009048 Genomic DNA. Translation: BAE78241.1.

PIR

E65236.

RefSeq

NP_418663.1. NC_000913.2.
YP_492382.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3GWI	X-ray	1.60	A	383-545	[»]

ProteinModelPortal

P0ABB8.

SMR

P0ABB8. Positions 44-897.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-48092N.

IntAct

P0ABB8. 2 interactions.

MINT

MINT-1285807.

STRING

511145.b4242.

Proteomic databases

PaxDb

P0ABB8.

PRIDE

P0ABB8.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC77199; AAC77199; b4242.
BAE78241; BAE78241; BAE78241.

GeneID

12932859.
948778.

KEGG

ecj:Y75_p4127.
eco:b4242.

PATRIC

32124059. VBIEscCol129921_4374.

Organism-specific databases

EchoBASE

EB2416.

EcoGene

EG12525. mgtA.

Phylogenomic databases

eggNOG

COG0474.

HOGENOM

HOG000265624.

K01531.

OMA

EEFSAPD.

ProtClustDB

PRK10517.

Enzyme and pathway databases

BioCyc

EcoCyc:MGTA-MONOMER.
ECOL316407:JW4201-MONOMER.

Gene expression databases

Genevestigator

P0ABB8.

Family and domain databases

Gene3D

1.20.1110.10. 2 hits.
2.70.150.10. 2 hits.
3.40.1110.10. 1 hit.

InterPro

IPR006068. ATPase_P-typ_cation-transptr_C.
IPR004014. ATPase_P-typ_cation-transptr_N.
IPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR023298. ATPase_P-typ_TM_dom.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR001757. Cation_transp_P_typ_ATPase.
IPR023214. HAD-like_dom.
IPR006415. Mg-transp_ATPase_P-typ.
[Graphical view]

PANTHER

PTHR24093. PTHR24093. 1 hit.
PTHR24093:SF128. PTHR24093:SF128. 1 hit.

Pfam

PF00689. Cation_ATPase_C. 1 hit.
PF00690. Cation_ATPase_N. 1 hit.
PF00122. E1-E2_ATPase. 1 hit.
PF00702. Hydrolase. 1 hit.
[Graphical view]

PRINTS

PR01836. MGATPASE.

SMART

SM00831. Cation_ATPase_N. 1 hit.
[Graphical view]

SUPFAM

SSF81660. ATPase_cation_domN. 1 hit.
SSF56784. HAD-like_dom. 1 hit.

TIGRFAMs

TIGR01524. ATPase-IIIB_Mg. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.

PROSITE

PS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P0ABB8.

Entry information

Entry name

ATMA_ECOLI

Accession

Primary (citable) accession number: P0ABB8
Secondary accession number(s): P39168, Q2M665

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 8, 2005
Last sequence update:	November 8, 2005
Last modified:	May 1, 2013
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents