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Reviewed, UniProtKB/Swiss-Prot P0ABB8 (ATMA_ECOLI)

Last modified February 9, 2010. Version 46. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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
OrganismEscherichia coli (strain K12) [Complete proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length898 AA.
Sequence statusComplete.
Protein existenceEvidence 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 extracellular levels of magnesium via the phoQ/phoP two-component regulatory system. Ref.4

Sequence similarities

Belongs to the cation transport ATPase (P-type) family. Type IIIB subfamily.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

pflBP093731EBI-556753,EBI-546682

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 898898Magnesium-transporting ATPase, P-type 1
PRO_0000046182

Regions

Topological domain1 – 9494Cytoplasmic Potential
Transmembrane95 – 115211 Potential
Topological domain1161Extracellular Potential
Transmembrane117 – 137212 Potential
Topological domain138 – 287150Cytoplasmic Potential
Transmembrane288 – 308213 Potential
Topological domain309 – 3179Extracellular Potential
Transmembrane318 – 335184 Potential
Topological domain336 – 695360Cytoplasmic Potential
Transmembrane696 – 715205 Potential
Topological domain716 – 7249Extracellular Potential
Transmembrane725 – 744206 Potential
Topological domain745 – 76622Cytoplasmic Potential
Transmembrane767 – 790247 Potential
Topological domain791 – 7999Extracellular Potential
Transmembrane800 – 818198 Potential
Topological domain819 – 83113Cytoplasmic Potential
Transmembrane832 – 851209 Potential
Topological domain852 – 86615Extracellular Potential
Transmembrane867 – 8862010 Potential
Topological domain887 – 89812Cytoplasmic Potential

Sites

Active site37314-aspartylphosphate intermediate By similarity
Metal binding3311Magnesium Potential
Metal binding6411Magnesium By similarity
Metal binding6451Magnesium By similarity
Metal binding7091Magnesium Potential
Metal binding7341Magnesium Potential
Metal binding7381Magnesium Potential

Experimental info

Sequence conflict301 – 31717PVVLL…DWWEA → AGGAVNQWLHQRRLVGS in AAA97139. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P0ABB8-1 [UniParc].

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

FASTA89899,466
        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' 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: 7610040] [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: 9278503] [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: 16738553] [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: 12813061] [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: 15919996] [Abstract]
Cited for: SUBCELLULAR LOCATION.
Strain: K12 / MG1655 / ATCC 47076.

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.
PIRE65236.
RefSeqAP_004740.1.
NP_418663.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3GWIX-ray1.60A383-545[»]
SMRP0ABB8. Positions 47-895.
ModBaseSearch...

Protein-protein interaction databases

IntActP0ABB8. 2 interactions.
STRINGP0ABB8.

Proteomic databases

PRIDEP0ABB8.

Genome annotation databases

GeneID948778.
GenomeReviewsGene locus JW4201 in contig AP009048_GR.
Gene locus b4242 in contig U00096_GR.
KEGGecj:JW4201.
eco:b4242.

Organism-specific databases

EchoBASEEB2416.
EcoGeneEG12525. mgtA.
CMRSearch...

Phylogenomic databases

eggNOGCOG0474.
HOGENOMHBG456486.
OMAHIFAKLS.

Enzyme and pathway databases

BioCycEcoCyc:MGTA-MONOMER.
ECOL168927:B4242-MONOMER.

Gene expression databases

GenevestigatorP0ABB8.

Family and domain databases

InterProIPR008250. ATPase_P-typ_ATPase-assoc-dom.
IPR004014. ATPase_P-typ_cation-transptr_N.
IPR001757. ATPase_P-typ_ion-transptr.
IPR006415. ATPase_P-typ_Mg-translocating.
IPR018303. ATPase_P-typ_P_site.
IPR005834. Dehalogen-like_hydro.
[Graphical view]
PANTHERPTHR11939:SF62. ATPase-IIIB_Mg. 1 hit.
PTHR11939. ATPase_P. 1 hit.
PfamPF00690. Cation_ATPase_N. 1 hit.
PF00122. E1-E2_ATPase. 1 hit.
PF00702. Hydrolase. 1 hit.
[Graphical view]
PRINTSPR01836. MGATPASE.
SMARTSM00831. Cation_ATPase_N. 1 hit.
[Graphical view]
TIGRFAMsTIGR01524. ATPase-IIIB_Mg. 1 hit.
TIGR01494. ATPase_P-type. 3 hits.
PROSITEPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameATMA_ECOLI
AccessionPrimary (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: February 9, 2010
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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 and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents