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Protein

Magnesium-transporting ATPase, P-type 1

Gene

mgtA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Mediates magnesium influx to the cytosol.

Catalytic activityi

ATP + H2O + Mg2+(Out) = ADP + phosphate + Mg2+(In).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi331 – 3311MagnesiumSequence analysis
Active sitei373 – 37314-aspartylphosphate intermediateBy similarity
Metal bindingi641 – 6411MagnesiumBy similarity
Metal bindingi645 – 6451MagnesiumBy similarity
Metal bindingi709 – 7091MagnesiumSequence analysis
Metal bindingi734 – 7341MagnesiumSequence analysis
Metal bindingi738 – 7381MagnesiumSequence analysis

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:MGTA-MONOMER.
ECOL316407:JW4201-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Magnesium-transporting ATPase, P-type 1 (EC:3.6.3.2)
Alternative name(s):
Mg(2+) transport ATPase, P-type 1
Gene namesi
Name:mgtA
Synonyms:corB, mgt
Ordered Locus Names:b4242, JW4201
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12525. mgtA.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 9494CytoplasmicSequence analysisAdd
BLAST
Transmembranei95 – 11521Helical; Name=1Sequence analysisAdd
BLAST
Topological domaini116 – 1161ExtracellularSequence analysis
Transmembranei117 – 13721Helical; Name=2Sequence analysisAdd
BLAST
Topological domaini138 – 287150CytoplasmicSequence analysisAdd
BLAST
Transmembranei288 – 30821Helical; Name=3Sequence analysisAdd
BLAST
Topological domaini309 – 3179ExtracellularSequence analysis
Transmembranei318 – 33518Helical; Name=4Sequence analysisAdd
BLAST
Topological domaini336 – 695360CytoplasmicSequence analysisAdd
BLAST
Transmembranei696 – 71520Helical; Name=5Sequence analysisAdd
BLAST
Topological domaini716 – 7249ExtracellularSequence analysis
Transmembranei725 – 74420Helical; Name=6Sequence analysisAdd
BLAST
Topological domaini745 – 76622CytoplasmicSequence analysisAdd
BLAST
Transmembranei767 – 79024Helical; Name=7Sequence analysisAdd
BLAST
Topological domaini791 – 7999ExtracellularSequence analysis
Transmembranei800 – 81819Helical; Name=8Sequence analysisAdd
BLAST
Topological domaini819 – 83113CytoplasmicSequence analysisAdd
BLAST
Transmembranei832 – 85120Helical; Name=9Sequence analysisAdd
BLAST
Topological domaini852 – 86615ExtracellularSequence analysisAdd
BLAST
Transmembranei867 – 88620Helical; Name=10Sequence analysisAdd
BLAST
Topological domaini887 – 89812CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 898898Magnesium-transporting ATPase, P-type 1PRO_0000046182Add
BLAST

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP0ABB8.
PRIDEiP0ABB8.

Expressioni

Inductioni

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.Curated1 Publication

Interactioni

Protein-protein interaction databases

BioGridi4261853. 9 interactions.
DIPiDIP-48092N.
IntActiP0ABB8. 2 interactions.
MINTiMINT-1285807.
STRINGi511145.b4242.

Structurei

Secondary structure

1
898
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi384 – 3896Combined sources
Helixi397 – 40913Combined sources
Helixi416 – 4238Combined sources
Helixi427 – 43610Combined sources
Beta strandi437 – 4437Combined sources
Turni447 – 4493Combined sources
Beta strandi451 – 46919Combined sources
Helixi471 – 4755Combined sources
Beta strandi478 – 4836Combined sources
Beta strandi486 – 4894Combined sources
Helixi492 – 50716Combined sources
Beta strandi511 – 52111Combined sources
Helixi529 – 5313Combined sources
Beta strandi534 – 54411Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3GWIX-ray1.60A383-545[»]
ProteinModelPortaliP0ABB8.
SMRiP0ABB8. Positions 48-848.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0ABB8.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105C52. Bacteria.
COG0474. LUCA.
HOGENOMiHOG000265624.
InParanoidiP0ABB8.
KOiK01531.
OMAiPFDFQRR.
PhylomeDBiP0ABB8.

Family and domain databases

Gene3Di1.20.1110.10. 2 hits.
2.70.150.10. 2 hits.
3.40.1110.10. 1 hit.
InterProiIPR006068. 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.
IPR023214. HAD-like_dom.
IPR006415. P-type_ATPase_IIIB.
IPR001757. P_typ_ATPase.
[Graphical view]
PfamiPF00689. Cation_ATPase_C. 1 hit.
PF00690. Cation_ATPase_N. 1 hit.
PF00122. E1-E2_ATPase. 1 hit.
[Graphical view]
PRINTSiPR01836. MGATPASE.
SMARTiSM00831. Cation_ATPase_N. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 1 hit.
SSF81660. SSF81660. 1 hit.
TIGRFAMsiTIGR01524. ATPase-IIIB_Mg. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0ABB8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFKEIFTRLI RHLPSRLVHR DPLPGAQQTV NTVVPPSLSA HCLKMAVMPE
60 70 80 90 100
EELWKTFDTH PEGLNQAEVE SAREQHGENK LPAQQPSPWW VHLWVCYRNP
110 120 130 140 150
FNILLTILGA ISYATEDLFA AGVIALMVAI STLLNFIQEA RSTKAADALK
160 170 180 190 200
AMVSNTATVL RVINDKGENG WLEIPIDQLV PGDIIKLAAG DMIPADLRIL
210 220 230 240 250
QARDLFVAQA SLTGESLPVE KAATTRQPEH SNPLECDTLC FMGTTVVSGT
260 270 280 290 300
AQAMVIATGA NTWFGQLAGR VSEQESEPNA FQQGISRVSM LLIRFMLVMA
310 320 330 340 350
PVVLLINGYT KGDWWEAALF ALSVAVGLTP EMLPMIVTST LARGAVKLSK
360 370 380 390 400
QKVIVKHLDA IQNFGAMDIL CTDKTGTLTQ DKIVLENHTD ISGKTSERVL
410 420 430 440 450
HSAWLNSHYQ TGLKNLLDTA VLEGTDEESA RSLASRWQKI DEIPFDFERR
460 470 480 490 500
RMSVVVAENT EHHQLVCKGA LQEILNVCSQ VRHNGEIVPL DDIMLRKIKR
510 520 530 540 550
VTDTLNRQGL RVVAVATKYL PAREGDYQRA DESDLILEGY IAFLDPPKET
560 570 580 590 600
TAPALKALKA SGITVKILTG DSELVAAKVC HEVGLDAGEV VIGSDIETLS
610 620 630 640 650
DDELANLAQR TTLFARLTPM HKERIVTLLK REGHVVGFMG DGINDAPALR
660 670 680 690 700
AADIGISVDG AVDIAREAAD IILLEKSLMV LEEGVIEGRR TFANMLKYIK
710 720 730 740 750
MTASSNFGNV FSVLVASAFL PFLPMLPLHL LIQNLLYDVS QVAIPFDNVD
760 770 780 790 800
DEQIQKPQRW NPADLGRFMI FFGPISSIFD ILTFCLMWWV FHANTPETQT
810 820 830 840 850
LFQSGWFVVG LLSQTLIVHM IRTRRVPFIQ SCASWPLMIM TVIVMIVGIA
860 870 880 890
LPFSPLASYL QLQALPLSYF PWLVAILAGY MTLTQLVKGF YSRRYGWQ
Length:898
Mass (Da):99,466
Last modified:November 8, 2005 - v1
Checksum:i2B097D67E3FFA956
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti301 – 31717PVVLL…DWWEA → AGGAVNQWLHQRRLVGS in AAA97139 (PubMed:7610040).CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14003 Genomic DNA. Translation: AAA97139.1.
U00096 Genomic DNA. Translation: AAC77199.1.
AP009048 Genomic DNA. Translation: BAE78241.1.
PIRiE65236.
RefSeqiNP_418663.1. NC_000913.3.
WP_000471889.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC77199; AAC77199; b4242.
BAE78241; BAE78241; BAE78241.
GeneIDi948778.
KEGGiecj:JW4201.
eco:b4242.
PATRICi32124059. VBIEscCol129921_4374.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14003 Genomic DNA. Translation: AAA97139.1.
U00096 Genomic DNA. Translation: AAC77199.1.
AP009048 Genomic DNA. Translation: BAE78241.1.
PIRiE65236.
RefSeqiNP_418663.1. NC_000913.3.
WP_000471889.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3GWIX-ray1.60A383-545[»]
ProteinModelPortaliP0ABB8.
SMRiP0ABB8. Positions 48-848.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261853. 9 interactions.
DIPiDIP-48092N.
IntActiP0ABB8. 2 interactions.
MINTiMINT-1285807.
STRINGi511145.b4242.

Proteomic databases

PaxDbiP0ABB8.
PRIDEiP0ABB8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC77199; AAC77199; b4242.
BAE78241; BAE78241; BAE78241.
GeneIDi948778.
KEGGiecj:JW4201.
eco:b4242.
PATRICi32124059. VBIEscCol129921_4374.

Organism-specific databases

EchoBASEiEB2416.
EcoGeneiEG12525. mgtA.

Phylogenomic databases

eggNOGiENOG4105C52. Bacteria.
COG0474. LUCA.
HOGENOMiHOG000265624.
InParanoidiP0ABB8.
KOiK01531.
OMAiPFDFQRR.
PhylomeDBiP0ABB8.

Enzyme and pathway databases

BioCyciEcoCyc:MGTA-MONOMER.
ECOL316407:JW4201-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0ABB8.
PROiP0ABB8.

Family and domain databases

Gene3Di1.20.1110.10. 2 hits.
2.70.150.10. 2 hits.
3.40.1110.10. 1 hit.
InterProiIPR006068. 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.
IPR023214. HAD-like_dom.
IPR006415. P-type_ATPase_IIIB.
IPR001757. P_typ_ATPase.
[Graphical view]
PfamiPF00689. Cation_ATPase_C. 1 hit.
PF00690. Cation_ATPase_N. 1 hit.
PF00122. E1-E2_ATPase. 1 hit.
[Graphical view]
PRINTSiPR01836. MGATPASE.
SMARTiSM00831. Cation_ATPase_N. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 1 hit.
SSF81660. SSF81660. 1 hit.
TIGRFAMsiTIGR01524. ATPase-IIIB_Mg. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiATMA_ECOLI
AccessioniPrimary (citable) accession number: P0ABB8
Secondary accession number(s): P39168, Q2M665
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: November 8, 2005
Last modified: September 7, 2016
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.