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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)DescriptionActionsGraphical viewLength
Metal bindingi331MagnesiumSequence analysis1
Active sitei3734-aspartylphosphate intermediateBy similarity1
Metal bindingi641MagnesiumBy similarity1
Metal bindingi645MagnesiumBy similarity1
Metal bindingi709MagnesiumSequence analysis1
Metal bindingi734MagnesiumSequence analysis1
Metal bindingi738MagnesiumSequence analysis1

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12525. mgtA.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 94CytoplasmicSequence analysisAdd BLAST94
Transmembranei95 – 115Helical; Name=1Sequence analysisAdd BLAST21
Topological domaini116ExtracellularSequence analysis1
Transmembranei117 – 137Helical; Name=2Sequence analysisAdd BLAST21
Topological domaini138 – 287CytoplasmicSequence analysisAdd BLAST150
Transmembranei288 – 308Helical; Name=3Sequence analysisAdd BLAST21
Topological domaini309 – 317ExtracellularSequence analysis9
Transmembranei318 – 335Helical; Name=4Sequence analysisAdd BLAST18
Topological domaini336 – 695CytoplasmicSequence analysisAdd BLAST360
Transmembranei696 – 715Helical; Name=5Sequence analysisAdd BLAST20
Topological domaini716 – 724ExtracellularSequence analysis9
Transmembranei725 – 744Helical; Name=6Sequence analysisAdd BLAST20
Topological domaini745 – 766CytoplasmicSequence analysisAdd BLAST22
Transmembranei767 – 790Helical; Name=7Sequence analysisAdd BLAST24
Topological domaini791 – 799ExtracellularSequence analysis9
Transmembranei800 – 818Helical; Name=8Sequence analysisAdd BLAST19
Topological domaini819 – 831CytoplasmicSequence analysisAdd BLAST13
Transmembranei832 – 851Helical; Name=9Sequence analysisAdd BLAST20
Topological domaini852 – 866ExtracellularSequence analysisAdd BLAST15
Transmembranei867 – 886Helical; Name=10Sequence analysisAdd BLAST20
Topological domaini887 – 898CytoplasmicSequence analysisAdd BLAST12

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000461821 – 898Magnesium-transporting ATPase, P-type 1Add BLAST898

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 interactors.
DIPiDIP-48092N.
IntActiP0ABB8. 2 interactors.
MINTiMINT-1285807.
STRINGi511145.b4242.

Structurei

Secondary structure

1898
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi384 – 389Combined sources6
Helixi397 – 409Combined sources13
Helixi416 – 423Combined sources8
Helixi427 – 436Combined sources10
Beta strandi437 – 443Combined sources7
Turni447 – 449Combined sources3
Beta strandi451 – 469Combined sources19
Helixi471 – 475Combined sources5
Beta strandi478 – 483Combined sources6
Beta strandi486 – 489Combined sources4
Helixi492 – 507Combined sources16
Beta strandi511 – 521Combined sources11
Helixi529 – 531Combined sources3
Beta strandi534 – 544Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3GWIX-ray1.60A383-545[»]
ProteinModelPortaliP0ABB8.
SMRiP0ABB8.
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)DescriptionActionsGraphical viewLength
Sequence conflicti301 – 317PVVLL…DWWEA → AGGAVNQWLHQRRLVGS in AAA97139 (PubMed:7610040).CuratedAdd BLAST17

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3GWIX-ray1.60A383-545[»]
ProteinModelPortaliP0ABB8.
SMRiP0ABB8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261853. 9 interactors.
DIPiDIP-48092N.
IntActiP0ABB8. 2 interactors.
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: November 2, 2016
This is version 100 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.