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Protein

Magnesium-transporting ATPase, P-type 1

Gene

mgtA

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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 bindingi335MagnesiumSequence analysis1
Active sitei3774-aspartylphosphate intermediateBy similarity1
Metal bindingi645MagnesiumBy similarity1
Metal bindingi649MagnesiumBy similarity1
Metal bindingi713MagnesiumSequence analysis1
Metal bindingi738MagnesiumSequence analysis1
Metal bindingi742MagnesiumSequence analysis1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Transport

Keywords - Ligandi

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

Protein family/group databases

TCDBi3.A.3.4.1. the p-type atpase (p-atpase) superfamily.

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
Ordered Locus Names:STM4456
OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Taxonomic identifieri99287 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeSalmonella
Proteomesi
  • UP000001014 Componenti: Chromosome

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 98CytoplasmicSequence analysisAdd BLAST98
Transmembranei99 – 119Helical; Name=1Sequence analysisAdd BLAST21
Topological domaini120ExtracellularSequence analysis1
Transmembranei121 – 141Helical; Name=2Sequence analysisAdd BLAST21
Topological domaini142 – 291CytoplasmicSequence analysisAdd BLAST150
Transmembranei292 – 312Helical; Name=3Sequence analysisAdd BLAST21
Topological domaini313 – 321ExtracellularSequence analysis9
Transmembranei322 – 339Helical; Name=4Sequence analysisAdd BLAST18
Topological domaini340 – 699CytoplasmicSequence analysisAdd BLAST360
Transmembranei700 – 719Helical; Name=5Sequence analysisAdd BLAST20
Topological domaini720 – 728ExtracellularSequence analysis9
Transmembranei729 – 748Helical; Name=6Sequence analysisAdd BLAST20
Topological domaini749 – 770CytoplasmicSequence analysisAdd BLAST22
Transmembranei771 – 794Helical; Name=7Sequence analysisAdd BLAST24
Topological domaini795 – 803ExtracellularSequence analysis9
Transmembranei804 – 822Helical; Name=8Sequence analysisAdd BLAST19
Topological domaini823 – 835CytoplasmicSequence analysisAdd BLAST13
Transmembranei836 – 855Helical; Name=9Sequence analysisAdd BLAST20
Topological domaini856 – 870ExtracellularSequence analysisAdd BLAST15
Transmembranei871 – 890Helical; Name=10Sequence analysisAdd BLAST20
Topological domaini891 – 902CytoplasmicSequence 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_00000461841 – 902Magnesium-transporting ATPase, P-type 1Add BLAST902

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP36640.

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+.Curated1 Publication

Interactioni

Protein-protein interaction databases

STRINGi99287.STM4456.

Structurei

3D structure databases

ProteinModelPortaliP36640.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105C52. Bacteria.
COG0474. LUCA.
HOGENOMiHOG000265624.
KOiK01531.
OMAiWINILTH.
PhylomeDBiP36640.

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.

P36640-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLKIITRQLF ARLNRHLPYR LVHRDPLPGA QTAVNATIPP SLSERCLKVA
60 70 80 90 100
AMEQETLWRV FDTHPEGLNA AEVTRAREKH GENRLPAQKP SPWWVHLWVC
110 120 130 140 150
YRNPFNILLT ILGGISYATE DLFAAGVIAL MVGISTLLNF VQEARSTKAA
160 170 180 190 200
DALKAMVSNT ATVLRVINEN GENAWLELPI DQLVPGDIIK LAAGDMIPAD
210 220 230 240 250
LRIIQARDLF VAQASLTGES LPVEKVAATR EPRQNNPLEC DTLCFMGTNV
260 270 280 290 300
VSGTAQAVVM ATGAGTWFGQ LAGRVSEQDN EQNAFQKGIS RVSMLLIRFM
310 320 330 340 350
LVMAPVVLII NGYTKGDWWE AALFALSVAV GLTPEMLPMI VTSTLARGAV
360 370 380 390 400
KLSKQKVIVK HLDAIQNFGA MDILCTDKTG TLTQDKIVLE NHTDISGKPS
410 420 430 440 450
EHVLHCAWLN SHYQTGLKNL LDTAVLEGVD ETAARQLSGR WQKIDEIPFD
460 470 480 490 500
FERRRMSVVV AEDSNVHQLV CKGALQEILN VCTQVRHNGD IVPLDDNMLR
510 520 530 540 550
RVKRVTDTLN RQGLRVVAVA TKYLPAREGD YQRIDESDLI LEGYIAFLDP
560 570 580 590 600
PKETTAPALK ALKASGITVK ILTGDSELVA AKVCHEVGLD AGDVIIGSDI
610 620 630 640 650
EGLSDDALAA LAARTTLFAR LTPMHKERIV TLLKREGHVV GFMGDGINDA
660 670 680 690 700
PALRAADIGI SVDGAVDIAR EAADIILLEK SLMVLEEGVI EGRRTFSNML
710 720 730 740 750
KYIKMTASSN FGNVFSVLVA SAFLPFLPML PLHLLIQNLL YDVSQVAIPF
760 770 780 790 800
DNVDEEQIQK PQRWNPADLG RFMVFFGPIS SIFDILTFCL MWWVFHANTP
810 820 830 840 850
ETQTLFQSGW FVVGLLSQTL IVHMIRTRRL PFIQSRAAWP LMAMTLLVMV
860 870 880 890 900
VGVSLPFSPL ASYLQLQALP LSYFPWLIAI LVGYMTLTQL VKGFYSRRYG

WQ
Length:902
Mass (Da):99,783
Last modified:June 1, 1994 - v1
Checksum:i3D2712E9A074C957
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U07843 Genomic DNA. Translation: AAA68988.1.
AE006468 Genomic DNA. Translation: AAL23275.1.
PIRiB57147.
RefSeqiNP_463316.1. NC_003197.1.
WP_001738655.1. NC_003197.1.

Genome annotation databases

EnsemblBacteriaiAAL23275; AAL23275; STM4456.
GeneIDi1255982.
KEGGistm:STM4456.
PATRICi32387851. VBISalEnt20916_4689.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U07843 Genomic DNA. Translation: AAA68988.1.
AE006468 Genomic DNA. Translation: AAL23275.1.
PIRiB57147.
RefSeqiNP_463316.1. NC_003197.1.
WP_001738655.1. NC_003197.1.

3D structure databases

ProteinModelPortaliP36640.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi99287.STM4456.

Protein family/group databases

TCDBi3.A.3.4.1. the p-type atpase (p-atpase) superfamily.

Proteomic databases

PaxDbiP36640.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL23275; AAL23275; STM4456.
GeneIDi1255982.
KEGGistm:STM4456.
PATRICi32387851. VBISalEnt20916_4689.

Phylogenomic databases

eggNOGiENOG4105C52. Bacteria.
COG0474. LUCA.
HOGENOMiHOG000265624.
KOiK01531.
OMAiWINILTH.
PhylomeDBiP36640.

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_SALTY
AccessioniPrimary (citable) accession number: P36640
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: November 2, 2016
This is version 131 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

Complete proteome, Reference proteome

Documents

  1. 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.