CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003289
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Magnesium-transporting ATPase, P-type 1 
Protein Synonyms/Alias
 Mg(2+) transport ATPase, P-type 1 
Gene Name
 mgtA 
Gene Synonyms/Alias
 corB; mgt; b4242; JW4201 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
55MPEEELWKTFDTHPEacetylation[1]
166VLRVINDKGENGWLEacetylation[1]
Reference
 [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli.
 Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C.
 Mol Cell. 2013 Jul 25;51(2):265-72. [PMID: 23830618
Functional Description
 Mediates magnesium influx to the cytosol. 
Sequence Annotation
 ACT_SITE 373 373 4-aspartylphosphate intermediate (By
 METAL 331 331 Magnesium (Potential).
 METAL 641 641 Magnesium (By similarity).
 METAL 645 645 Magnesium (By similarity).
 METAL 709 709 Magnesium (Potential).
 METAL 734 734 Magnesium (Potential).
 METAL 738 738 Magnesium (Potential).  
Keyword
 3D-structure; ATP-binding; Cell inner membrane; Cell membrane; Complete proteome; Hydrolase; Magnesium; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 898 AA 
Protein Sequence
MFKEIFTRLI RHLPSRLVHR DPLPGAQQTV NTVVPPSLSA HCLKMAVMPE EELWKTFDTH 60
PEGLNQAEVE SAREQHGENK LPAQQPSPWW VHLWVCYRNP FNILLTILGA ISYATEDLFA 120
AGVIALMVAI STLLNFIQEA RSTKAADALK AMVSNTATVL RVINDKGENG WLEIPIDQLV 180
PGDIIKLAAG DMIPADLRIL QARDLFVAQA SLTGESLPVE KAATTRQPEH SNPLECDTLC 240
FMGTTVVSGT AQAMVIATGA NTWFGQLAGR VSEQESEPNA FQQGISRVSM LLIRFMLVMA 300
PVVLLINGYT KGDWWEAALF ALSVAVGLTP EMLPMIVTST LARGAVKLSK QKVIVKHLDA 360
IQNFGAMDIL CTDKTGTLTQ DKIVLENHTD ISGKTSERVL HSAWLNSHYQ TGLKNLLDTA 420
VLEGTDEESA RSLASRWQKI DEIPFDFERR RMSVVVAENT EHHQLVCKGA LQEILNVCSQ 480
VRHNGEIVPL DDIMLRKIKR VTDTLNRQGL RVVAVATKYL PAREGDYQRA DESDLILEGY 540
IAFLDPPKET TAPALKALKA SGITVKILTG DSELVAAKVC HEVGLDAGEV VIGSDIETLS 600
DDELANLAQR TTLFARLTPM HKERIVTLLK REGHVVGFMG DGINDAPALR AADIGISVDG 660
AVDIAREAAD IILLEKSLMV LEEGVIEGRR TFANMLKYIK MTASSNFGNV FSVLVASAFL 720
PFLPMLPLHL LIQNLLYDVS QVAIPFDNVD DEQIQKPQRW NPADLGRFMI FFGPISSIFD 780
ILTFCLMWWV FHANTPETQT LFQSGWFVVG LLSQTLIVHM IRTRRVPFIQ SCASWPLMIM 840
TVIVMIVGIA LPFSPLASYL QLQALPLSYF PWLVAILAGY MTLTQLVKGF YSRRYGWQ 898 
Gene Ontology
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0015444; F:magnesium-importing ATPase activity; IEA:EC.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. 
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. 
Pfam
 PF00689; Cation_ATPase_C
 PF00690; Cation_ATPase_N
 PF00122; E1-E2_ATPase
 PF00702; Hydrolase 
SMART
 SM00831; Cation_ATPase_N 
PROSITE
 PS00154; ATPASE_E1_E2 
PRINTS
 PR01836; MGATPASE.