CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-013522
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Copper-exporting P-type ATPase A 
Protein Synonyms/Alias
  
Gene Name
 copA 
Gene Synonyms/Alias
 ybaR; b0484; JW0473 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
19LSCGHCVKRVKESLEacetylation[1]
169EAIEDDAKRRERQQEacetylation[1]
316RSSKALEKLLDLTPPacetylation[1]
334LVTDEGEKSVPLAEVacetylation[1]
539KPQVVAVKTFADVDEacetylation[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
 Involved in copper export. May also be involved in silver export. 
Sequence Annotation
 DOMAIN 4 65 HMA 1.
 DOMAIN 100 163 HMA 2.
 ACT_SITE 523 523 4-aspartylphosphate intermediate
 METAL 14 14 Copper (Potential).
 METAL 17 17 Copper (Potential).
 METAL 110 110 Copper (Potential).
 METAL 113 113 Copper (Potential).
 METAL 720 720 Magnesium (By similarity).
 METAL 724 724 Magnesium (By similarity).  
Keyword
 ATP-binding; Cell membrane; Complete proteome; Copper; Copper transport; Direct protein sequencing; Hydrolase; Ion transport; Magnesium; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 834 AA 
Protein Sequence
MSQTIDLTLD GLSCGHCVKR VKESLEQRPD VEQADVSITE AHVTGTASAE QLIETIKQAG 60
YDASVSHPKA KPLAESSIPS EALTAVSEAL PAATADDDDS QQLLLSGMSC ASCVTRVQNA 120
LQSVPGVTQA RVNLAERTAL VMGSASPQDL VQAVEKAGYG AEAIEDDAKR RERQQETAVA 180
TMKRFRWQAI VALAVGIPVM VWGMIGDNMM VTADNRSLWL VIGLITLAVM VFAGGHFYRS 240
AWKSLLNGAA TMDTLVALGT GVAWLYSMSV NLWPQWFPME ARHLYYEASA MIIGLINLGH 300
MLEARARQRS SKALEKLLDL TPPTARLVTD EGEKSVPLAE VQPGMLLRLT TGDRVPVDGE 360
ITQGEAWLDE AMLTGEPIPQ QKGEGDSVHA GTVVQDGSVL FRASAVGSHT TLSRIIRMVR 420
QAQSSKPEIG QLADKISAVF VPVVVVIALV SAAIWYFFGP APQIVYTLVI ATTVLIIACP 480
CALGLATPMS IISGVGRAAE FGVLVRDADA LQRASTLDTV VFDKTGTLTE GKPQVVAVKT 540
FADVDEAQAL RLAAALEQGS SHPLARAILD KAGDMQLPQV NGFRTLRGLG VSGEAEGHAL 600
LLGNQALLNE QQVGTKAIEA EITAQASQGA TPVLLAVDGK AVALLAVRDP LRSDSVAALQ 660
RLHKAGYRLV MLTGDNPTTA NAIAKEAGID EVIAGVLPDG KAEAIKHLQS EGRQVAMVGD 720
GINDAPALAQ ADVGIAMGGG SDVAIETAAI TLMRHSLMGV ADALAISRAT LHNMKQNLLG 780
AFIYNSIGIP VAAGILWPFT GTLLNPVVAG AAMALSSITV VSNANRLLRF KPKE 834 
Gene Ontology
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0031224; C:intrinsic to membrane; IDA:EcoliWiki.
 GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0015662; F:ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism; IDA:EcoliWiki.
 GO:0019829; F:cation-transporting ATPase activity; IEA:InterPro.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0006825; P:copper ion transport; IMP:EcoliWiki.
 GO:0010273; P:detoxification of copper ion; IMP:EcoliWiki. 
Interpro
 IPR023299; ATPase_P-typ_cyto_domN.
 IPR018303; ATPase_P-typ_P_site.
 IPR008250; ATPase_P-typ_transduc_dom_A.
 IPR027256; Cation_transp_P-typ_ATPase_IB.
 IPR001757; Cation_transp_P_typ_ATPase.
 IPR023214; HAD-like_dom.
 IPR017969; Heavy-metal-associated_CS.
 IPR006121; HeavyMe-assoc_HMA. 
Pfam
 PF00122; E1-E2_ATPase
 PF00403; HMA
 PF00702; Hydrolase 
SMART
  
PROSITE
 PS00154; ATPASE_E1_E2
 PS01047; HMA_1
 PS50846; HMA_2 
PRINTS
 PR00119; CATATPASE.
 PR00120; HATPASE.