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Reviewed, UniProtKB/Swiss-Prot Q9X5X3 (ATCU_SINMW)

Last modified November 4, 2008. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Copper-transporting P-type ATPase
    EC=3.6.3.4
Gene names
Name: actP
Ordered Locus Names: Smed_4897
Encoded onPlasmid pSMED01
OrganismSinorhizobium medicae (strain WSM419) (Ensifer medicae) [Complete proteome] [HAMAP]
Taxonomic identifier366394 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Rhizobiaceae › Sinorhizobium/Ensifer group › Sinorhizobium

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Protein attributes

Sequence length827 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Involved in copper efflux.

Catalytic activity

ATP + H(2)O + Cu(2+)(In) = ADP + phosphate + Cu(2+)(Out).

Subcellular location

Cell membrane; Multi-pass membrane proteinProbable.

Induction

Transcriptionally regulated by hmrR in response to Cu(+) ions.

Sequence similarities

Belongs to the cation transport ATPase (P-type) family. Type IB subfamily.

Contains 2 HMA domains.

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Ontologies

Keywords

   Biological processCopper transport
Ion transport
Transport
   Cellular componentCell membrane
Membrane
   DomainRepeat
Transmembrane
   LigandATP-binding
Copper
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical termComplete proteome
Plasmid

Gene Ontology (GO)

   Biological processcopper ion transport

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentplasma membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functioncopper ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

magnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 827827Copper-transporting P-type ATPase
PRO_0000046329

Regions

Transmembrane174 – 19421 Potential
Transmembrane210 – 23021 Potential
Transmembrane248 – 26821 Potential
Transmembrane271 – 29121 Potential
Transmembrane430 – 45021 Potential
Transmembrane458 – 47821 Potential
Transmembrane541 – 56121 Potential
Transmembrane569 – 58921 Potential
Transmembrane727 – 74721 Potential
Transmembrane773 – 79321 Potential
Transmembrane795 – 81521 Potential
Domain16 – 8166HMA 1
Domain83 – 14967HMA 2

Sites

Active site51514-aspartylphosphate intermediate By similarity
Metal binding261Copper Potential
Metal binding291Copper Potential
Metal binding931Copper Potential
Metal binding961Copper Potential
Metal binding7141Magnesium By similarity
Metal binding7181Magnesium By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q9X5X3-1 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 707E2148DDDA5004

FASTA82786,239
        10         20         30         40         50         60 
MTALKQTEKS TSLPMSFDFD IEGMTCASCV RRVEKAIAAV PGVASANVNL ATERATVQFN 

        70         80         90        100        110        120 
GVPETTSVLR AVEKAGYAPR IVTEEIQIEG MTCASCVSRV EKALKAVPGV ADASVNLATE 

       130        140        150        160        170        180 
KATVRLVSGS AEISALAAAV KGAGYGIRKA TPAEAMKEDV DHRTAELRSL KSAVTISSLM 

       190        200        210        220        230        240 
TLPLFLLEMG SHFIPGVHDF IMGTIGMRNN LYLQFALATL VLFGPGLRFF RKGVPNLLRW 

       250        260        270        280        290        300 
TPDMNSLVVL GTTAAWGYSV VTTFVPAILP SGTANVYYEA AAVIVTLILV GRYLESRAKG 

       310        320        330        340        350        360 
RTSQAIKRLV GLQPKTAFVL HSGEFVETEI TEVVTGDVIR IRPGEKIPVD GTVTDGSSYV 

       370        380        390        400        410        420 
DESMITGEPV PVQKATDSAV IGGTINKTGS ITFKATKVGS DTLLAQIIRL VEAAQGSKLP 

       430        440        450        460        470        480 
IQALVDRVTA WFVPVVILAA LLTFAAWYVL GPSPALSFAL VNAVAVLIIA CPCAMGLATP 

       490        500        510        520        530        540 
TSIMVGTGRA AELGILFRKG EALQSLRDAD VVAVDKTGTL TKGRPELTDL VAAEGFEPDE 

       550        560        570        580        590        600 
VLCLVASLET LSEHPIAEAI VSAAKSRGIA TVAVSAFEAT PGFGVSGTVS GRRVLVGADR 

       610        620        630        640        650        660 
ALVKNGIDIT GFADEAERLG SGGKSPLYAA IDGRLAAIVA VSDPVKESTP QAIKSLHALG 

       670        680        690        700        710        720 
LKVAMVTGDN RRTAEAIAKK LGIDEVVAEV LPEGKVDAVR KLRQGGRSVA FIGDGINDAP 

       730        740        750        760        770        780 
ALAEADVGIA VGTGTDIAIE SADVVLMSGD LNGVAKALAL SKATIRNIKQ NLFWAFVYNI 

       790        800        810        820 
SLVPVAAGVL YPVNGTLLSP IFAAAAMAMS SVFVLGNALR LKSFDPA

« Hide

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References

« Hide 'large scale' references
[1]"ActP controls copper homeostasis in Rhizobium leguminosarum bv. viciae and Sinorhizobium meliloti preventing low pH-induced copper toxicity."
Reeve W.G., Tiwari R.P., Kale N.B., Dilworth M.J., Glenn A.R.
Mol. Microbiol. 43:981-991(2002) [PubMed: 11936079] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
[2]"Complete sequence of Sinorhizobium medicae WSM419 plasmid pSMED01."
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Reeve W.G., Richardson P.
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

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Cross-references

Sequence databases

AF129004 Genomic DNA. Translation: AAD27639.1.
CP000739 Genomic DNA. Translation: ABR63681.1.
RefSeqYP_001313614.1.

3D structure databases

HSSPHSSP built from PDB template 1JWW based on UniProtKB O32220.
ModBaseSearch...

Genome annotation databases

GeneID5318235.
GenomeReviewsGene locus Smed_4897 in contig CP000739_GR.
KEGGsmd:Smed_4897.

Organism-specific databases

CMRSearch...

Family and domain databases

InterProIPR006416. ATPase-IB_hvy.
IPR001757. ATPase_P.
IPR000579. ATPase_P_cat.
IPR006403. ATPase_P_cat/Cu.
IPR005834. Dehalogen-like_hydro.
IPR008250. E1-E2_ATPase_reg.
IPR006121. HeavyMe_transpt.
[Graphical view]
PANTHERPTHR11939. ATPase_P. 1 hit.
PfamPF00122. E1-E2_ATPase. 1 hit.
PF00403. HMA. 2 hits.
PF00702. Hydrolase. 1 hit.
[Graphical view]
PRINTSPR00119. CATATPASE.
PR00940. CATPATPASEA.
TIGRFAMsTIGR01511. ATPase-IB1_Cu. 1 hit.
TIGR01525. ATPase-IB_hvy. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.
PROSITEPS00154. ATPASE_E1_E2. 1 hit.
PS01047. HMA_1. 2 hits.
PS50846. HMA_2. 2 hits.
[Graphical view]
BLOCKSSearch...
ProtoNetSearch...

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Entry information

Entry nameATCU_SINMW
AccessionPrimary (citable) accession number: Q9X5X3
Secondary accession number(s): A6UJ51
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1999
Last modified: November 4, 2008
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents