Copper-transporting ATPase 1 - Rhizobium meliloti (strain 1021) (Ensifer meliloti)

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P58341 (ATCU1_RHIME) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 83. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Copper-transporting ATPase 1
EC=3.6.3.4

Gene names

Name:	actP1
Synonyms:	actP
Ordered Locus Names:	RA0548
ORF Names:	SMa1013

Encoded on

Plasmid pSymA (megaplasmid 1)

Organism

Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti) [Complete proteome] [HAMAP]

Taxonomic identifier

266834 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Rhizobiaceae › Sinorhizobium/Ensifer group › Sinorhizobium

Protein attributes

Sequence length	826 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Involved in copper transport By similarity.
Catalytic activity	ATP + H₂O + Cu²⁺(In) = ADP + phosphate + Cu²⁺(Out).
Subcellular location	Cell membrane; Multi-pass membrane protein By similarity.
Sequence similarities	Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IB subfamily. [View classification] Contains 2 HMA domains.

Ontologies

Keywords
Biological process	Copper transport Ion transport Transport
Cellular component	Cell membrane Membrane
Domain	Repeat Transmembrane Transmembrane helix
Ligand	ATP-binding Copper Magnesium Metal-binding Nucleotide-binding
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome Plasmid
Gene Ontology (GO)
Biological process	ATP biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW copper ion binding Inferred from electronic annotation. Source: InterPro copper-exporting ATPase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 826

826

Copper-transporting ATPase 1

PRO_0000046327

Regions

Transmembrane

172 – 192

Helical; Potential

Transmembrane

209 – 229

Helical; Potential

Transmembrane

246 – 266

Helical; Potential

Transmembrane

270 – 290

Helical; Potential

Transmembrane

429 – 449

Helical; Potential

Transmembrane

457 – 477

Helical; Potential

Transmembrane

772 – 792

Helical; Potential

Transmembrane

795 – 815

Helical; Potential

Domain

16 – 81

HMA 1

Domain

83 – 148

HMA 2

Sites

Active site

514

4-aspartylphosphate intermediate By similarity

Metal binding

Copper Potential

Metal binding

Copper Potential

Metal binding

Copper Potential

Metal binding

Copper Potential

Metal binding

713

Magnesium By similarity

Metal binding

717

Magnesium By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P58341 [UniParc].

Last modified November 2, 2001. Version 1.
Checksum: 91966D720D870F70
Show »

FASTA

826

86,285

        10         20         30         40         50         60 
MTAFTQIEKS AAVPAPTDFG IEGMTCASCV RRVEKAISAV PGVASATVNL ATERASVQFT 

        70         80         90        100        110        120 
GAPDTGGVLL AIEKAGYEPK VIIQEFGIEG MTCASCVSRV EKALRTVPGV ADASVNLATE 

       130        140        150        160        170        180 
KGTVRFVSGV DVAAIEAAVR DAGYDVRKAK ASGATAEPED RRELETRTLK RLVILSAVLT 

       190        200        210        220        230        240 
LPLFLVEMGS HFMPGVHEWI MENIGMRHNL YIQFALATAV LFGPGLRFFR KGVPNLLRWT 

       250        260        270        280        290        300 
PDMNSLVVLG TTAAWGYSVV ATFASGLLPS GTANVYYEAA AVIVTLILLG RYLEARAKGR 

       310        320        330        340        350        360 
TSQAIKRLLG LQPKTAFVAH GDEFVEIQIS DVVVGDVIRI RPGEKIPVDG TVLDGNSYVD 

       370        380        390        400        410        420 
ESMITGEPVP VQKAAGAEVV GGTINKNGSF TFRATKVGGD TLLAQIIKMV ETAQGSKLPI 

       430        440        450        460        470        480 
QALVDKVTAW FVPAVILVAV LTFAAWYVFG PSPALTFALV NAVAVLIIAC PCAMGLATPT 

       490        500        510        520        530        540 
SIMVGTGRAA ELGILFRKGE ALQSLREADV IALDKTGTLT KGRPELTDIV PADGFEADEV 

       550        560        570        580        590        600 
LSFVASLEAL SEHPIAEAIV SAAKSRGIAL VPATDFEATP GFGVRGAVSG LPVQVGADRA 

       610        620        630        640        650        660 
FSGVGIDVSP FVVEAERLGN SGKSPLYAAI DGRLAAIIAV SDPIKDTTPQ AIKALHDLGL 

       670        680        690        700        710        720 
KVAMITGDNR RTADAIARQL GIDEVVAEVL PDGKVDAVKR LREGGRKVAF IGDGINDAPA 

       730        740        750        760        770        780 
LTEADVGIAV GTGTDIAIES ADVVLMSGDL IGVPKAIALS KATIRNIKQN LFWAFAYNVS 

       790        800        810        820 
LVPVAAGVLY PLNGTLLSPI LAAAAMAMSS VFVLGNALRL RSVNPA

« Hide

References

[1]

"Nucleotide sequence and predicted functions of the entire Sinorhizobium meliloti pSymA megaplasmid."
Barnett M.J., Fisher R.F., Jones T., Komp C., Abola A.P., Barloy-Hubler F., Bowser L., Capela D., Galibert F., Gouzy J., Gurjal M., Hong A., Huizar L., Hyman R.W., Kahn D., Kahn M.L., Kalman S., Keating D.H.

Long S.R.
Proc. Natl. Acad. Sci. U.S.A. 98:9883-9888(2001) [PubMed: 11481432] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 1021.

[2]

"The composite genome of the legume symbiont Sinorhizobium meliloti."
Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F., Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G., Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P., Cowie A.

Batut J.
Science 293:668-672(2001) [PubMed: 11474104] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 1021.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE006469 Genomic DNA. Translation: AAK65206.1.
PIR	D95330.
RefSeq	NP_435794.1. NC_003037.1.
3D structure databases
ProteinModelPortal	P58341.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1235584.
GenomeReviews	Gene locus RA0548 in contig AE006469_GR.
KEGG	sme:SMa1013.
NMPDR	fig\|266834.1.peg.548.
PATRIC	23627570. VBISinMel96828_0564.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG507745.
OMA	HEWIMEN.
ProtClustDB	CLSK807623.
Enzyme and pathway databases
BioCyc	SMEL266834:SMA1013-MONOMER.
Family and domain databases
InterPro	IPR008250. ATPase_P-typ_ATPase-assoc-dom. IPR006403. ATPase_P-typ_cat/Cu-transptr. IPR023300. ATPase_P-typ_cyto_domA. IPR023299. ATPase_P-typ_cyto_domN. IPR000695. ATPase_P-typ_H-transp. IPR006416. ATPase_P-typ_heavy-metal. IPR001757. ATPase_P-typ_ion-transptr. IPR018303. ATPase_P-typ_P_site. IPR005834. Dehalogen-like_hydro. IPR023214. HAD-like_dom. IPR017969. Heavy-metal-associated_CS. IPR006121. HeavyMe-assoc_HMA. IPR006122. HMA_Cu_ion-bd. [Graphical view]
Gene3D	G3DSA:2.70.150.10. ATPase_P-typ_cyto_domA. 1 hit. G3DSA:3.40.1110.10. ATPase_P-typ_cyto_domN. 1 hit. G3DSA:3.40.50.1000. HAD-like_dom. 2 hits.
KO	K01533.
Pfam	PF00122. E1-E2_ATPase. 1 hit. PF00403. HMA. 2 hits. PF00702. Hydrolase. 1 hit. [Graphical view]
PRINTS	PR00119. CATATPASE. PR00120. HATPASE.
SUPFAM	SSF56784. HAD-like_dom. 1 hit. SSF55008. HeavyMe_transpt. 2 hits.
TIGRFAMs	TIGR01511. ATPase-IB1_Cu. 1 hit. TIGR01525. ATPase-IB_hvy. 1 hit. TIGR01494. ATPase_P-type. 1 hit. TIGR00003. TIGR00003. 2 hits.
PROSITE	PS00154. ATPASE_E1_E2. 1 hit. PS01047. HMA_1. 2 hits. PS50846. HMA_2. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ATCU1_RHIME

Accession

Primary (citable) accession number: P58341

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 2, 2001
Last sequence update:	November 2, 2001
Last modified:	January 25, 2012
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents