Reviewed, UniProtKB/Swiss-Prot Q9X5X3 (ATCU_SINMW)

Names and origin

Protein names

Recommended name:
    Copper-transporting P-type ATPase
    EC=3.6.3.4

Gene names

Name:	actP
Ordered Locus Names:	Smed_4897

Encoded on

Plasmid pSMED01

Organism

Sinorhizobium medicae (strain WSM419) (Ensifer medicae) [Complete proteome] [HAMAP]

Taxonomic identifier

366394 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	827 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Involved in copper efflux.
Catalytic activity	ATP + H2O + Cu2+(In) = ADP + phosphate + Cu2+(Out).
Subcellular location	Cell membrane; Multi-pass membrane protein Probable.
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.

Ontologies

Keywords
Biological process	Copper transport Ion transport Transport
Cellular component	Cell membrane Membrane
Domain	Repeat Transmembrane
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 copper ion transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW cation channel activity Inferred from electronic annotation. Source: InterPro copper ion binding Inferred from electronic annotation. Source: UniProtKB-KW copper-exporting ATPase activity Inferred from electronic annotation. Source: EC magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 827	827	Copper-transporting P-type ATPase		PRO_0000046329
Regions
	Transmembrane	174 – 194	21	Potential
	Transmembrane	210 – 230	21	Potential
	Transmembrane	248 – 268	21	Potential
	Transmembrane	271 – 291	21	Potential
	Transmembrane	430 – 450	21	Potential
	Transmembrane	458 – 478	21	Potential
	Transmembrane	541 – 561	21	Potential
	Transmembrane	569 – 589	21	Potential
	Transmembrane	727 – 747	21	Potential
	Transmembrane	773 – 793	21	Potential
	Transmembrane	795 – 815	21	Potential
	Domain	16 – 81	66	HMA 1
	Domain	83 – 149	67	HMA 2
Sites
	Active site	515	1	4-aspartylphosphate intermediate By similarity
	Metal binding	26	1	Copper Potential
	Metal binding	29	1	Copper Potential
	Metal binding	93	1	Copper Potential
	Metal binding	96	1	Copper Potential
	Metal binding	714	1	Magnesium By similarity
	Metal binding	718	1	Magnesium By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9X5X3-1 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: 707E2148DDDA5004	FASTA	827	86,239
	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

References

	« Hide 'large scale' referencesShow '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].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF129004 Genomic DNA. Translation: AAD27639.1. CP000739 Genomic DNA. Translation: ABR63681.1.
RefSeq	YP_001313614.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q9X5X3.
Genome annotation databases
GeneID	5318235.
GenomeReviews	Gene locus Smed_4897 in contig CP000739_GR.
KEGG	smd:Smed_4897.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	WLAFGPS
Family and domain databases
InterPro	IPR008250. ATPase_P-typ_ATPase-assoc-reg. IPR006403. ATPase_P-typ_cat/Cu-transptr. IPR001366. ATPase_P-typ_Cd-transp. IPR006416. ATPase_P-typ_heavy-metal. IPR001757. ATPase_P-typ_ion-transptr. IPR018303. ATPase_P-typ_P_site. IPR005834. Dehalogen-like_hydro. IPR017969. Heavy-metal-associated_CS. IPR006121. HeavyMe_transpt. [Graphical view]
PANTHER	PTHR11939. ATPase_P. 1 hit.
Pfam	PF00122. E1-E2_ATPase. 1 hit. PF00403. HMA. 2 hits. PF00702. Hydrolase. 1 hit. [Graphical view]
PRINTS	PR00119. CATATPASE. PR00941. CDATPASE.
TIGRFAMs	TIGR01511. ATPase-IB1_Cu. 1 hit. TIGR01525. ATPase-IB_hvy. 1 hit. TIGR01494. ATPase_P-type. 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

ATCU_SINMW

Accession

Primary (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 24, 2009
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)