ATCU_SINMW
ID ATCU_SINMW Reviewed; 827 AA.
AC Q9X5X3; A6UJ51;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Copper-transporting P-type ATPase;
DE EC=7.2.2.9;
GN Name=actP; OrderedLocusNames=Smed_4897;
OS Sinorhizobium medicae (strain WSM419) (Ensifer medicae).
OG Plasmid pSMED01.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=366394;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RX PubMed=11936079; DOI=10.1046/j.1365-2958.2002.02791.x;
RA Reeve W.G., Tiwari R.P., Kale N.B., Dilworth M.J., Glenn A.R.;
RT "ActP controls copper homeostasis in Rhizobium leguminosarum bv. viciae and
RT Sinorhizobium meliloti preventing low pH-induced copper toxicity.";
RL Mol. Microbiol. 43:981-991(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSM419;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Reeve W.G.,
RA Richardson P.;
RT "Complete sequence of Sinorhizobium medicae WSM419 plasmid pSMED01.";
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in copper efflux.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + Cu(2+)(in) + H2O = ADP + Cu(2+)(out) + H(+) + phosphate;
CC Xref=Rhea:RHEA:10376, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29036, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:456216; EC=7.2.2.9;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- INDUCTION: Transcriptionally regulated by HmrR in response to Cu(+)
CC ions.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IB subfamily. {ECO:0000305}.
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DR EMBL; AF129004; AAD27639.1; -; Genomic_DNA.
DR EMBL; CP000739; ABR63681.1; -; Genomic_DNA.
DR RefSeq; WP_012061811.1; NC_009620.1.
DR RefSeq; YP_001313614.1; NC_009620.1.
DR AlphaFoldDB; Q9X5X3; -.
DR SMR; Q9X5X3; -.
DR EnsemblBacteria; ABR63681; ABR63681; Smed_4897.
DR KEGG; smd:Smed_4897; -.
DR PATRIC; fig|366394.8.peg.1375; -.
DR HOGENOM; CLU_001771_0_3_5; -.
DR OMA; ITFFGWM; -.
DR OrthoDB; 237367at2; -.
DR Proteomes; UP000001108; Plasmid pSMED01.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0043682; F:P-type divalent copper transporter activity; IEA:UniProtKB-EC.
DR CDD; cd00371; HMA; 2.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR InterPro; IPR018303; ATPase_P-typ_P_site.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR017969; Heavy-metal-associated_CS.
DR InterPro; IPR006122; HMA_Cu_ion-bd.
DR InterPro; IPR006121; HMA_dom.
DR InterPro; IPR036163; HMA_dom_sf.
DR InterPro; IPR027256; P-typ_ATPase_IB.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR Pfam; PF00403; HMA; 2.
DR PRINTS; PR00941; CDATPASE.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SUPFAM; SSF55008; SSF55008; 2.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01525; ATPase-IB_hvy; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 1.
DR TIGRFAMs; TIGR00003; TIGR00003; 2.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS01047; HMA_1; 2.
DR PROSITE; PS50846; HMA_2; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Copper; Copper transport; Ion transport;
KW Magnesium; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Plasmid; Repeat; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..827
FT /note="Copper-transporting P-type ATPase"
FT /id="PRO_0000046329"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 210..230
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 248..268
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 271..291
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 430..450
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 458..478
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 541..561
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 569..589
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 727..747
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 773..793
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 795..815
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 15..80
FT /note="HMA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT DOMAIN 82..148
FT /note="HMA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT ACT_SITE 515
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 26
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 29
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 93
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 96
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 714
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 718
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
SQ SEQUENCE 827 AA; 86239 MW; 707E2148DDDA5004 CRC64;
MTALKQTEKS TSLPMSFDFD IEGMTCASCV RRVEKAIAAV PGVASANVNL ATERATVQFN
GVPETTSVLR AVEKAGYAPR IVTEEIQIEG MTCASCVSRV EKALKAVPGV ADASVNLATE
KATVRLVSGS AEISALAAAV KGAGYGIRKA TPAEAMKEDV DHRTAELRSL KSAVTISSLM
TLPLFLLEMG SHFIPGVHDF IMGTIGMRNN LYLQFALATL VLFGPGLRFF RKGVPNLLRW
TPDMNSLVVL GTTAAWGYSV VTTFVPAILP SGTANVYYEA AAVIVTLILV GRYLESRAKG
RTSQAIKRLV GLQPKTAFVL HSGEFVETEI TEVVTGDVIR IRPGEKIPVD GTVTDGSSYV
DESMITGEPV PVQKATDSAV IGGTINKTGS ITFKATKVGS DTLLAQIIRL VEAAQGSKLP
IQALVDRVTA WFVPVVILAA LLTFAAWYVL GPSPALSFAL VNAVAVLIIA CPCAMGLATP
TSIMVGTGRA AELGILFRKG EALQSLRDAD VVAVDKTGTL TKGRPELTDL VAAEGFEPDE
VLCLVASLET LSEHPIAEAI VSAAKSRGIA TVAVSAFEAT PGFGVSGTVS GRRVLVGADR
ALVKNGIDIT GFADEAERLG SGGKSPLYAA IDGRLAAIVA VSDPVKESTP QAIKSLHALG
LKVAMVTGDN RRTAEAIAKK LGIDEVVAEV LPEGKVDAVR KLRQGGRSVA FIGDGINDAP
ALAEADVGIA VGTGTDIAIE SADVVLMSGD LNGVAKALAL SKATIRNIKQ NLFWAFVYNI
SLVPVAAGVL YPVNGTLLSP IFAAAAMAMS SVFVLGNALR LKSFDPA
