ATCU2_RHIME
ID ATCU2_RHIME Reviewed; 827 AA.
AC P58342;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2001, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Copper-transporting ATPase 2;
DE EC=7.2.2.9;
GN Name=actP2; Synonyms=atcU2; OrderedLocusNames=RB1018; ORFNames=SMb21578;
OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS meliloti).
OG Plasmid pSymB (megaplasmid 2).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=266834;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11481431; DOI=10.1073/pnas.161294698;
RA Finan T.M., Weidner S., Wong K., Buhrmester J., Chain P., Vorhoelter F.J.,
RA Hernandez-Lucas I., Becker A., Cowie A., Gouzy J., Golding B., Puehler A.;
RT "The complete sequence of the 1,683-kb pSymB megaplasmid from the N2-fixing
RT endosymbiont Sinorhizobium meliloti.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9889-9894(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11474104; DOI=10.1126/science.1060966;
RA Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA Wong K., Yeh K.-C., Batut J.;
RT "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL Science 293:668-672(2001).
CC -!- FUNCTION: Involved in copper transport. {ECO:0000250}.
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:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
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; AL591985; CAC49418.1; -; Genomic_DNA.
DR PIR; B95969; B95969.
DR RefSeq; NP_437558.1; NC_003078.1.
DR RefSeq; WP_010975861.1; NC_003078.1.
DR AlphaFoldDB; P58342; -.
DR SMR; P58342; -.
DR STRING; 266834.SM_b21578; -.
DR EnsemblBacteria; CAC49418; CAC49418; SM_b21578.
DR GeneID; 61600979; -.
DR KEGG; sme:SM_b21578; -.
DR PATRIC; fig|266834.11.peg.5945; -.
DR eggNOG; COG2217; Bacteria.
DR HOGENOM; CLU_001771_0_3_5; -.
DR OMA; ICRIHIR; -.
DR Proteomes; UP000001976; Plasmid pSymB.
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; PR00120; HATPASE.
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 3: Inferred from homology;
KW ATP-binding; Cell membrane; Copper; Copper transport; Ion transport;
KW Magnesium; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Plasmid; Reference proteome; Repeat; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..827
FT /note="Copper-transporting ATPase 2"
FT /id="PRO_0000046328"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 210..230
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 246..266
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 771..793
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 797..819
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; 85862 MW; A3D8DFFDD1315FCB CRC64;
MTALKKIEKA APLPVSTNFG IEGMTCASCV RRVEKAITAV PGVASANVNL ATERATVQFD
GEPDTLAVLH AIEKAGYAPR IATEELQIEG MTCASCVSRV EKALKAVPGV ADAAVNLATE
KATVSLISGT ADLSALEAAV RGAGYELRKT KPAEASAGDE DHRAAELGSL KSAVTISVLM
TLPLFLMEMG SHFISGVHEL IMGTIGMRNN LYLQFALATL VLFGPGLRFF RKGVPNLLRW
TPDMNSLVVL GTTAAWGYSV VATFVPRVLP SGTANVYYEA AAVIVTLVLL GRYLESRAKG
RTSQAIKRLV GLQPKTAFVL RGGEFVEAQI SEVVAGDVIR IRPGEKIPVD GTVIDGSSYV
DEAMITGEPL PVQKTADSAV VGGTINKTGS ITFKATKVGS DTLLAQIIKL VETAQGSKLP
IQALVDRVTG WFVPAVILAA VLTFAAWYTF GPSPALSFAL VNAVAVLIIA CPCAMGLATP
TSIMVGTGRA AELGILFRKG EALQRLRDAD VVALDKTGTL TKGRPELTDL VAAEGFEADE
VLFLVASLET LSEHPIAEAI VSAAKSKGIA TAAVNGFEAT PGFGVSGSVS GRQVLVGADR
ALATNGIDVS GFSTEAELLG ASGKSPLYAA IEGRLAAIVA VSDPVKETTP QAIRSLHELG
LKVAMITGDN RRTAEAIARK LGIDEVVAEV LPEGKVEAIR KLRQGGRSVA FIGDGINDAP
ALAEADVGIA VGTGTDIAIE SADVVLMSGD LNGVAKAIAL SKATILNIKQ NLFWAFAYNV
SLIPVAAGVL YPVTGILLSP IFAAAAMAMS SVFVLGNALR LKSVNPA
