COPB_ENTHA
ID COPB_ENTHA Reviewed; 745 AA.
AC P05425; I6S229;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Copper-exporting P-type ATPase B;
DE EC=7.2.2.8 {ECO:0000269|PubMed:7721839};
DE AltName: Full=Cu(+)-exporting ATPase;
GN Name=copB; OrderedLocusNames=EHR_09090;
OS Enterococcus hirae (strain ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 /
OS NBRC 3181 / NCIMB 6459 / NCDO 1258 / NCTC 12367 / WDCM 00089 / R).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=768486;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION IN COPPER HOMEOSTASIS.
RC STRAIN=ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 / NBRC 3181 / NCIMB 6459
RC / NCDO 1258 / NCTC 12367 / WDCM 00089 / R;
RX PubMed=8048974; DOI=10.1016/s0021-9258(18)31455-8;
RA Odermatt A., Suter H., Krapf R., Solioz M.;
RT "Primary structure of two P-type ATPases involved in copper homeostasis in
RT Enterococcus hirae.";
RL J. Biol. Chem. 268:12775-12779(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 / NBRC 3181 / NCIMB 6459
RC / NCDO 1258 / NCTC 12367 / WDCM 00089 / R;
RX PubMed=22933757; DOI=10.1128/jb.01075-12;
RA Gaechter T., Wunderlin C., Schmidheini T., Solioz M.;
RT "Genome sequence of Enterococcus hirae (Streptococcus faecalis) ATCC 9790,
RT a model organism for the study of ion transport, bioenergetics, and copper
RT homeostasis.";
RL J. Bacteriol. 194:5126-5127(2012).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 162-745.
RX PubMed=2953719; DOI=10.1016/s0021-9258(18)48244-0;
RA Solioz M., Mathews S., Fuerst P.;
RT "Cloning of the K+-ATPase of Streptococcus faecalis. Structural and
RT evolutionary implications of its homology to the KdpB-protein of
RT Escherichia coli.";
RL J. Biol. Chem. 262:7358-7362(1987).
RN [4]
RP FUNCTION IN COPPER AND SILVER EXPORT, AND INDUCTION BY COPPER AND SILVER.
RC STRAIN=ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 / NBRC 3181 / NCIMB 6459
RC / NCDO 1258 / NCTC 12367 / WDCM 00089 / R;
RX PubMed=8037745; DOI=10.1006/bbrc.1994.1891;
RA Odermatt A., Krapf R., Solioz M.;
RT "Induction of the putative copper ATPases, CopA and CopB, of Enterococcus
RT hirae by Ag+ and Cu2+, and Ag+ extrusion by CopB.";
RL Biochem. Biophys. Res. Commun. 202:44-48(1994).
RN [5]
RP FUNCTION IN COPPER AND SILVER EXPORT, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 / NBRC 3181 / NCIMB 6459
RC / NCDO 1258 / NCTC 12367 / WDCM 00089 / R;
RX PubMed=7721839; DOI=10.1074/jbc.270.16.9217;
RA Solioz M., Odermatt A.;
RT "Copper and silver transport by CopB-ATPase in membrane vesicles of
RT Enterococcus hirae.";
RL J. Biol. Chem. 270:9217-9221(1995).
CC -!- FUNCTION: Involved in copper export. Can also export silver.
CC {ECO:0000269|PubMed:7721839, ECO:0000269|PubMed:8037745,
CC ECO:0000269|PubMed:8048974}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + Cu(+)(in) + H2O = ADP + Cu(+)(out) + H(+) + phosphate;
CC Xref=Rhea:RHEA:25792, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:49552,
CC ChEBI:CHEBI:456216; EC=7.2.2.8;
CC Evidence={ECO:0000269|PubMed:7721839};
CC -!- ACTIVITY REGULATION: Inhibited by vanadate.
CC {ECO:0000269|PubMed:7721839}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6. {ECO:0000269|PubMed:7721839};
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- INDUCTION: By copper and silver. {ECO:0000269|PubMed:8037745}.
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; L13292; AAA61836.1; -; Genomic_DNA.
DR EMBL; CP003504; AFM70730.1; -; Genomic_DNA.
DR PIR; B45995; B45995.
DR RefSeq; WP_010737924.1; NZ_KB946231.1.
DR AlphaFoldDB; P05425; -.
DR SMR; P05425; -.
DR STRING; 768486.EHR_09090; -.
DR TCDB; 3.A.3.5.2; the p-type atpase (p-atpase) superfamily.
DR EnsemblBacteria; AFM70730; AFM70730; EHR_09090.
DR KEGG; ehr:EHR_09090; -.
DR eggNOG; COG2217; Bacteria.
DR HOGENOM; CLU_001771_11_2_9; -.
DR OrthoDB; 237367at2; -.
DR BRENDA; 7.2.2.8; 2097.
DR SABIO-RK; P05425; -.
DR Proteomes; UP000002895; Chromosome.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0140581; F:P-type monovalent copper transporter activity; IEA:UniProtKB-EC.
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; IPR027256; P-typ_ATPase_IB.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR PRINTS; PR00120; HATPASE.
DR SFLD; SFLDF00027; p-type_atpase; 1.
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 PROSITE; PS00154; ATPASE_E1_E2; 1.
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 Repeat; Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..745
FT /note="Copper-exporting P-type ATPase B"
FT /id="PRO_0000046251"
FT TOPO_DOM 1..108
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 109..128
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 129..139
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 161..170
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 171..191
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 192..200
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 218..359
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 360..379
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 380..388
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 389..409
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 410..703
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 704..721
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 722..723
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 724..744
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 745
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 60..71
FT /note="1"
FT REPEAT 73..84
FT /note="2"
FT REPEAT 86..97
FT /note="3"
FT REGION 1..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 60..97
FT /note="3 X 12 AA approximate repeats"
FT COMPBIAS 24..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..76
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 440
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 638
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 642
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT CONFLICT 196
FT /note="N -> S (in Ref. 3; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 329..333
FT /note="NGYLA -> MVTC (in Ref. 3; no nucleotide entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 745 AA; 81523 MW; 956EDF22D23C8D94 CRC64;
MNNGIDPENE TNKKGAIGKN PEEKITVEQT NTKNNLQEHG KMENMDQHHT HGHMERHQQM
DHGHMSGMDH SHMDHEDMSG MNHSHMGHEN MSGMDHSMHM GNFKQKFWLS LILAIPIILF
SPMMGMSFPF QVTFPGSNWV VLVLATILFI YGGQPFLSGA KMELKQKSPA MMTLIAMGIT
VAYVYSVYSF IANLINPHTH VMDFFWELAT LIVIMLLGHW IEMNAVSNAS DALQKLAELL
PESVKRLKKD GTEETVSLKE VHEGDRLIVR AGDKMPTDGT IDKGHTIVDE SAVTGESKGV
KKQVGDSVIG GSINGDGTIE ITVTGTGENG YLAKVMEMVR KAQGEKSKLE FLSDKVAKWL
FYVALVVGII AFIAWLFLAN LPDALERMVT VFIIACPHAL GLAIPLVVAR STSIAAKNGL
LLKNRNAMEQ ANDLDVIMLD KTGTLTQGKF TVTGIEILDE AYQEEEILKY IGALEAHANH
PLAIGIMNYL KEKKITPYQA QEQKNLAGVG LEATVEDKDV KIINEKEAKR LGLKIDPERL
KNYEAQGNTV SFLVVSDKLV AVIALGDVIK PEAKEFIQAI KEKNIIPVML TGDNPKAAQA
VAEYLGINEY YGGLLPDDKE AIVQRYLDQG KKVIMVGDGI NDAPSLARAT IGMAIGAGTD
IAIDSADVVL TNSDPKDILH FLELAKETRR KMIQNLWWGA GYNIIAIPLA AGILAPIGLI
LSPAVGAVLM SLSTVVVALN ALTLK
