ID   COPB_STAAU              Reviewed;         672 AA.
AC   Q69HU0;
DT   23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Probable copper-transporting P-type ATPase B;
DE            EC=7.2.2.8;
GN   Name=copB;
OS   Staphylococcus aureus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 12600 / DSM 20231 / IAM 12544 / NCDO 949 / NCTC 8532;
RX   PubMed=16151171; DOI=10.1128/aem.71.9.5650-5653.2005;
RA   Sitthisak S., Howieson K., Amezola C., Jayaswal R.K.;
RT   "Characterization of a multicopper oxidase gene from Staphylococcus
RT   aureus.";
RL   Appl. Environ. Microbiol. 71:5650-5653(2005).
CC   -!- FUNCTION: Involved in copper transport. {ECO:0000250}.
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   -!- 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; AY259130; AAQ17237.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q69HU0; -.
DR   SMR; Q69HU0; -.
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   3: Inferred from homology;
KW   ATP-binding; Cell membrane; Copper; Copper transport; Ion transport;
KW   Magnesium; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW   Translocase; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..672
FT                   /note="Probable copper-transporting P-type ATPase B"
FT                   /id="PRO_0000350602"
FT   TRANSMEM        30..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        55..75
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        93..113
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        125..145
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        282..302
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        313..333
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        621..643
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        647..669
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        365
FT                   /note="4-aspartylphosphate intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         563
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         567
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   672 AA;  73184 MW;  D5416440C2E5B418 CRC64;
     MEHHSHQEHE NHTSHGNHEH HHHGNFKSKF FISLIFAIPI IILSPMMGVK LPFQISFTGS
     DWIVLILATI LFFYGGKPFL SGAKDEISTK KPGMMTLVAL GISVAYIYSL YAFYMNNFSG
     SSTHTMDFFW ELATLILIML LGHWIEMNAV GNAGNALKKM AELLPNTAVK LIDNNQREEV
     KISDIHIDDI VEVRAGESIP TDGIIVRGET SIDESLVTGE SKKVHKTHND DVIGGSINGS
     GTVQVKVTAT GENGYLSQVM GLVNQAQNDK SKAELLSDKV AGYLFYFAVS IGLISFIVWM
     LIQNNVDFAL ERLVTVLVIA CPHALGLAIP LVTARSTSIG AHNGLIIKNR ESVEIAQHID
     YIMMDKTGTL TEGNFSVNHY ESFTDELNNE EILSLFASLE SNSNHPLATG IVDFAKGKNI
     SYATPQEVNN IPGVGLEGTV DNKKLKIVNV SYLDKSNFDY NKEQFTNLAQ QGNSISYLIH
     DRQVIGIIAQ GDKIKESSKQ MVSDLLSRNI TPVMLTGDNK EVAQTVAEEL GISDVHAQLM
     PEDKESIIQD YQSNGSKIMM VGDGINDAPS LIRADIGMAI GAGTDVAIES GDVILVKSNP
     SDIINFLSLS KNTMKKMVQN LWWGAGYNVI AVPLAAGILA SIGLILSPAV GAILMSLSTI
     IVAINAFTLK LK