ID   COPB_STAAR              Reviewed;         681 AA.
AC   Q6GIX4;
DT   23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Probable copper-transporting P-type ATPase B;
DE            EC=7.2.2.8;
GN   Name=copB; OrderedLocusNames=SAR0720;
OS   Staphylococcus aureus (strain MRSA252).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282458;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MRSA252;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
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; BX571856; CAG39731.1; -; Genomic_DNA.
DR   RefSeq; WP_000069452.1; NC_002952.2.
DR   AlphaFoldDB; Q6GIX4; -.
DR   SMR; Q6GIX4; -.
DR   KEGG; sar:SAR0720; -.
DR   HOGENOM; CLU_001771_11_2_9; -.
DR   OMA; MALEPMG; -.
DR   Proteomes; UP000000596; 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   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..681
FT                   /note="Probable copper-transporting P-type ATPase B"
FT                   /id="PRO_0000350603"
FT   TRANSMEM        39..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        64..84
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        102..122
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        134..154
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        291..311
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        322..342
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        630..652
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        656..678
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..26
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        374
FT                   /note="4-aspartylphosphate intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         572
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         576
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   681 AA;  74272 MW;  88936CE656352ED2 CRC64;
     MSNNKKHQNH EHHSHQEHEN HTSHGNHEHH HHGNFKSKFF ISLIFAIPII ILSPMMGVKL
     PFQISFTGSD WIVLILATIL FFYGGKPFLS GAKDEISTKK PGMMTLVALG ISVAYIYSLY
     AFYMNNFSGS STHTMDFFWE LATLILIMLL GHWIEMNAVG NAGNALKKMA ELLPNTAVKL
     IDNNQREEVK ISDIHIDDIV EVRAGESIPT DGIIVRGETS IDESLVTGES KKVHKTHNDD
     VIGGSINGSG TVQVKVTATG ENGYLSQVMG LVNQAQNDKS KAELLSDKVA GYLFYFAVSI
     GLISFIVWML IQNNVDFALE RLVTVLVIAC PHALGLAIPL VTARSTSIGA HNGLIIKNRE
     SVEIAQHIDY IMMDKTGTLT EGNFSVNHYE SFTDELNNEE ILSLFASLES NSNHPLATGI
     VDFAKGKNIS YATPQEVNNI PGVGLEGTVD NKKLKIVNVS YLDKSNFDYN KEQFTNLAQQ
     GNSISYLIHD RQVIGIIAQG DKIKESSKQM VSDLLSRNIT PVMLTGDNKE VAQTVAEELG
     ISDVHAQLMP EDKESIIQDY QSNGSKIMMV GDGINDAPSL IRADIGMAIG AGTDVAIESG
     DVILVKSNPS DIINFLSLSK NTMKKMVQNL WWGAGYNVIA VPLAAGILAS IGLILSPAVG
     AILMSLSTII VAINAFTLKL K