COPB_STAAT
ID COPB_STAAT Reviewed; 674 AA.
AC A8YZ02;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Probable copper-transporting P-type ATPase B;
DE EC=7.2.2.8;
GN Name=copB; OrderedLocusNames=USA300HOU_0084;
OS Staphylococcus aureus (strain USA300 / TCH1516).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=451516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USA300 / TCH1516;
RX PubMed=17986343; DOI=10.1186/1471-2180-7-99;
RA Highlander S.K., Hulten K.G., Qin X., Jiang H., Yerrapragada S.,
RA Mason E.O. Jr., Shang Y., Williams T.M., Fortunov R.M., Liu Y., Igboeli O.,
RA Petrosino J., Tirumalai M., Uzman A., Fox G.E., Cardenas A.M., Muzny D.M.,
RA Hemphill L., Ding Y., Dugan S., Blyth P.R., Buhay C.J., Dinh H.H.,
RA Hawes A.C., Holder M., Kovar C.L., Lee S.L., Liu W., Nazareth L.V.,
RA Wang Q., Zhou J., Kaplan S.L., Weinstock G.M.;
RT "Subtle genetic changes enhance virulence of methicillin resistant and
RT sensitive Staphylococcus aureus.";
RL BMC Microbiol. 7:99-99(2007).
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; CP000730; ABX28125.1; -; Genomic_DNA.
DR AlphaFoldDB; A8YZ02; -.
DR SMR; A8YZ02; -.
DR KEGG; sax:USA300HOU_0084; -.
DR HOGENOM; CLU_001771_11_2_9; -.
DR OMA; MALEPMG; -.
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..674
FT /note="Probable copper-transporting P-type ATPase B"
FT /id="PRO_0000350604"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 284..304
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 315..335
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 623..645
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 649..671
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 367
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 565
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 569
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 674 AA; 73167 MW; 4755838406AE5E4B CRC64;
MNHSNQMHHD NHASHDHHSG HAHHHGNFKV KFFVSLIFAI PIILLSPLMG VNLPFQFTFP
GSEWVVLILS TILFFYGGKP FLSGGKDEIA TKKPGMMTLV ALGISVAYIY SLYAFYMNNF
SSATGHTMDF FWELATLILI MLLGHWIEMN AVGNAGDALK KMAELLPNSA IKVMDNGQRE
EVKISDIMTD DIVEVKAGES IPTDGIIVQG QTSIDESLVT GESKKVQKNQ NDNVIGGSIN
GSGTIQVKVT AVGEDGYLSQ VMGLVNQAQN DKSSAELLSD KVAGYLFYFA VSVGVISFIV
WMLIQNDVDF ALERLVTVLV IACPHALGLA IPLVTARSTS IGAHNGLIIK NRESVEIAQH
IDYVMMDKTG TLTEGNFSVN HYESFKNDLS NDTILSLFAS LESQSNHPLA ISIVDFAKSK
NVSFTNPQDV NNIPGVGLEG LIDNKTYKIT NVSYLDKHKL NYDDDLFTKL AQQGNSISYL
IEDQQVIGMI AQGDQIKESS KQMVADLLSR NITPVMLTGD NNEVAHAVAK ELGISDVHAQ
LMPEDKESII KDYQSDGNKV MMVGDGINDA PSLIRADIGI AIGAGTDVAV DSGDIILVKS
NPSDIIHFLT LSNNTMRKMV QNLWWGAGYN IVAVPLAAGI LAFIGLILSP AIGAILMSLS
TIIVAINAFT LKLK
