COPB_STAES
ID COPB_STAES Reviewed; 674 AA.
AC Q8CQF7;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Probable copper-transporting P-type ATPase B;
DE EC=7.2.2.8;
GN Name=copB; OrderedLocusNames=SE_0126;
OS Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176280;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12228 / FDA PCI 1200;
RX PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT "Genome-based analysis of virulence genes in a non-biofilm-forming
RT Staphylococcus epidermidis strain (ATCC 12228).";
RL Mol. Microbiol. 49:1577-1593(2003).
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; AE015929; AAO03723.1; -; Genomic_DNA.
DR RefSeq; NP_763681.1; NC_004461.1.
DR RefSeq; WP_011082563.1; NZ_WBME01000049.1.
DR AlphaFoldDB; Q8CQF7; -.
DR SMR; Q8CQF7; -.
DR STRING; 176280.SE_0126; -.
DR EnsemblBacteria; AAO03723; AAO03723; SE_0126.
DR KEGG; sep:SE_0126; -.
DR PATRIC; fig|176280.10.peg.117; -.
DR eggNOG; COG2217; Bacteria.
DR HOGENOM; CLU_001771_0_3_9; -.
DR OMA; MALEPMG; -.
DR Proteomes; UP000001411; 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..674
FT /note="Probable copper-transporting P-type ATPase B"
FT /id="PRO_0000350606"
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; 73165 MW; 36B60C8EB08FE6ED CRC64;
MNHSNQMHHD NHESHNHHSG HAHHHGNFKV KFFVSLIFAI PIILLSPLMG INLPFQFTFP
GSEWVVLILS TILFFYGGKP FLSGGKDEIA TKKPGMMTLV ALGISVAYIY SLYAFYMNNF
SSATGHTMDF FWELATLILI MLLGHWIEMN AVGNAGDALK KMAELLPNSA IKVMDNGQRE
EVKISDIMTD DIVEVKAGES IPTDGIIVQG QTSIDESLVT GESKKVQKNQ NDNVIGGSIN
GSGTIQVKVT AVGEDGYLSQ VMGLVNQAQN DKSSAELLSD KVAGYLFYFA VIVGVISFIV
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 KDYQSNGNKV MMVGDGINDA PSLIRADIGI AIGAGTDVAV DSGDIILVKS
NPSDIVHFLT LSNNTMRKMV QNLWWGAGYN IVAVPLAAGA LAFVGLILSP AVGAILMSLS
TVIVAINAFT LKLK
