ID COPB_STAHJ Reviewed; 674 AA.
AC Q4LAB1;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 2.
DT 24-JAN-2024, entry version 127.
DE RecName: Full=Probable copper-transporting P-type ATPase B;
DE EC=7.2.2.8;
GN Name=copB; OrderedLocusNames=SH0105;
OS Staphylococcus haemolyticus (strain JCSC1435).
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=279808;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCSC1435;
RX PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA Hiramatsu K.;
RT "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT extreme plasticity of its genome and the evolution of human-colonizing
RT staphylococcal species.";
RL J. Bacteriol. 187:7292-7308(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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE03414.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AP006716; BAE03414.1; ALT_FRAME; Genomic_DNA.
DR AlphaFoldDB; Q4LAB1; -.
DR SMR; Q4LAB1; -.
DR KEGG; sha:SH0105; -.
DR eggNOG; COG2217; Bacteria.
DR HOGENOM; CLU_001771_6_3_9; -.
DR Proteomes; UP000000543; Chromosome.
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 CDD; cd07552; P-type_ATPase_Cu-like; 1.
DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1.
DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 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 NCBIfam; TIGR01511; ATPase-IB1_Cu; 1.
DR NCBIfam; TIGR01525; ATPase-IB_hvy; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
DR PANTHER; PTHR43520; ATP7, ISOFORM B; 1.
DR PANTHER; PTHR43520:SF5; CATION-TRANSPORTING P-TYPE ATPASE-RELATED; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00120; HATPASE.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR SUPFAM; SSF56784; HAD-like; 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_0000350608"
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..20
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; 73255 MW; 42BE404EA8C59E06 CRC64;
MNHSNHMHHD NHESHHHYSG HAHHHGNFKV KFFVSLIFAI PIILLSPMMG VNLPFQFTFP
GSEWVVLILS TILFFYGGKP FLSGGKDEIA AKKPGMMTLV ALGISVAYIY SLYAFYMNNF
SSATGHTMDF FWELATLILI MLLGHWIEMN AVGNAGDALK KMAELLPNSA IKVMDNGQRE
EVKISDIMTD DIVEVKAGES IPTDGIIVQG QTSVDESLVT GESKKVQKNQ NDNVIGGSIN
GSGTIQVKVT AVGEDGYLSQ VMGLVNQAQN DKSSAELLSD KVAGYLFYFA VIVGVISFIV
WMLIQNDVDF ALERLVTVLV IACPHALGLA IPLVTARSTS IGAHNGLIIK NRESVEIAQH
IDYVMMDKTG TLTEGNFSVN HYESFKNDLS NDTILSLFAS LESQSNHPLA ISIVDFTKSK
NVSFTNPQDV NNIPGVGLEG LIDNKTYKIT NVSYLDQHGF EYDNDLFIKL AQQGNSISYL
IEDQQVIGMI AQGDQIKESS KQMVADLLSR HITPVMLTGD NDEVAHAVAK ELGISDVHAQ
LMPEDKESII KDYQSDGNKV MMVGDGINDA PSLIRADIGI AIGAGTDVAV DSGDIILVKS
NPSDIIHFLT LSNNTMRKMV QNLWWGAGYN IVAVPLAAGA LAFIGLILSP AVGAILMSLS
TVIVAINAFT LKLK
//
