COPB_STAEQ
ID COPB_STAEQ Reviewed; 674 AA.
AC Q5HKB0;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Probable copper-transporting P-type ATPase B;
DE EC=7.2.2.8;
GN Name=copB; OrderedLocusNames=SERP2438;
OS Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176279;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35984 / RP62A;
RX PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete genome
RT analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT strain.";
RL J. Bacteriol. 187:2426-2438(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=AAW53295.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000029; AAW53295.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q5HKB0; -.
DR SMR; Q5HKB0; -.
DR STRING; 176279.SERP2438; -.
DR EnsemblBacteria; AAW53295; AAW53295; SERP2438.
DR KEGG; ser:SERP2438; -.
DR eggNOG; COG2217; Bacteria.
DR HOGENOM; CLU_001771_11_2_9; -.
DR Proteomes; UP000000531; 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 Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..674
FT /note="Probable copper-transporting P-type ATPase B"
FT /id="PRO_0000350607"
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; 73220 MW; AE5722CF22687E7E CRC64;
MNHSNQMHHD NHESHNHHSG 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 LIHNKTYKIT NVSYLDQHGF EYDNDLFIKL AQQGNSISYL
IEDQQVIGMI AQGDQIKESS KQMVADLLSR NITPVMLTGD NNEVAHAVAK ELGISDVHAQ
LMPEDKESII KDYQSNGNKV MMVGDGINDA PSLIRADIGI AIGAGTDVAV DSGDIILVKS
NPSDIIHFLT LSNNTMRKMV QNLWWGAGYN IVAVPLAAGI LAFIGLILSP AIGAILMSLS
TVIVAINAFT LKLK
