ID G5JK61_9STAP Unreviewed; 695 AA.
AC G5JK61;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Probable copper-transporting P-type ATPase B {ECO:0000256|ARBA:ARBA00041014};
DE EC=7.2.2.8 {ECO:0000256|ARBA:ARBA00012517};
GN ORFNames=SS7213T_09364 {ECO:0000313|EMBL:EHJ07391.1};
OS Staphylococcus simiae CCM 7213 = CCUG 51256.
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=911238 {ECO:0000313|EMBL:EHJ07391.1, ECO:0000313|Proteomes:UP000005413};
RN [1] {ECO:0000313|EMBL:EHJ07391.1, ECO:0000313|Proteomes:UP000005413}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCM 7213 {ECO:0000313|EMBL:EHJ07391.1,
RC ECO:0000313|Proteomes:UP000005413};
RX PubMed=22272658; DOI=10.1186/1471-2164-13-38;
RA Suzuki H., Lefebure T., Pavinski Bitar P., Stanhope M.J.;
RT "Comparative genomic analysis of the genus Staphylococcus including
RT Staphylococcus aureus and its newly described sister species Staphylococcus
RT simiae.";
RL BMC Genomics 13:38-38(2012).
CC -!- FUNCTION: Involved in copper transport.
CC {ECO:0000256|ARBA:ARBA00037427}.
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 Evidence={ECO:0000256|ARBA:ARBA00001390};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU362081}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IB subfamily. {ECO:0000256|ARBA:ARBA00006024,
CC ECO:0000256|RuleBase:RU362081}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHJ07391.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AEUN01000475; EHJ07391.1; -; Genomic_DNA.
DR AlphaFoldDB; G5JK61; -.
DR PATRIC; fig|911238.3.peg.1631; -.
DR Proteomes; UP000005413; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0019829; F:ATPase-coupled monoatomic cation transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006825; P:copper ion transport; IEA:UniProtKB-KW.
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 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 {ECO:0000256|RuleBase:RU362081};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|RuleBase:RU362081}; Copper {ECO:0000256|ARBA:ARBA00023008};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362081};
KW Metal-binding {ECO:0000256|RuleBase:RU362081};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362081};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362081};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362081}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 53..72
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 78..97
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 118..139
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 151..168
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 303..325
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 337..357
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 644..666
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 672..692
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 695 AA; 75823 MW; 2F4F693EEEE9DEF9 CRC64;
MDKKHQMHMN HSEHEHHENH SGHDHHGNHS GHEHHGNHSG HDHHHHGNFK QKFFVSLIFA
IPIIILSPMM GLRLPFQFTF PGSDWIVLIL ATILFFYGGK PFLSGAKDEV ASKKPGMMTL
VALGITVAYI YSLYAFYLNH FTATSQHTMD FFWELATLIL IMLLGHWIEM NAVGNASNAL
QKMAELLPNT ATKITQDSQR ETVKIADIHV DDVVEVKTGE SIPTDGVIIK GDTAVDESLV
TGESKQVPKG IDDKVIAGSI NGAGSIQIKV TATGEESYLS QVMDLISQAQ NDKSQAELLS
DRVAGYLFYF AVTVGIIAFI TWMLITHSVD FALERLVTVL VIACPHALGL AIPLVTARST
SLGAQNGLII KNREAVELAQ HIDYVMMDKT GTLTEGNFSV NHVESYSNQY TNNEILGLFA
SLEGHSNHPL ALSINNYAEQ QQISVPQSQD VQTISGVGLE GHINNQKFTI ANVSYLDQHD
MSYDQSQFEQ LAQQGNSISY LIADQTVLGI IAQGDQIKES SKQMVSDLKE RGIEPVMLTG
DNKAVAKAVA KELGISHVHA QLMPEDKEQI IKDYQAKGHK VMMVGDGIND APSLVRADIG
LAIGAGTDVA VESGDIILVK SNPADIIHFF TLSKNTMRKM IQNLWWGAGY NIVAVPLAAG
ILASIGLILS PAIGAVLMSL STVIVAINAF TLKLK
//
