ID A0A258P252_9BURK Unreviewed; 791 AA.
AC A0A258P252;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Copper-translocating P-type ATPase {ECO:0000313|EMBL:OYY36625.1};
GN ORFNames=B7Y60_10650 {ECO:0000313|EMBL:OYY36625.1};
OS Polaromonas sp. 35-63-35.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Polaromonas.
OX NCBI_TaxID=1970418 {ECO:0000313|EMBL:OYY36625.1, ECO:0000313|Proteomes:UP000216365};
RN [1] {ECO:0000313|EMBL:OYY36625.1, ECO:0000313|Proteomes:UP000216365}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=35-63-35 {ECO:0000313|EMBL:OYY36625.1};
RA Kantor R.S., Colenbrander Nelson T., Marshall S., Bennett D., Apte S.,
RA Camacho D., Thomas B.C., Warren L.A., Banfield J.F.;
RT "Lifting the veil on microbial sulfur biogeochemistry in mining
RT wastewaters.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
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:OYY36625.1}.
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DR EMBL; NCFQ01000007; OYY36625.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A258P252; -.
DR Proteomes; UP000216365; 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:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0015662; F:P-type ion transporter activity; IEA:UniProt.
DR CDD; cd02094; 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 Gene3D; 1.10.620.20; Ribonucleotide Reductase, subunit A; 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; IPR045800; HMBD.
DR InterPro; IPR027256; P-typ_ATPase_IB.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR InterPro; IPR012348; RNR-like.
DR InterPro; IPR011017; TRASH_dom.
DR InterPro; IPR007029; YHS_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:SF8; COPPER-TRANSPORTING ATPASE 2; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF19335; HMBD; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR Pfam; PF04945; YHS; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00943; CUATPASE.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SMART; SM00746; TRASH; 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|RuleBase:RU362081};
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 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}.
FT TRANSMEM 137..160
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 166..186
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 198..216
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 228..250
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 389..411
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 417..440
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 733..752
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 758..780
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 26..63
FT /note="TRASH"
FT /evidence="ECO:0000259|SMART:SM00746"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 791 AA; 82556 MW; D521F4E988F1F924 CRC64;
MAAGSAHGTG HDHSRTHSDD PAGLRDPVCG MAVTTASGHQ LEHEGRSWYF CSAACLAKFA
AHPSAYLDKP TDAPAAEAKT AVADDQAGTT VYTCPMHPEI RQDHPGNCPI CGMTLEPVMP
SLDEEENPEL QSFTRRFWWT LPLTVVVTVL AMAGHQFGWF DMATQSWIEL VLTLPVVLWA
GWPFFVRGAQ SVIHRSPNMW TLIGLGTGAA FVYSVVATMA PGVFPDSFIS MGRVAVYFEA
AAVIISLTLL GQMLELKARS QTSAAIKSLL GLAPKTARRI RADGAEEDVP LTHVHVGDSL
RVRPGEKVPV DGVVTEGSSA VDESMLTGEP LPVSKRAGDK LIGATLNTSG ALVMRSERVG
AQTMLSQIVQ MVAQAQRSKA PMQRMADQVA GWFVMAVVTV AVLTFFGWGF FGPQPSWVYG
LINAVAVLII ACPCALGLAT PMSIMVATGK AAGQGILFRD AAAIEHLRTV DVLIVDKTGT
LTAGKPAFDR AVPAAGFSAD EVLRLAASLD QGSEHPLADA IVAAARERGL ALDKPESFES
ASGIGVSGNV AGRALALGNT ALMEQTGVAV DVLLTQAEAL RAEGASVMHL AVDGQLAGLL
AVADPVKAST PEALATLKVA GLRVIMATGD GLTTAKAVAA RLGLTEVHGG VQPADKLVLV
KRLQEEGHIV AMAGDGINDA PALAQANVGI AMGTGTDVAM NSAQVTLVKG DLRGIAQARA
ISEATIANMK QNLGFAFVYN ALGVPLAAGL LYPFTGWLLS PMIAALAMSL SSVSVISNAL
RLRKARLSIS A
//
