ID A5PD69_9SPHN Unreviewed; 794 AA.
AC A5PD69;
DT 10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 10-JUL-2007, sequence version 1.
DT 08-NOV-2023, entry version 91.
DE SubName: Full=Copper/silver efflux P-type ATPase {ECO:0000313|EMBL:EDL48189.1};
GN ORFNames=ED21_31599 {ECO:0000313|EMBL:EDL48189.1};
OS Erythrobacter sp. SD-21.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX NCBI_TaxID=161528 {ECO:0000313|EMBL:EDL48189.1, ECO:0000313|Proteomes:UP000005498};
RN [1] {ECO:0000313|EMBL:EDL48189.1, ECO:0000313|Proteomes:UP000005498}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SD-21 {ECO:0000313|EMBL:EDL48189.1,
RC ECO:0000313|Proteomes:UP000005498};
RA Tebo B., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (JUN-2007) 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:EDL48189.1}.
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DR EMBL; ABCG01000007; EDL48189.1; -; Genomic_DNA.
DR RefSeq; WP_006834095.1; NZ_ABCG01000007.1.
DR AlphaFoldDB; A5PD69; -.
DR STRING; 161528.ED21_31599; -.
DR eggNOG; COG2217; Bacteria.
DR OrthoDB; 9813266at2; -.
DR Proteomes; UP000005498; 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; IPR009078; Ferritin-like_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; SFLDG00002; C1.7:_P-type_atpase_like; 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; SSF47240; Ferritin-like; 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 Reference proteome {ECO:0000313|Proteomes:UP000005498};
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 127..150
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 162..180
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 232..250
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 385..407
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 413..436
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 729..751
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 757..776
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 23..61
FT /note="TRASH"
FT /evidence="ECO:0000259|SMART:SM00746"
SQ SEQUENCE 794 AA; 84003 MW; DB2F88C81A5A6042 CRC64;
MTDHENCCEP AKAPPGADGV AIDPVCGMSV TIEGAEHRAE HDNAQHYFCS SRCHDKFRAD
PELYLSGEHL NVVEDMPEGT IYTCPMHPEI RQTGPGSCPI CGMALEPETV SLDDGPDPEL
VDMRRRFWWS ALLTLPLFVY AMSDMIPWLS FDQLIEPARA QWAQFVLATP VVLWGGWPFF
VRAWESLKTR NLNMFTLIGI GVGIAYLFSL VATAMPELFP PAFRDHSGRV GVYYEAAAVI
TVLVLLGQVL ELKARGSTSS ALRALLELAP PSAVKIFGSG DEREVPLDEL ESGDRLRVRP
GDKVPVDGEI EEGSSAIDES MVSGEPLPVK KGAGDTVIGG TVNQTGGFIM RATNVGKDTM
LSKIVQMVAE AQRSRAPIQR LADQVAGWFV PAVVMVAVVT FAVWAIWGPA PALTYALVNA
IAVLIIACPC ALGLATPMSV MTGTGKGAQH GILIRNAEAL ETLEKIDTLV VDKTGTLTMG
KPDLVAVNPV EGIDEAEFLA AVAGVEMGSE HPLAHAIVEG ARSRGVSPAD ATDLASTTGE
GVEADVNGRR VAIGNEKMMR RVGISDESWL GTAEAGRTKG QTVMFVAFAG KPAGLIAVAD
PIKPTSANAI AALHARDIRV VMLTGDSRGT AEAVAQEMGI DEVHANVSPE DKHREVERLK
SEGRRVAMAG DGINDAPALA AADVGIAMGT GTDVAIESAG VTLVRGDLTG VVQAIVLSRA
TMRNIRQNLF FAFAYNTLGI PVAAGVLFPA FGLLLNPMIA AAAMSLSSVS VIANALRLRG
LRLSTSDGVA EQPA
//
