ID E3HKU6_ACHXA Unreviewed; 768 AA.
AC E3HKU6;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE SubName: Full=Copper-translocating P-type ATPase 2 {ECO:0000313|EMBL:ADP14471.1};
DE EC=3.6.3.4 {ECO:0000313|EMBL:ADP14471.1};
GN OrderedLocusNames=AXYL_01127 {ECO:0000313|EMBL:ADP14471.1};
OS Achromobacter xylosoxidans (strain A8).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Achromobacter.
OX NCBI_TaxID=762376 {ECO:0000313|EMBL:ADP14471.1, ECO:0000313|Proteomes:UP000006876};
RN [1] {ECO:0000313|EMBL:ADP14471.1, ECO:0000313|Proteomes:UP000006876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A8 {ECO:0000313|EMBL:ADP14471.1,
RC ECO:0000313|Proteomes:UP000006876};
RX PubMed=21097610; DOI=10.1128/JB.01299-10;
RA Strnad H., Ridl J., Paces J., Kolar M., Vlcek C., Paces V.;
RT "Complete genome sequence of the haloaromatic acids-degrading bacterium
RT Achromobacter xylosoxidans A8.";
RL J. Bacteriol. 193:791-792(2011).
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}.
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DR EMBL; CP002287; ADP14471.1; -; Genomic_DNA.
DR AlphaFoldDB; E3HKU6; -.
DR STRING; 762376.AXYL_01127; -.
DR KEGG; axy:AXYL_01127; -.
DR eggNOG; COG2217; Bacteria.
DR HOGENOM; CLU_001771_0_3_4; -.
DR Proteomes; UP000006876; Chromosome.
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; 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 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 Hydrolase {ECO:0000313|EMBL:ADP14471.1};
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 118..135
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 147..166
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 178..197
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 217..235
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 370..392
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 398..421
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 714..733
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 739..761
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 7..38
FT /note="YHS"
FT /evidence="ECO:0000259|Pfam:PF04945"
FT DOMAIN 74..99
FT /note="Heavy metal binding"
FT /evidence="ECO:0000259|Pfam:PF19335"
FT REGION 45..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 768 AA; 80586 MW; F2CC8F951519E05D CRC64;
MAVTAASEHR STHLGNTYLF CSTGCKAKFD ADPARYASGG AGIGTGSGHA PHHHASTAIS
PAPAASPTAP GTIYTCPMHP EIRQDHPGIC PKCGMTLEPL LPDLDDDNPE LRDFSRRFWW
TLPLTLVVLA LAMLGERLHL MDMATQSWVE LVLSLPIVLW AGWPFFSRGW LSVVNRSPNM
WTLIGLGTGA AFIYSVVATV APEVFPASFM SMGRVGVYFE AAAVIISLTL LGQVLELKAR
SQTSAAIKSL LGLAPKTARR INADGSEEDV PLSHVHVGDL LRIRPGEKVP VDGIVHEGSS
SIDESMLTGE PLPVSKRAGD KVIGATLNTS GALVMRSERI GSDTVLSQIV QMVAQAQRSK
APMQRMADVV AGYFVMAVVA IAVTTLFVWG FFGPQPTWVY GLINAVAVLI IACPCALGLA
TPMSIMVATG RGATQGVLFR DAAAIENLRK VDTLVIDKTG TLTEGRPAFD QVVAAPGFTN
DEVLRLAASL DQGSEHPLAD AIVQAARAQG LQLVKPQSFE SGTGIGVRGK VEHRQLALGN
TVLMEQSGVS VEPLVPQAEA LRGEGASVMY LAVDGQLAGL LAVSDPVKGS TPEALAALKA
AGLRVIMATG DGQTTAKAVG ARLGIDEVHG EVKPADKLML IERLQKEGRI VAMAGDGIND
APALAKADVG IAMGTGTDVA MNSAQVTLVK GDLRGIAVAR TLSVSTVRNM KQNLMFAFLY
NALGIPIAAG VLYPLTGWLL SPLIAALAMS LSSASVVGNA LRLRASRL
//
