ID F9ZUG8_ACICS Unreviewed; 862 AA.
AC F9ZUG8;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=Heavy metal translocating P-type ATPase {ECO:0000313|EMBL:AEK59617.1};
GN OrderedLocusNames=Atc_m086 {ECO:0000313|EMBL:AEK59617.1};
OS Acidithiobacillus caldus (strain SM-1).
OG Plasmid megaplasmid {ECO:0000313|EMBL:AEK59617.1}.
OC Bacteria; Pseudomonadota; Acidithiobacillia; Acidithiobacillales;
OC Acidithiobacillaceae; Acidithiobacillus.
OX NCBI_TaxID=990288 {ECO:0000313|EMBL:AEK59617.1, ECO:0000313|Proteomes:UP000006135};
RN [1] {ECO:0000313|EMBL:AEK59617.1, ECO:0000313|Proteomes:UP000006135}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM-1 {ECO:0000313|EMBL:AEK59617.1,
RC ECO:0000313|Proteomes:UP000006135};
RC PLASMID=Plasmid megaplasmid {ECO:0000313|Proteomes:UP000006135};
RX PubMed=21703548; DOI=10.1016/j.jgg.2011.04.006;
RA You X.Y., Guo X., Zheng H.J., Zhang M.J., Liu L.J., Zhu Y.Q., Zhu B.,
RA Wang S.Y., Zhao G.P., Poetsch A., Jiang C.Y., Liu S.J.;
RT "Unraveling the Acidithiobacillus caldus complete genome and its central
RT metabolisms for carbon assimilation.";
RL J. Genet. Genomics 38:243-252(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; CP002574; AEK59617.1; -; Genomic_DNA.
DR AlphaFoldDB; F9ZUG8; -.
DR KEGG; acu:Atc_m086; -.
DR HOGENOM; CLU_001771_0_3_6; -.
DR Proteomes; UP000006135; Plasmid megaplasmid.
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:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0015662; F:P-type ion transporter activity; IEA:UniProt.
DR CDD; cd00371; HMA; 2.
DR CDD; cd02094; P-type_ATPase_Cu-like; 1.
DR Gene3D; 3.30.70.100; -; 2.
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; IPR017969; Heavy-metal-associated_CS.
DR InterPro; IPR006122; HMA_Cu_ion-bd.
DR InterPro; IPR006121; HMA_dom.
DR InterPro; IPR036163; HMA_dom_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 NCBIfam; TIGR00003; copper ion binding protein; 2.
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; PF00403; HMA; 2.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00943; CUATPASE.
DR PRINTS; PR00942; CUATPASEI.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 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 SUPFAM; SSF55008; HMA, heavy metal-associated domain; 2.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS01229; COF_2; 1.
DR PROSITE; PS01047; HMA_1; 2.
DR PROSITE; PS50846; HMA_2; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU362081};
KW Cell membrane {ECO:0000256|RuleBase:RU362081};
KW Copper {ECO:0000256|ARBA:ARBA00023008};
KW Copper transport {ECO:0000256|ARBA:ARBA00022796};
KW Ion transport {ECO:0000256|ARBA:ARBA00022796};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362081};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU362081};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362081};
KW Plasmid {ECO:0000313|EMBL:AEK59617.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006135};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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:ARBA00022796}.
FT TRANSMEM 194..217
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 229..247
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 268..290
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 296..315
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 450..472
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 478..499
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 789..812
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 818..835
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 33..99
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 101..167
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 862 AA; 91599 MW; 5A9B7CC21D0A4333 CRC64;
MHIVSRNPSL RRDPLYTAGI TRGDIFMDDK TRGHLEIGID GMTCASCSAR VERALGKLPG
VTSANVNLAT ERAEVLFDPQ QLDAARIAET IRETGYVPVT DEIDLVVEGM TCASCVGRVE
RALRQQSGVL EAVVNLATER AHVRYIPAMI STDELASTVS EAGYAAHPVL EDGEQDVNEA
DQRRVSLRAM GRDVIVAAVL AMAILVLSMG ATFVPAFDHA LMVASPFAHF WEWVQFVLAS
IVLFGPGRRF FRPGLIAYRH LSPDMNSLVA TGTGAAWAYS VLVLVAPAWF PLDARHVYFD
SAAVVIAAVL AGKYLEGLAK GRTSSAIRKL AGLQAKTAHR LDANGIEQEM PVSRLRTGER
IVVRPGERIP VDGRVVEGRA HVDEAMLTGE PLPSAKTMDD TVVGGTICQD GRLVVEATSV
GRDTVLAHII HLVESAQTGK LPIQGLTDRA VRVFTPVVLV IALTTFGVWI ALTGNVSIAL
VAAVAVLVVA CPCAMGLATP AAIMVGTGRA AELGVLFRKG EALETLSHVD TLLFDKTGTL
TEGRPALVDQ GGPDPATALR LAAALESASE HPLGRAIVTA AGERGIHLPT VNNFRSIAGY
GIEGEVEGRM VRVGARRFME RENVLLGDNA ETVTQIENDG RTVVFVAVDT TLIGWLAIAD
RIKPEAYMVV QALRARGLQV AMVTGDTRAT AQSVARQLQI EQVHAEVLPQ DKAKVVTQLQ
EQGRRVAFVG DGINDAPALA QANVGIALAS GTDIAIEAAD VTLTRGQLGE VVTALTAARR
TLSNIRGNLF WAFFYNILLI PVAAGVAVPI GIHLNPMVAG VAMGLSSVFV LSNSLRLKRL
KAYVPTVTPG AVPNTALEPA HS
//
