ID C9R973_AMMDK Unreviewed; 720 AA.
AC C9R973;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=P-type Cu(+) transporter {ECO:0000256|ARBA:ARBA00012517};
DE EC=7.2.2.8 {ECO:0000256|ARBA:ARBA00012517};
GN OrderedLocusNames=Adeg_1763 {ECO:0000313|EMBL:ACX52852.1};
OS Ammonifex degensii (strain DSM 10501 / KC4).
OC Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Ammonifex.
OX NCBI_TaxID=429009 {ECO:0000313|EMBL:ACX52852.1, ECO:0000313|Proteomes:UP000002620};
RN [1] {ECO:0000313|EMBL:ACX52852.1, ECO:0000313|Proteomes:UP000002620}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10501 / KC4 {ECO:0000313|Proteomes:UP000002620};
RG US DOE Joint Genome Institute;
RA Kerfeld C., Goodner B., Huber H., Stetter K., Lucas S., Copeland A.,
RA Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L.,
RA Pitluck S., Saunders E., Brettin T., Detter J.C., Han C., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Ovchinnikova G., Richardson P.;
RT "Complete sequence of chromosome of Ammonifex degensii KC4.";
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP001785; ACX52852.1; -; Genomic_DNA.
DR AlphaFoldDB; C9R973; -.
DR STRING; 429009.Adeg_1763; -.
DR KEGG; adg:Adeg_1763; -.
DR eggNOG; COG2217; Bacteria.
DR HOGENOM; CLU_001771_11_2_9; -.
DR OrthoDB; 9760364at2; -.
DR Proteomes; UP000002620; 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:0006825; P:copper ion transport; IEA:UniProtKB-KW.
DR CDD; cd00371; HMA; 1.
DR CDD; cd02094; P-type_ATPase_Cu-like; 1.
DR Gene3D; 3.30.70.100; -; 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; IPR017969; Heavy-metal-associated_CS.
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 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; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00943; CUATPASE.
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; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS01047; HMA_1; 1.
DR PROSITE; PS50846; HMA_2; 1.
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 Reference proteome {ECO:0000313|Proteomes:UP000002620};
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 88..107
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 119..141
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 332..354
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 366..390
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 673..692
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 698..716
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 4..69
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 720 AA; 77400 MW; B7764B1184012783 CRC64;
MLVSEYLLAV KNLTCAACAA NLERKLKELP GVEEAAVSVV SGRIRLKLSH PTVLTQVMDY
VKAAGFSVEL LEEETAKTVS SEGRSSELFW PLLAAFLLTL PLIYRSLAEL FSWPLPSFLA
GNLVPLLLAS AVQFGPGLIF YRGAWRAMTS RTATMDTLVA LGTTAAYVTQ IVNWYHALPS
HHEPAGVIIT TILLGRYLEE KAQQKTGKAL RELHSLKPQK ARVLRGDKEE EVPLEEVKVG
ELLVVRPGER IPVDGVVEKG FSTVDESLLT GESLPVEKHP GNQVAGGTLN HNGVLYIRAT
RVGSQTTLAR IIRLVTEAQE QKAHSQRLAD QIVARFVPAV LVLSLLTLVG WGVFRGDWEQ
GLRQMIAVLV VACPCALGLA TPTAVIVGLG KGAKAGVLFR GGEYLEKAAR IDTVVFDKTG
TLTHGRLEVT AFYPAPGFDR EKVLSLVAAT EAFSEHPVGR ALARLAPAPP VATGEIQVRA
LPGFGLEAQV QGREVLLGKE ELLREKGIDT EALAEKAREI VSRGATVVFV AVDRRLAGVI
GVADTVREEA RSTVEKLERL GIKVVLATGD NPVTARQVAE RAGITTWYAG LLPEDKVKLV
KELQREGRRV AMVGDGINDA PALASADLGL AIDTGTDVAA EVAGVILFRG DLRGVERALI
LGKAVARKIK QNLFWAFIYN ILALPAAALG FLSPVMAAAL MGLSDVSVVS SSLLLYRLRM
//
