ID A0A140E4I4_9GAMM Unreviewed; 749 AA.
AC A0A140E4I4;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=Copper-exporting P-type ATPase {ECO:0000256|ARBA:ARBA00015102};
DE EC=7.2.2.8 {ECO:0000256|ARBA:ARBA00012517};
DE AltName: Full=Copper-exporting P-type ATPase A {ECO:0000256|ARBA:ARBA00029719};
DE AltName: Full=Cu(+)-exporting ATPase {ECO:0000256|ARBA:ARBA00033239};
GN Name=copA {ECO:0000313|EMBL:AMK75308.1};
GN ORFNames=JT25_002195 {ECO:0000313|EMBL:AMK75308.1};
OS Methylomonas denitrificans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC Methylococcaceae; Methylomonas.
OX NCBI_TaxID=1538553 {ECO:0000313|EMBL:AMK75308.1, ECO:0000313|Proteomes:UP000030512};
RN [1] {ECO:0000313|EMBL:AMK75308.1, ECO:0000313|Proteomes:UP000030512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FJG1 {ECO:0000313|EMBL:AMK75308.1,
RC ECO:0000313|Proteomes:UP000030512};
RX PubMed=25580993; DOI=10.1111/1462-2920.12772;
RA Kits K.D., Klotz M.G., Stein L.Y.;
RT "Methane oxidation coupled to nitrate reduction under hypoxia by the
RT Gammaproteobacterium Methylomonas denitrificans, sp. nov. type strain
RT FJG1.";
RL Environ. Microbiol. 17:3219-3232(2015).
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; CP014476; AMK75308.1; -; Genomic_DNA.
DR RefSeq; WP_036272074.1; NZ_CP014476.1.
DR AlphaFoldDB; A0A140E4I4; -.
DR STRING; 1538553.JT25_002195; -.
DR KEGG; mdn:JT25_002195; -.
DR OrthoDB; 9814270at2; -.
DR Proteomes; UP000030512; 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:0015662; F:P-type ion transporter activity; IEA:UniProt.
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:SF6; COPPER-EXPORTING P-TYPE ATPASE; 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 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:UP000030512};
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 96..116
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 167..186
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 192..211
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 348..370
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 376..408
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 692..711
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 717..735
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 11..74
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 749 AA; 78439 MW; D949D191CC1ED77A CRC64;
MTLDQSTNQQ QEVRLSILGM RCAGCVSAVE TALQSVPGVE AVVVNFADHS ATVGGNPDHQ
AMKQALKSAG YDAAVMEGLE DPSEEERQEE ERYRDLLCKA GVAGALGLPL MLGAHLDLFP
VMGSAAGTVF WSEVALLTLA VMFYSGGHFF HSALKLLLVK QANMDTLIAL GTGSAWLYSC
IVIDYSSQLP SLSAHAYFEA SAVILAFINL GSALETRARG KTSAAIRALI GLQPRTARVV
REGQEIDIPI EQVGLGETLR VRPGEKIAVD GVVLEGHSTI DESMLTGESM PVEKVEGASV
AAGTINQQGS FLFSATRIGR DTALAQIIQS VRQAQNSKPA IAKLADKISA VFVPAVVIIS
VLTFLIWLSI GPDPAMGYAF VTSMTVLVIA CPCALGLATP ISVMVAVGRA AQMGILIRKG
EALQSAGKLT CLILDKTGTV TAGKPSLAEV IAFGDYDEAR VLQYAASLES GSEHPLAAAI
LTAAEQKQLT LDKVRKFQAV AGHGIVGRIA DRQCLFGNAA LLAEHGIDDS NHRDKMAELA
AKGQTPMFLA VENAVVGIVS VADPIKPDSA AAVQQLRQRG IRVLMVTGDN DITARAIAAQ
AGISEVRAQV LPQDKAAVVK ALQQQGEIVG MVGDGINDAP ALAQADVGFA IGTGTDVAIE
SADIVLLQGS LLKVSEAMAL STLTVANIKQ NLLGAFFYNT IGIPVAAGLL YPMFGLLLNP
MIAGAAMAMS SVTVVSNANR LRWIKLDIG
//
