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Database: UniProt
Entry: R4T093_9PSEU
LinkDB: R4T093_9PSEU
Original site: R4T093_9PSEU 
ID   R4T093_9PSEU            Unreviewed;       751 AA.
AC   R4T093;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 64.
DE   SubName: Full=Cu2+-exporting ATPase {ECO:0000313|EMBL:AGM04123.1};
GN   Name=copA {ECO:0000313|EMBL:AGM04123.1};
GN   ORFNames=AORI_1535 {ECO:0000313|EMBL:AGM04123.1};
OS   Amycolatopsis keratiniphila.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Amycolatopsis; Amycolatopsis japonica group.
OX   NCBI_TaxID=129921 {ECO:0000313|EMBL:AGM04123.1, ECO:0000313|Proteomes:UP000013968};
RN   [1] {ECO:0000313|EMBL:AGM04123.1, ECO:0000313|Proteomes:UP000013968}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HCCB10007 {ECO:0000313|EMBL:AGM04123.1,
RC   ECO:0000313|Proteomes:UP000013968};
RX   PubMed=23627759; DOI=10.1186/1471-2164-14-289;
RA   Tang B., Wang Q., Yang M., Xie F., Zhu Y., Zhuo Y., Wang S., Gao H.,
RA   Ding X., Zhang L., Zhao G., Zheng H.;
RT   "ContigScape: a Cytoscape plugin facilitating microbial genome gap
RT   closing.";
RL   BMC Genomics 14:289-289(2013).
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
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; CP003410; AGM04123.1; -; Genomic_DNA.
DR   RefSeq; WP_016331928.1; NC_021252.1.
DR   AlphaFoldDB; R4T093; -.
DR   KEGG; aoi:AORI_1535; -.
DR   PATRIC; fig|1156913.3.peg.1569; -.
DR   HOGENOM; CLU_001771_0_3_11; -.
DR   Proteomes; UP000013968; 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   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; PR00120; HATPASE.
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:UP000013968};
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        102..119
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        125..143
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        163..186
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        206..224
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        358..378
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        384..407
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        700..717
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        723..741
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   DOMAIN          11..75
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
SQ   SEQUENCE   751 AA;  78261 MW;  6B9989DCA32A94A4 CRC64;
     MTSDLDQATT AEVELAITGM TCASCAMRIE KKLNKLDGVT ATVNYATEKA KVTYSGEIEP
     QRLIEQVEAA GYAAALPAPP KQEQPDGPVE EADPIAPLRQ RLIGSTVLSV PVILLAMVPA
     FQFTYWQWIS LTLAAPVLVW AAWPFHKAAW ANLRHGAATM DTLISMGTLA AFLWSLYALL
     FGSAGTPGMT HAFELTVERM AGDGNIYLEV AAGVTTFILA GRYFEARSKR RAGAALRALL
     ELGAKDVAVL RDGKEERIPV DRLVVGDRFV VRPGEKIATD GVIVEGSSAV DASMLTGESV
     PVEVGPGDAV VGATVNAGGR LVVRAKRVGA DTQLAQMAKL VEDAQTGKAQ VQRLADRVSG
     VFVPIVIALA VGTLMFWLGA GGSVAAAFTA AVAVLIIACP CALGLATPTA LLVGTGRGAQ
     LGILIKGPEV LESTRSVDTV VLDKTGTVTT GQMSLVAVHV AEDADEETTL RLAGALENAS
     EHPIAQAIAR AARERVGELP AVEEFTNVEG LGVQGIVDGK AVLAGRSALL EEWAHHLPPD
     LAEKKAAEEK DGRTAIAVGW DGKARAVLVV ADTVKPTSAE AITQLRALGL TPVLLTGDNE
     AVARAVAAEV GITEVIAEVL PKDKVDVVKR LQGEGKVVAM VGDGVNDAAA LAQADLGLAM
     GTGTDVAIEA SDLTLVRGDL RAAVDAIRLS RRTLRTIKGN LFWAFAYNVA ALPLAAAGLL
     NPMIAGAAMA FSSVFVVTNS LRLKGFRSTA S
//
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