ID A0A0W1KIT4_9ACTO Unreviewed; 780 AA.
AC A0A0W1KIT4;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE SubName: Full=Putative copper-importing P-type ATPase A {ECO:0000313|EMBL:KTF03533.1};
DE EC=3.6.3.54 {ECO:0000313|EMBL:KTF03533.1};
GN Name=copA {ECO:0000313|EMBL:KTF03533.1};
GN ORFNames=AQZ59_01663 {ECO:0000313|EMBL:KTF03533.1};
OS Trueperella bernardiae.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Trueperella.
OX NCBI_TaxID=59561 {ECO:0000313|EMBL:KTF03533.1, ECO:0000313|Proteomes:UP000054404};
RN [1] {ECO:0000313|EMBL:KTF03533.1, ECO:0000313|Proteomes:UP000054404}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LCDC 89-0504 {ECO:0000313|EMBL:KTF03533.1,
RC ECO:0000313|Proteomes:UP000054404};
RA Bernier A.-M., Bernard K.;
RT "Draft Genome Sequence of the Type Strain Trueperella bernardiae LCDC 89-
RT 0504T, Isolated from Blood Culture.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KTF03533.1}.
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DR EMBL; LNIZ01000009; KTF03533.1; -; Genomic_DNA.
DR RefSeq; WP_062614176.1; NZ_LNIZ01000009.1.
DR AlphaFoldDB; A0A0W1KIT4; -.
DR STRING; 59561.AQZ59_01663; -.
DR PATRIC; fig|59561.3.peg.1656; -.
DR OrthoDB; 7059309at2; -.
DR Proteomes; UP000054404; Unassembled WGS sequence.
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; TIGR01525; ATPase-IB_hvy; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 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; 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; PS01229; COF_2; 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 Hydrolase {ECO:0000313|EMBL:KTF03533.1};
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:UP000054404};
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 105..123
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 129..148
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 169..190
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 210..228
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 367..388
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 394..421
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 735..754
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 2..69
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 780 AA; 80037 MW; CC84BD545987D53A CRC64;
MIEVDLAVRG MTCASCVARV EKKLNKVPGV TAVVNLATER AHIELDDSAA ELSNEELVGT
VVKAGYDASV ISRTGDAPDA DMIQAAEAAA EASAQARVAD LWRRFVVSAV LSVPVVGLSM
VPALQFPGWQ WVIGAVSLVV AFWCGWPFHR AAFRAARYGS STMDTLVSLG VLASMGWSLW
ALTLGGAGRI GYTMHMTGVH GLGHAAEPHL YFETSAMIVT FLLIGRWLEA RSRRSAGDAL
RSLLELGASE ALLVRRAGSD DTVEQVVPVA QLRVGDVFRV RPGQTVATDG VIVAGSSSID
ASLVTGESLP VDVGEGDEVT GATLNTHGSI EVRATRVGKD TTLAQMGRLL AEAQTGKAPV
QRIADQISAV FVPVVILIAL ATFGVRMFTD NAEMALASAI TVLVVACPCA LGLATPTALL
VGSGRLSRLG ALIRGPEVLE GAHAVDTIML DKTGTLTSGV MSVSEVEAAA GAGFGRIGTG
ADAADAESAA SGADSGTAGT RAADAVLALA AGLESHSEHP IAQAIVRSAR ERGITPAPVS
DFANHAGMGV AGTAGGERVA AGRLTWLAAN VPSDLAERAE DLAREGASVV VVTRGNTALG
LIAVRDTVRP EAADTLAALR DRGLTPVLVT GDNAPAATTV AAELGIEDVR ADVLPEQKLE
VLKELQATGK KVAMVGDGVN DAAALAGADL SIAMGSGTDV AKAAADITIV NSDIRAIPNS
LRVSARTLQI IKENLAWAFA YNLIAIPLAV FGVIVPGIAA FAMASSSVIV VGNSLRLRNA
//
