ID Q6ML02_BDEBA Unreviewed; 724 AA.
AC Q6ML02;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 148.
DE SubName: Full=Copper-transporting ATPase copA {ECO:0000313|EMBL:CAE80055.1};
DE EC=3.6.3.4 {ECO:0000313|EMBL:CAE80055.1};
GN Name=copA {ECO:0000313|EMBL:CAE80055.1};
GN OrderedLocusNames=Bd2224 {ECO:0000313|EMBL:CAE80055.1};
OS Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIMB 9529 /
OS HD100).
OC Bacteria; Bdellovibrionota; Bdellovibrionia; Bdellovibrionales;
OC Pseudobdellovibrionaceae; Bdellovibrio.
OX NCBI_TaxID=264462 {ECO:0000313|EMBL:CAE80055.1, ECO:0000313|Proteomes:UP000008080};
RN [1] {ECO:0000313|EMBL:CAE80055.1, ECO:0000313|Proteomes:UP000008080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15356 / DSM 50701 / NCIMB 9529 / HD100
RC {ECO:0000313|Proteomes:UP000008080};
RX PubMed=14752164; DOI=10.1126/science.1093027;
RA Rendulic S., Jagtap P., Rosinus A., Eppinger M., Baar C., Lanz C.,
RA Keller H., Lambert C., Evans K.J., Goesmann A., Meyer F., Sockett R.E.,
RA Schuster S.C.;
RT "A predator unmasked: life cycle of Bdellovibrio bacteriovorus from a
RT genomic perspective.";
RL Science 303:689-692(2004).
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; BX842652; CAE80055.1; -; Genomic_DNA.
DR RefSeq; WP_011164657.1; NC_005363.1.
DR AlphaFoldDB; Q6ML02; -.
DR STRING; 264462.Bd2224; -.
DR KEGG; bba:Bd2224; -.
DR eggNOG; COG2217; Bacteria.
DR HOGENOM; CLU_001771_0_3_7; -.
DR Proteomes; UP000008080; 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; PR00943; CUATPASE.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 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:CAE80055.1};
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:UP000008080};
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..120
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 126..144
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 156..179
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 185..204
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 338..360
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 366..396
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 676..693
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 699..719
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 6..71
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 724 AA; 77500 MW; D2C99B33A1951ABA CRC64;
METQGNSAEL QLIGMSCVNC AGKIEKTLNG LPGVTATVNF ATEKAQVNLG DSPLTVGNLI
KTIQELGYQA FEVNSEVDAQ KIKEEAAAEY RKELRLFIVS AILTAPFLVE MAMMLTGAAH
EMIPRWVQWI LATPVQFWVG WRFYRGSYYA LKSGSANMDV LVALGTTMAY GLSAVMTVMD
WHHHHVYFEA STAVITLILL GKLMESRAKG KTSEAVEGLL RLQPKQAMVE RNGEVVALDI
TELVAGDIVI VKNGESIPVD GLVVQGVSSV DESMLTGESM PVQKGIDDRV YAATLNQEGS
LRIKATGVGS KTQLAQIIKI VTTAQGSKAP IQRLADKISA VFVPVVVGIS VLTFIGTWLW
TGDLTMALIS SVSVLVIACP CALGLATPTA VVVGIGKGAQ AGVLFRDAKA LELAEKIDIL
VLDKTGTITE GKPVVTEIHV TAGQDRNQVL SFAASLEAGS SHPLAHAILE EARKEGLSLH
TVQNFKSVMG QGVEGQIGNQ SLKLGRSAWV APEFSLNQDL LKELESKGQT LMVLADEARV
LGYIAVADRI RESSKEAIAE IQKRGVKVMM LTGDNEGTAR EISRQAGITD FKHSVKPADK
ANVIVTLKRK KLRVAMVGDG INDAPALAMA DVSFSMSSGT DIAIETADVT LMKNDLRSVA
QAIQLSHLTL KKIRQNLFFA FIYNVLGIPL AALGMLNPVI AGAAMAMSSV SVVSNSLLLK
RKKI
//
