ID A0A0W0X2V3_9GAMM Unreviewed; 731 AA.
AC A0A0W0X2V3;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Copper transporting P-type ATPase {ECO:0000313|EMBL:KTD38926.1};
DE EC=3.6.3.4 {ECO:0000313|EMBL:KTD38926.1};
GN Name=copA_1 {ECO:0000313|EMBL:KTD38926.1};
GN ORFNames=Lnau_0420 {ECO:0000313|EMBL:KTD38926.1};
OS Legionella nautarum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=45070 {ECO:0000313|EMBL:KTD38926.1, ECO:0000313|Proteomes:UP000054725};
RN [1] {ECO:0000313|EMBL:KTD38926.1, ECO:0000313|Proteomes:UP000054725}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49506 {ECO:0000313|EMBL:KTD38926.1,
RC ECO:0000313|Proteomes:UP000054725};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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:KTD38926.1}.
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DR EMBL; LNYO01000004; KTD38926.1; -; Genomic_DNA.
DR RefSeq; WP_058503498.1; NZ_LNYO01000004.1.
DR AlphaFoldDB; A0A0W0X2V3; -.
DR STRING; 45070.Lnau_0420; -.
DR PATRIC; fig|45070.6.peg.443; -.
DR OrthoDB; 9814270at2; -.
DR Proteomes; UP000054725; 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 GO; GO:0015662; F:P-type ion transporter activity; IEA:UniProt.
DR CDD; cd02094; P-type_ATPase_Cu-like; 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; IPR045800; HMBD.
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; TIGR01512; ATPase-IB2_Cd; 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; PF19335; HMBD; 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 PROSITE; PS00154; ATPASE_E1_E2; 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:KTD38926.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362081};
KW Metal-binding {ECO:0000256|RuleBase:RU362081};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362081};
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 79..103
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 109..128
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 180..198
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 333..355
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 361..384
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 677..696
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 702..724
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 33..60
FT /note="Heavy metal binding"
FT /evidence="ECO:0000259|Pfam:PF19335"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 731 AA; 78994 MW; AB0D1267BEA0CEBF CRC64;
MEHNQNKHQA ENHSCCHSKS KSQTAAPING PVVYTCPMHP EIRQEKPGTC PLCGMGLEPE
AISAEETSNP EYLDMRRRFW IALILSLPVF ILAMGEHVFA QWLPIPLSIW IQLILATPVV
LWCGWPFFQR GWQSLKSRHL NMFTLIAMGT VVAWGYSVVA TLFPNLFPLS FRNRDGMVDV
YFEAAAVITT LVLLGQMLEL KAREKTGGAI RALLKLAPET AHRLQDNDQE TEIGLEQVLA
GDRLRVRPGE KIPVDGELTE GQSNVDESMV TGEPLAVTKK VGDKLIGATI NLTGSFVMKA
EHVGSDTMLS RIVQMVSDAQ RSRAPIQRLA DAVSGWFVPI VILVALLAFF LWLIFGPPPS
VSYGLIAAVS VLIIACPCAL GLATPMSIMV GIGKGAGNGV LIKNAESLEQ LEKVDTLVVD
KTGTLTEGHP KLTRLIPLQE FTEEEILTLA ASLENHSEHP LAHAIVSAAL EKNLALAAVK
DFEALTGKGV RGTINNRLIA IGTAALMQEL ESDVKIISTQ ADELRSEGAS VMFMAIDRQI
AAILAIEDPI KSTTREAIRT LQSKGIKIVM LTGDNKKTAE AVASKLGIKT VIAEVLPTDK
SRIVAELQQK NCIVAMAGDG VNDAPALAKA DIGIAMGTGT DVAIESAGIT LLHGDLHGIV
KARHLSEVTM KNIRQNLFFA FIYNLIGVPI AAGILYPFTG LLLNPMISAA AMSLSSVSVI
LNALRLRWTN L
//
