ID   Q8F8G3_LEPIN            Unreviewed;       739 AA.
AC   Q8F8G3;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 157.
DE   SubName: Full=Cation transport ATPase {ECO:0000313|EMBL:AAN47793.1};
GN   Name=zntA {ECO:0000313|EMBL:AAN47793.1};
GN   OrderedLocusNames=LA_0594 {ECO:0000313|EMBL:AAN47793.1};
OS   Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain
OS   56601).
OC   Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC   Leptospira.
OX   NCBI_TaxID=189518 {ECO:0000313|EMBL:AAN47793.1, ECO:0000313|Proteomes:UP000001408};
RN   [1] {ECO:0000313|EMBL:AAN47793.1, ECO:0000313|Proteomes:UP000001408}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=56601 {ECO:0000313|EMBL:AAN47793.1,
RC   ECO:0000313|Proteomes:UP000001408};
RX   PubMed=12712204; DOI=10.1038/nature01597;
RA   Ren S.X., Fu G., Jiang X.G., Zeng R., Miao Y.G., Xu H., Zhang Y.X.,
RA   Xiong H., Lu G., Lu L.F., Jiang H.Q., Jia J., Tu Y.F., Jiang J.X., Gu W.Y.,
RA   Zhang Y.Q., Cai Z., Sheng H.H., Yin H.F., Zhang Y., Zhu G.F., Wan M.,
RA   Huang H.L., Qian Z., Wang S.Y., Ma W., Yao Z.J., Shen Y., Qiang B.Q.,
RA   Xia Q.C., Guo X.K., Danchin A., Saint Girons I., Somerville R.L., Wen Y.M.,
RA   Shi M.H., Chen Z., Xu J.G., Zhao G.P.;
RT   "Unique physiological and pathogenic features of Leptospira interrogans
RT   revealed by whole-genome sequencing.";
RL   Nature 422:888-893(2003).
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; AE010300; AAN47793.1; -; Genomic_DNA.
DR   RefSeq; NP_710775.1; NC_004342.2.
DR   RefSeq; WP_000868075.1; NC_004342.2.
DR   AlphaFoldDB; Q8F8G3; -.
DR   STRING; 189518.LA_0594; -.
DR   PaxDb; 189518-LA_0594; -.
DR   EnsemblBacteria; AAN47793; AAN47793; LA_0594.
DR   KEGG; lil:LA_0594; -.
DR   PATRIC; fig|189518.3.peg.597; -.
DR   HOGENOM; CLU_001771_0_3_12; -.
DR   InParanoid; Q8F8G3; -.
DR   OrthoDB; 9760364at2; -.
DR   Proteomes; UP000001408; Chromosome I.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
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:0005507; F:copper ion binding; IBA:GO_Central.
DR   GO; GO:0043682; F:P-type divalent copper transporter activity; IBA:GO_Central.
DR   GO; GO:0055070; P:copper ion homeostasis; IBA:GO_Central.
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; 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:UP000001408};
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        132..150
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        162..185
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        197..215
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        352..372
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        384..405
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        693..710
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   DOMAIN          10..75
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
SQ   SEQUENCE   739 AA;  80585 MW;  51BCBF37510F9D64 CRC64;
     MKVQQELHLN EVTLDVIGMT CANCALRIEK GLKKIPGVKD VRVNFAMETA KIDFESSISK
     EILMDKIDFL GYRAVVHEDI EIDGEIQKKE FKKLKVRVIV SAFLSLPLLL SMIGHFENNL
     NFEYLSFLMN PWLQFVLATP IQFWIGASFY KGSFRALRNG GANMDVLVVL GTSAAYFYSV
     YLTFIFNEKY IHKTANLYYE TSSVLITLIL FGKLLEHIVK GKSSKAIQSL VNLQPKKANV
     IREKEIQEIP LLAVRSGDLI LVKPGESIPV DGIIEEGSST IDESMLTGES IPVEKTISNF
     VYGGSLNQNG TFKFRALKVG KETLLSGIIR AVREAQGTKA PIQRIADQIS EIFVPVIVLI
     SVITLCVWYF WILPSTFSVA LEKAIAVLVV ACPCALGLAT PISVLTGSGK AATMGILFRS
     AEALEILHKV NAIVFDKTGT LTYGKPVLKS LESLNIAKEN NLLTLAASAE QNSEHPLSKA
     IVESAKKKGL VLAIPENFET IPGGGISAIV EGNRILIGTE RLFYAKGIEL NQELNNLKRI
     REEEGNTVVH LSVNEIHSAI LTLADTLKES TPATIAKLKS LGIEVYMITG DNERTARVIS
     KDCGIERVLA EVLPEKKAME VKNLKSLGKV VSMVGDGIND APALAISDLG IAMGTGTDVA
     MESSDLVIVN GDLNSIVNAI TISRKTVYNI RQNFFWALLY NTLGIPIAAA GFLAPWVAGG
     AMALSSVSVV LNALRLQRD
//