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
//
