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Database: UniProt
Entry: G0ENZ2_BRAIP
LinkDB: G0ENZ2_BRAIP
Original site: G0ENZ2_BRAIP 
ID   G0ENZ2_BRAIP            Unreviewed;       758 AA.
AC   G0ENZ2;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 67.
DE   SubName: Full=ZntA, Cation transport ATPase {ECO:0000313|EMBL:AEM20666.1};
GN   Name=zntA {ECO:0000313|EMBL:AEM20666.1};
GN   OrderedLocusNames=Bint_0030 {ECO:0000313|EMBL:AEM20666.1};
OS   Brachyspira intermedia (strain ATCC 51140 / PWS/A) (Serpulina intermedia).
OC   Bacteria; Spirochaetota; Spirochaetia; Brachyspirales; Brachyspiraceae;
OC   Brachyspira.
OX   NCBI_TaxID=1045858 {ECO:0000313|EMBL:AEM20666.1, ECO:0000313|Proteomes:UP000008522};
RN   [1] {ECO:0000313|EMBL:AEM20666.1, ECO:0000313|Proteomes:UP000008522}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51140 / PWS/A {ECO:0000313|Proteomes:UP000008522};
RX   PubMed=21816042; DOI=10.1186/1471-2164-12-395;
RA   Hafstrom T., Jansson D.S., Segerman B.;
RT   "Complete genome sequence of Brachyspira intermedia reveals unique genomic
RT   features in Brachyspira species and phage-mediated horizontal gene
RT   transfer.";
RL   BMC Genomics 12:395-395(2011).
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; CP002874; AEM20666.1; -; Genomic_DNA.
DR   RefSeq; WP_014486519.1; NC_017243.1.
DR   AlphaFoldDB; G0ENZ2; -.
DR   KEGG; bip:Bint_0030; -.
DR   PATRIC; fig|1045858.4.peg.30; -.
DR   eggNOG; COG2217; Bacteria.
DR   HOGENOM; CLU_001771_0_3_12; -.
DR   OMA; HWMLPAW; -.
DR   OrthoDB; 9760364at2; -.
DR   Proteomes; UP000008522; 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; 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   PRINTS; PR00942; CUATPASEI.
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; 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|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        88..110
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        122..143
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        163..186
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        192..211
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        348..367
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        373..394
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        684..706
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        726..749
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   DOMAIN          1..67
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
SQ   SEQUENCE   758 AA;  81799 MW;  9EA9765FB9814B9A CRC64;
     MKMTLKIGGM HCAACSRAVE RALKKTEGIE DANVNIATEK AVFNYDEKKL KYDDIVNVVV
     KAGYQVLAKE EDPAIVKARE IKEQKIRLIV SAIFSIPLFY ISMAPMVSFV KFPIPSFLVH
     HINPQVFSIV AIFLCVPVMI SGYKFYTLGF PALFRGSPNM DSLVAIGTTA AFSYSIYSTV
     LAFMGLNPHG ENLYYESAAV IITLVQFGKY LEARSKGKTG EAIKKLMGLQ PKTATIIKDG
     EEKEIKIADV KVDDIVLVRP GEKIPVDGEI IEGYSSVDES MLTGESIPVE KSVGDKVVGA
     SINKTGSFKF KAQKVGADTA LAQIIKLVED AQGSKAPIAH IADVVSSYFV PAVITIALIS
     GIIWFIALHN FVFSLTVFVS VLVIACPCAL GLATPTAIMV GTGKGAELGI LFKNAEALEV
     SEKINAVMFD KTGTLTEGKP YVTDIISDDK DKLLLIAASA ENGSEHPLGE AIVREAKEKN
     IKLLNIENFK AIAGFGIEVF IDNKKVLMGN DKLMNKENIN TENYNSYMDK LSKEGKTPMY
     VAYDNKLLGI IAVADKLKKE SIEAINRLHK LGIKTAMITG DNKNTANSVA KEAGIDIVFA
     EVLPEEKSNE VKKLQDQGLT VAMVGDGIND APALTQANVG IAIGSGTDVA IESADIVLVK
     SNTNDVVTAI ELSKATMRDI KQNLFWAFCY NVIGIPIAAG VLHVFREPLI ASSIGGFLTA
     IMGKDLLLNP IFAALAMSLS SVSVVTNALR LNFFKPSK
//
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