ID   A0A1G6Y2E8_PEPNI        Unreviewed;       700 AA.
AC   A0A1G6Y2E8;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=ATPase, P-type (Transporting), HAD superfamily, subfamily IC/heavy metal translocating P-type ATPase {ECO:0000313|EMBL:SDD84568.1};
GN   ORFNames=SAMN04489866_10861 {ECO:0000313|EMBL:SDD84568.1};
OS   Peptococcus niger.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC   Peptococcus.
OX   NCBI_TaxID=2741 {ECO:0000313|EMBL:SDD84568.1, ECO:0000313|Proteomes:UP000198995};
RN   [1] {ECO:0000313|EMBL:SDD84568.1, ECO:0000313|Proteomes:UP000198995}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20475 {ECO:0000313|EMBL:SDD84568.1,
RC   ECO:0000313|Proteomes:UP000198995};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FNAF01000008; SDD84568.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G6Y2E8; -.
DR   STRING; 2741.SAMN04489866_10861; -.
DR   OrthoDB; 9760364at2; -.
DR   Proteomes; UP000198995; 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   CDD; cd07550; P-type_ATPase_HM; 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; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR027256; P-typ_ATPase_IB.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR   NCBIfam; TIGR01525; ATPase-IB_hvy; 1.
DR   NCBIfam; TIGR01494; ATPase_P-type; 1.
DR   PANTHER; PTHR48085; CADMIUM/ZINC-TRANSPORTING ATPASE HMA2-RELATED; 1.
DR   PANTHER; PTHR48085:SF1; CATION TRANSPORTING ATPASE (E1-E2 FAMILY); 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00120; HATPASE.
DR   SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR   SFLD; SFLDF00027; p-type_atpase; 1.
DR   SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
DR   PROSITE; PS01229; COF_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};
KW   Metal-binding {ECO:0000256|RuleBase:RU362081};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU362081};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198995};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
SQ   SEQUENCE   700 AA;  76919 MW;  E12104A823E4F625 CRC64;
     MTYQVVSALP GYLRLRAPRF AISEDDSYIL SHVIGQMPTV FSVDVNYMTG SILVRHMGDN
     EKLTADIEAI DVASYPPVPL HEQDQHVKIS LTFKGMLAKT FMGRLLKGFM PMPVYKVMTV
     YSALRYVWRG LKSVSQGRFD VDVLDGAAIG LSVAFGHYHS ASSIMFLLSI SDILEEYARQ
     RTRNALTTAL IMNVDTVWVR LEEGLEVQKS LSDVQVGEEI IVRSGTMIPL DGEVIAGEAG
     VNQQTLTGES APVIKEVGDS VYAGTAIAEG ELVIRVRKLL EESRIQYILN MVERAEDEKI
     GTAAKAEALA DRIVPYSFLF AGIVWLLTRD GHKALSALTV DYSCAIKLAT PLAIISAMRE
     ATQNRIMVKG GKYLEALAEA DTVVFDKTGT LTCATPRVKK VIPLMDDMNR DEVLRLAACL
     EEHFPHSLAR AIVRQAEEEG LQHREEHADV SYVVAHGITS EWRGQTVHIG SRHFLEEDKG
     IVFSEAAETL LREEGSGYSC VYLAIGDQLA GFICIQDPPR EEAKEVIALL RKTGIQNVVM
     LTGDGPQIAE RIAEELGIDR YFAEVLPEDK AAKIRTLQDE GKKVIMVGDG VNDTPALAQA
     DVSVSLRDAS DVAREVADVT LLQSDLLALV TARKISIRLM RRVDSNFNRI FTFNTGLLIL
     GATGLLQPTT TALWHNVSTA ALGYLACQPL LSPKERTLAE
//