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Database: UniProt
Entry: F8N7B7_9BACT
LinkDB: F8N7B7_9BACT
Original site: F8N7B7_9BACT 
ID   F8N7B7_9BACT            Unreviewed;       651 AA.
AC   F8N7B7;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   SubName: Full=Heavy metal translocating P-type ATPase {ECO:0000313|EMBL:EGN56344.1};
DE            EC=3.6.3.5 {ECO:0000313|EMBL:EGN56344.1};
GN   ORFNames=Premu_0887 {ECO:0000313|EMBL:EGN56344.1};
OS   Hallella multisaccharivorax DSM 17128.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Hallella.
OX   NCBI_TaxID=688246 {ECO:0000313|EMBL:EGN56344.1, ECO:0000313|Proteomes:UP000002772};
RN   [1] {ECO:0000313|Proteomes:UP000002772}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17128 {ECO:0000313|Proteomes:UP000002772};
RX   PubMed=22180809; DOI=10.4056/sigs.2164949;
RA   Pati A., Gronow S., Lu M., Lapidus A., Nolan M., Lucas S., Hammon N.,
RA   Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S.,
RA   Liolios K., Pagani I., Mavromatis K., Mikhailova N., Huntemann M., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Detter J.C., Brambilla E.M., Rohde M.,
RA   Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Ivanova N.;
RT   "Non-contiguous finished genome sequence of the opportunistic oral pathogen
RT   Prevotella multisaccharivorax type strain (PPPA20).";
RL   Stand. Genomic Sci. 5:41-49(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; GL945017; EGN56344.1; -; Genomic_DNA.
DR   RefSeq; WP_007573417.1; NZ_GL945017.1.
DR   AlphaFoldDB; F8N7B7; -.
DR   STRING; 688246.Premu_0887; -.
DR   eggNOG; COG2217; Bacteria.
DR   HOGENOM; CLU_001771_6_2_10; -.
DR   OrthoDB; 1521937at2; -.
DR   Proteomes; UP000002772; 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   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; 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; 2.
DR   PANTHER; PTHR48085; CADMIUM/ZINC-TRANSPORTING ATPASE HMA2-RELATED; 1.
DR   PANTHER; PTHR48085:SF5; CADMIUM_ZINC-TRANSPORTING ATPASE HMA2; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
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:EGN56344.1};
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   Reference proteome {ECO:0000313|Proteomes:UP000002772};
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        5..22
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        28..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        242..262
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        274..297
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        603..623
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        629..646
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
SQ   SEQUENCE   651 AA;  69889 MW;  2AB3CCCEE8778D25 CRC64;
     MDKRLLTRII VAAVLLFVAW MMTKTFMMPV WAQLLVYLIP YLLISYDVMG EAVEEGIKER
     NPFNEDFLMC VATVGALLIG FLPSAEPQFP EAVFVMLFFQ VGELFEDYAE DKSKHSIKAL
     MDIRPDTANV EREGMVSIVD PKDVKVGETV VVRPGEKVPM DGKIIEGSSS LNTVALTGES
     VPRSVSVGDD ALSGCVNVSG LLKIRVTKSF GDSTASKIIR LVEESSENKS KSETFIRRFS
     RVYTPIVVFL ALAVAFLPPF FYDSYVQGLV TWGYRALSFL VVSCPCALVI SVPLSFFGGI
     GGASRQGILI KGGNYMDALA KLSTVVFDKT GTLTKGVFAV TAIHPETLDA HDLLHLAAHA
     ESYSTHPIAS ALRAAFDGAT FKDLTLNNDG TPRGGDLLAD GCRLEDVQEI AGQGIRASVN
     GHAVSVGNDR LMEAVGAKVA ECRKCKDIVG TTIHVAVDGV YAGHIIIADR VKDDSREAIA
     GLKRLGVRRT VMLTGDHEAV ARSVAGHLKL DEYHAELMPQ DKVTEVERLL NERTEGTTLA
     FVGDGINDAP VLARADVGIA MGALGSDAAI EAADVVLMDD KPSKIATAIR IARRTIANAR
     QNSTFAIAVK VLILVLVATG LLGSLAMPVA VFGDVGVMVL CVLNAMRMLR A
//
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