ID A0A1M3LXP3_9PROT Unreviewed; 767 AA.
AC A0A1M3LXP3;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=ATPase P {ECO:0000313|EMBL:OJX77486.1};
GN ORFNames=BGO92_10620 {ECO:0000313|EMBL:OJX77486.1};
OS Magnetospirillum sp. 64-120.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Magnetospirillum.
OX NCBI_TaxID=1895778 {ECO:0000313|EMBL:OJX77486.1, ECO:0000313|Proteomes:UP000184435};
RN [1] {ECO:0000313|EMBL:OJX77486.1, ECO:0000313|Proteomes:UP000184435}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=64-120 {ECO:0000313|EMBL:OJX77486.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OJX77486.1}.
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DR EMBL; MKVK01000022; OJX77486.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M3LXP3; -.
DR STRING; 1895778.BGO92_10620; -.
DR Proteomes; UP000184435; 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 GO; GO:0015662; F:P-type ion transporter activity; IEA:UniProt.
DR CDD; cd00371; HMA; 1.
DR CDD; cd02092; P-type_ATPase_FixI-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 NCBIfam; TIGR01511; ATPase-IB1_Cu; 1.
DR NCBIfam; TIGR01512; ATPase-IB2_Cd; 1.
DR NCBIfam; TIGR01525; ATPase-IB_hvy; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR43520; ATP7, ISOFORM B; 1.
DR PANTHER; PTHR43520:SF5; CATION-TRANSPORTING P-TYPE ATPASE-RELATED; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00403; HMA; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
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; PS01229; COF_2; 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 Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362081};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362081}.
FT TRANSMEM 150..174
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 186..203
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 223..241
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 247..265
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 403..425
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 431..457
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 719..735
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 741..759
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 66..132
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 767 AA; 82345 MW; 2720AB903B945F1B CRC64;
MPVGLDGDFC CRGCEGAFAL LEDMGLGRYY QRRCVDPAVR PLRPEEGAGA HHDYAAHIID
EDDGLASLNL MVEGIHCAAC IWLIEALLSR QPAVVWARVN MTTRRLVLRW KKDQADPAGI
LAPVLAVGYR LVPYDPTKLG RETERHEKQL LRAMAVAGFA AGNVMLLSVS VWAGHFSGMG
FYTRELMHWI SALIVLPAVL YCIRPFLYSA LTALSNRRTN MDVPITLGVL LASGMSLAET
IRGGEHAYFD SAITLLFFLL IGRYLDSRAR GKARSAAEHL LTLDAVAVTV LEDDGTQRLI
PPTQVKVGQT VLVAAGERIG IDGVIRSGVS DVDTSLITGE TVPMAVNPGA QVFAGTINLS
APLRLTVSAV GERTLLAEIV RMMEVAEQGR ARYVALADRV SRWYAPVVHV AALSTFLGWV
LLGGIPWQVA LLHAVAVLII TCPCALALAV PVVQVIASGR LLRQGILLKS ATALERVADI
DVVVFDKTGT LTVGKPELLE DGTWGEEDLL QAVRLAAASH HPLARALAAA RPGIAADPQA
IEEPGRGMVA GDWRLGSRTH VGVTREDGAE GPELWLAGPD RPPVRFAFAD RPRSDAAEVV
ARLRRWGLAV ELLSGDRVAT VRRLAGDLDI AQWRAGCTPA QKVARLEELK AQGKRVMMVG
DGLNDAPALS AAHVSMSPST AVDVSQTAAD VVFQGERLSP VMEVLEVARR SRTLVQQNFV
LALGYNFFTV PLAVAGHVTP LIAAIAMSTS SLVVIGNALR LTRGRKA
//
