ID E0RTQ7_SPITD Unreviewed; 762 AA.
AC E0RTQ7;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=Heavy metal translocating P-type ATPase {ECO:0008006|Google:ProtNLM};
GN OrderedLocusNames=STHERM_c14920 {ECO:0000313|EMBL:ADN02432.1};
OS Spirochaeta thermophila (strain ATCC 49972 / DSM 6192 / RI 19.B1).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Spirochaetaceae;
OC Spirochaeta.
OX NCBI_TaxID=665571 {ECO:0000313|EMBL:ADN02432.1, ECO:0000313|Proteomes:UP000001296};
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 6192;
RA Angelov A., Mientus M., Wittenberg S., Lehmann R., Liesegang H., Daniel R.,
RA Liebl W.;
RT "The genome sequence of Spirochaeta thermophila DSM6192.";
RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADN02432.1, ECO:0000313|Proteomes:UP000001296}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49972 / DSM 6192 / RI 19.B1
RC {ECO:0000313|Proteomes:UP000001296};
RX PubMed=20935097; DOI=10.1128/JB.01023-10;
RA Angelov A., Liebl S., Ballschmiter M., Bomeke M., Lehmann R., Liesegang H.,
RA Daniel R., Liebl W.;
RT "Genome sequence of the polysaccharide-degrading, thermophilic anaerobe
RT Spirochaeta thermophila DSM 6192.";
RL J. Bacteriol. 192:6492-6493(2010).
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; CP001698; ADN02432.1; -; Genomic_DNA.
DR AlphaFoldDB; E0RTQ7; -.
DR PaxDb; 665571-STHERM_c14920; -.
DR KEGG; sta:STHERM_c14920; -.
DR eggNOG; COG2217; Bacteria.
DR HOGENOM; CLU_001771_11_2_12; -.
DR Proteomes; UP000001296; 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 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 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; 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; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00120; HATPASE.
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 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 132..149
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 164..183
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 195..216
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 222..240
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 374..396
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 408..435
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 709..728
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 734..758
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT REGION 14..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..121
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 762 AA; 81790 MW; 32825441C89D2BA7 CRC64;
MTRYRCPTCG MTFEQEGVCP MDGTPLVPAP EESPHSRGGM GSLHEDAPAS HRHDHGSAPT
HSPHGNHPPH HEGHEDHEHH GGVTGETGHA HHEHHTGHSG EAGHAHHGHE HHGGHDHAEH
HKAMIRDFRR RFFVSLLLTL PILALSPLIQ EVFGFSFDLP VQEYLLWALS SLVFFYGGWP
FLVGGRDEIQ RRQPGMMTLI ALAISVAYVY STAVVFGLSG KFFFWELATL IDVMLLGHWI
EMASVLGASR ALEKLAQLLP DTAHKVEGEE VVDVRTSELA AGDLVLVKAG EKIPADGEVV
KGTSYVNESM LTGESVPVKK GPGDGVIGGS VNGDGVLTVR ITGTGEDSYL QKVIHLVEEA
QRTKSKTQRL ADRAAQWLTF IAIGAGSLTF VLWMVFTGDL AAAIERMVTV MVITCPHALG
LAVPLVVAVS TSLSARNGLL IRNRTAFENA RKISTVVFDK TGTLTEGRFG VAGAAAFVGS
EEELLTLAAS LERNSEHPVA RGIVEEAEKR GLAPLPVEDF SVRKGEGVEG VVNGRRIALL
SRRALEEGGY TVPETEGSHI GTLVYVVEEG KVRGAVVLAD RIRPESREAV RTLQKKGIRC
WMLTGDNRKV AEAVAKELGL DGVFAEVLPH EKQEKVKELQ AKGEFVAMTG DGINDAPALA
QADVGIAIGS GTDIAAETAD IILVHDSPAD VAALIEFGRA TYRKMVQNLL WATGYNVVAI
PLAAGVLYPL TGLLLSPAVG AALMSLSTVI VAVNASFLRV RR
//
