ID A0A2T6FB38_9BURK Unreviewed; 806 AA.
AC A0A2T6FB38;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Heavy metal translocating P-type ATPase {ECO:0000313|EMBL:PUA20239.1};
GN ORFNames=C7W93_10805 {ECO:0000313|EMBL:PUA20239.1};
OS Glaciimonas sp. PCH181.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Glaciimonas.
OX NCBI_TaxID=2133943 {ECO:0000313|EMBL:PUA20239.1, ECO:0000313|Proteomes:UP000244112};
RN [1] {ECO:0000313|EMBL:PUA20239.1, ECO:0000313|Proteomes:UP000244112}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCH181 {ECO:0000313|EMBL:PUA20239.1,
RC ECO:0000313|Proteomes:UP000244112};
RA Kumar V., Thakur V., Kumar S., Singh D.;
RT "Genome analysis of a novel bacterium Glaciimonas sp. PCH181 isolated from
RT glacier stream of Indian trans-Himalaya.";
RL Submitted (MAR-2018) 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:PUA20239.1}.
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; PYFP01000001; PUA20239.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T6FB38; -.
DR OrthoDB; 8552908at2; -.
DR Proteomes; UP000244112; 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 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; 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; 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 PRINTS; PR00941; CDATPASE.
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.
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 Reference proteome {ECO:0000313|Proteomes:UP000244112};
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 183..202
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 208..227
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 239..255
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 261..279
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 412..437
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 443..470
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 754..774
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 780..802
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 56..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 806 AA; 86119 MW; 5B022C3E3A28F9BD CRC64;
MGSCQHDHKH DQTHAKAHRP THDHPHDHAT EHAPEPAHKH DHAHPQQVHA HECCHAHDHD
HDHGHHPESD SASTAAVAAP FPPVAVADGS AEAVFLIQKM DCPTEEKLIR DRFKNMAGIV
GMQFNLIQRE LTVQHHLNSV ETIISSLKAL DLDPALKSDS LTGVVGLSAE NGDGAFKIAR
SKWLLIGLSG LAAIASEIVA WTSGNETSWL VIGLALLAIA TGGLDTLKKG WIALRNFSLN
MNFLMSLAVI GAAIIGQWPE AAVVIFLFAL AEMIEALSLD RARNAIKGLM AMAPDQATVQ
KATGEWREIP TAQVVLAALV RVKPGERVPL DGVVVTGQTT INQAPITGES MPVVKQPGDQ
VFAGTINERS AFDYKVTALQ ANSTLSRIIK SVQQAQGQRA PTQRFVDEFA RYYIPAVVLM
AALVAVLPPL IMGTAFYPWL YKALVLLVIA CPCALVISTP VTVVSGLAAA AKHGLLIKGG
VYLEMGRKIK ALALDKTGTL TIGKPVVTDM QLVEPEEAAG NLLPYQRYAA SLAHRSDHPV
STAVAADWQA TKQLGDLRDI SDFEALTGLG VKGRIDGVLF YLGNHRMVHD MGICSESLEA
RLDALEIQGK TTIVLCSATA PLLILAVADT VRDTSVEAIA QLQAMGIAAV ILSGDNPHTA
QAIADKVGVT DARGNLLPED KLTAVDDLIR RYGYVGMVGD GINDAPALAK ANIGFAMGAA
GTDTALETAD VALMDDDLRK IPDFIRLSKK THNVLMQNIT LALGIKAVFL VLALTGEATL
WMAVFADMGA SLLVVFNGLR LLRALR
//
