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Database: UniProt
Entry: A0A0P7XIQ0_9BACT
LinkDB: A0A0P7XIQ0_9BACT
Original site: A0A0P7XIQ0_9BACT 
ID   A0A0P7XIQ0_9BACT        Unreviewed;       782 AA.
AC   A0A0P7XIQ0;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Au2+ exporting ATPase GolT {ECO:0000313|EMBL:KPQ00995.1};
DE            EC=3.6.3.- {ECO:0000313|EMBL:KPQ00995.1};
GN   Name=golT {ECO:0000313|EMBL:KPQ00995.1};
GN   ORFNames=HLUCCA01_03640 {ECO:0000313|EMBL:KPQ00995.1};
OS   Bacteroidetes bacterium HLUCCA01.
OC   Bacteria; Bacteroidota.
OX   NCBI_TaxID=1666909 {ECO:0000313|EMBL:KPQ00995.1, ECO:0000313|Proteomes:UP000050310};
RN   [1] {ECO:0000313|EMBL:KPQ00995.1, ECO:0000313|Proteomes:UP000050310}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HLUCCA01 {ECO:0000313|EMBL:KPQ00995.1};
RA   Nelson W.C., Romine M.F., Lindemann S.R.;
RT   "Identification and resolution of microdiversity through metagenomic
RT   sequencing of parallel consortia.";
RL   Submitted (AUG-2015) 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:KPQ00995.1}.
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DR   EMBL; LIHN01000001; KPQ00995.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0P7XIQ0; -.
DR   SMR; A0A0P7XIQ0; -.
DR   STRING; 1666909.HLUCCA01_03640; -.
DR   PATRIC; fig|1666909.3.peg.1388; -.
DR   Proteomes; UP000050310; 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; cd00371; HMA; 1.
DR   CDD; cd02094; P-type_ATPase_Cu-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   InterPro; IPR044492; P_typ_ATPase_HD_dom.
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   PRINTS; PR00120; HATPASE.
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   SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 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   Hydrolase {ECO:0000313|EMBL:KPQ00995.1};
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   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        123..143
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        163..182
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        194..213
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        225..243
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        377..399
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        405..425
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        737..756
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        762..779
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   DOMAIN          9..73
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
FT   REGION          74..97
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   782 AA;  82097 MW;  E3C9B5FFCE030C27 CRC64;
     MSNPTTQSNE IQLSVRGMTC ASCVAHVEKA MQGVDGVRQA EVNLATEEAR VQVEGASAAA
     LIRAIEKAGY EATELAGDED ETDGEDPAAL SDTGADPMKA HADTMQKLGW GDALSNASFR
     TKFLVALPLA ALVMVLEMGP MITGGAWMEW TQQNLFTVNM VKLGLTAVVL FYAGSSFFTR
     ALGAARHGRA DMNTLVAVGT GSAFLFSTWA ALFGSDEGLV SPADVYFDTA AVIVALILLG
     RWMEERAKDQ TRDTLRGLLE LAPKTAHLRD GDDVRTIPLK EVKKGDLLVV KAYESVPVDG
     VITEGTTSVD EAMMTGEPVP VDKSAGDAVT GGTRNTSQTF TMKATKVGKE TALAAIIEAV
     KKAQGSKAPI QRLVDRVAGV FVPVVILVAL ITAGLWFVYG TPEQALVNMV AVLVIACPCA
     LGLATPTGIM VGSGRAAEKG ILIKDAVTLE QARSVKTILF DKTGTLTTGA MRLAEVILAG
     DGVSGPSPAA GDGEKANQAP PKAVTREDVL RLAASVEQGS DHPIAKSILK AARDEGVTPE
     YGMSIGTRAG VGISGLVGSQ TVEIGSVRLL SEEQTETWSE QIAAQQQEGR TVLVMLCDRK
     LTALLALEDE LREESAAVVK ALQQEGIRVV MLTGDQQRTA LAVARKLGIT DVEAGVSPTG
     KSDIVAKYQQ YGDVAMVGDG INDAAALTRA DLGIAMSGGS DLAVSSSDIT IVGDDLHNVA
     ESIRLSKNVL RVIRQNLFWA FLYNTLGIPL AALGFLNPMV AGAAMALSSV SVVTNSLRIK
     RF
//
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