ID A0A1G1ZP76_9BACT Unreviewed; 694 AA.
AC A0A1G1ZP76;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 13-SEP-2023, entry version 28.
DE RecName: Full=HMA domain-containing protein {ECO:0000259|PROSITE:PS50846};
DE Flags: Fragment;
GN ORFNames=A3A16_03310 {ECO:0000313|EMBL:OGY66372.1};
OS Candidatus Harrisonbacteria bacterium RIFCSPLOWO2_01_FULL_44_18.
OC Bacteria; Candidatus Harrisonbacteria.
OX NCBI_TaxID=1798407 {ECO:0000313|EMBL:OGY66372.1, ECO:0000313|Proteomes:UP000177942};
RN [1] {ECO:0000313|EMBL:OGY66372.1, ECO:0000313|Proteomes:UP000177942}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGY66372.1}.
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; MHJJ01000001; OGY66372.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G1ZP76; -.
DR STRING; 1798407.A3A16_03310; -.
DR Proteomes; UP000177942; 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; 2.
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; IPR017969; Heavy-metal-associated_CS.
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; TIGR01525; ATPase-IB_hvy; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
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; PF00403; HMA; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00942; CUATPASEI.
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; PS01047; HMA_1; 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|ARBA:ARBA00022723,
KW 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 111..130
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 145..163
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 183..205
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 211..231
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 393..412
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 418..441
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 2..67
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT REGION 261..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..283
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 694
FT /evidence="ECO:0000313|EMBL:OGY66372.1"
SQ SEQUENCE 694 AA; 74697 MW; 0A52A00846E3CE0A CRC64;
MKKEQFLIQG MHCVSCVLTI EHALKKVPGV KSASVNFATE KAMVEYEDSV TPEILREAVA
QTGYKLILSQ DGISVEGVHG AHKTAESASA QAPADTHDHH RMLKEAEIKL LWKKFIVGAI
LSSIVILLSL PDYLPFAKDM MATSWRYLLL LIFTAPVEFW IGYQFWRGAW YGLKNFTANM
DTLVALGTGA AFIFSVAVTF LYWLTPAPYT LEVYFDVAAV VTTLVILGKY LEAKAKGAAS
EAIKKLLKLQ AKTAHVLREG NGSTRLTTGG STRLTTGGST GSPQVHEMEV PIEQVQTGDI
ILVKPGEKVP VDGIIIDGAS TIDESMVTGE SMPVDKKVGD GVIGATINKT GAFKFRATKV
GKETFLAQVV KLVEEAQASK APIQKLADAI TSYFVPVVLL VAILSFGIWF IFGPEPALTF
AMVNAVAVLV IACPCALGLA TPTAIMVGTG KAAERGIIIR DAEALEFAGK INALVLDKTG
TLTKGEPAVT DVMVTSDKRQ ATSNEIIQIA ASLEKLSEHP IAKAVVAYAA SLGKQSSHPL
DTAVRKQAEE LKMPLYEVKN FLAHPGKGIE GLVEGTRMFL GNRSLIEDVG ISLASEIEDR
AVTLESEGKT LLFLARTYLK DTSAQKELLG IIAVADTLKE SAAKSVELLK KIGLEVWMIT
GDNERTAQAI GKKLGIDKVM AKVLPDQKSE KIKE
//
