ID A0A2W2CRZ3_9ACTN Unreviewed; 621 AA.
AC A0A2W2CRZ3;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Heavy metal translocating P-type ATPase {ECO:0000313|EMBL:PZF82953.1};
DE Flags: Fragment;
GN ORFNames=C1I93_30340 {ECO:0000313|EMBL:PZF82953.1};
OS Micromonospora endophytica.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=515350 {ECO:0000313|EMBL:PZF82953.1, ECO:0000313|Proteomes:UP000248627};
RN [1] {ECO:0000313|EMBL:PZF82953.1, ECO:0000313|Proteomes:UP000248627}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45430 {ECO:0000313|EMBL:PZF82953.1,
RC ECO:0000313|Proteomes:UP000248627};
RA Sahin N., Ay H., Saygin H.;
RT "Draft genome sequence of Jishengella endophytica.";
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
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:PZF82953.1}.
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DR EMBL; POTX01000447; PZF82953.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2W2CRZ3; -.
DR Proteomes; UP000248627; 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 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; 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 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 18..39
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 46..64
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 76..104
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 241..260
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 266..287
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT NON_TER 621
FT /evidence="ECO:0000313|EMBL:PZF82953.1"
SQ SEQUENCE 621 AA; 64622 MW; 49588029CB8E6325 CRC64;
MPQRPAQPGR SERSRWRLWA PLTGLTGLVL VGAVLWWSGR AGAADAVWAV VTVLALLPAA
FSVLRELWRR RFGVDVIAVL ALAGALGVGE YLAGAVIAVM LATGRTLEAY AQRRATRDLR
ALLERAPRTA RRRSADGGVE VVPVDRVAVG DRLLVGPGDV VAVDGVTESP ATLDESVVTG
ESRLVERAAG EAVASGVINA GAGFGLRATE NAERSTYAGI VRLAQEATAR KAPTVRLADR
YAAAFVPFTL VLAGLGWVLS GDFIRAVAVL VVATPCPLLL ATPIAIVSGL SRVARRGVLV
RDGGSLEVLG RARTLLVDKT GTLTAGRPRV AETVVAPGGD PDEVLRLAAS VEQLSPHVLA
AALVRQAGDR GLALRTPTEV TEEPGRGVHG RVDGRLIRVG QLTVDLPEWA AQVRSRAEAA
GHSVVWVADE HGPLGAVLFA DPVRPDAHRA VERLRAAGLT RIVMVTGDRE GTARQVADAV
GVDDVLARCT PQEKVARVRA EADRAVTVMV GDGVNDAPAL AEAHVGVAMG ATGATASADV
ADAVLTVDRL DPLADAVEVA RHARRIAVQS ATIGMGLAVL AMCFAAAGRL PPVAGAFLQE
GIDVLVILNA LRALRSPRPP A
//