ID A0A1G8UVQ2_9FLAO Unreviewed; 645 AA.
AC A0A1G8UVQ2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Cd2+/Zn2+-exporting ATPase {ECO:0000313|EMBL:SDJ57724.1};
GN ORFNames=SAMN04487935_1062 {ECO:0000313|EMBL:SDJ57724.1};
OS Flavobacterium noncentrifugens.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1128970 {ECO:0000313|EMBL:SDJ57724.1, ECO:0000313|Proteomes:UP000199580};
RN [1] {ECO:0000313|EMBL:SDJ57724.1, ECO:0000313|Proteomes:UP000199580}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10076 {ECO:0000313|EMBL:SDJ57724.1,
RC ECO:0000313|Proteomes:UP000199580};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FNEZ01000002; SDJ57724.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G8UVQ2; -.
DR STRING; 1128970.SAMN04487935_1062; -.
DR OrthoDB; 1521937at2; -.
DR Proteomes; UP000199580; 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 InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01512; ATPase-IB2_Cd; 1.
DR NCBIfam; TIGR01525; ATPase-IB_hvy; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
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; SFLDS00003; Haloacid_Dehalogenase; 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 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:UP000199580};
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 37..54
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 60..79
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 264..284
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 296..323
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 593..613
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 619..638
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
SQ SEQUENCE 645 AA; 70384 MW; D718B119F87F99EA CRC64;
MEKEHNKNED IERAIIAAGN NANHPVEESS WKSHWQLLLS IQILFVMLTL EFGFDYVPPF
PGNLIIFFIA YLLSGYNVLY LAWRKAIRFD FFNEFFLMSI ATLGAFAIGE YSEGVAVMAF
YSIGEWFQDA AVNRAKRSIK ALLDIRPDEV SVVRNGTTVV VNPKEVQIGE VIRVKPGEKV
ALDGKLISEK AAFNTAALTG ESKPDSKAKG EVVYAGMINL NTVSEIKVNS LFTDSKLSRI
LEMVQDATAR KSQTQLFISR FAKIYTPIVF ALAVAVCFVP YFFVDPYIFN VWFYRALVFL
VISCPCALVV SIPLGYFGGI GLASRNGILF KGSNFLDVMT KIDTVVMDKT GTLTEGVFKV
QEIVTKDIEE SYLIKLAAAI ESQSTHPIGL AVVEHAGKET AELSVAEVEE ISGHGLKGKI
DGKEVLAGNT KLMKKFNIDY PAEVDAIVYT IVVVAVDKKY KGYITIADKI KEDAKQAIKE
LHKLNIKTVM LSGDKQSVVD EVAKQLAIDS AYGDLLPEGK VEKVQALKNE GRRIAFVGDG
VNDAPVVALA DAGIAMGGLG SDATIETADI VIQNDQPSKI VTAIKAGKIT RNIVWQNIIL
AMVVKIIVLA LGAGGVATLW EAVIADVGVA LLAILNAVRI QKMKL
//