ID A0A0Q5SYI8_9BACT Unreviewed; 663 AA.
AC A0A0Q5SYI8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Cadmium/zinc/cobalt-transporting ATPase {ECO:0000313|EMBL:KQS28127.1};
GN ORFNames=ASG33_17230 {ECO:0000313|EMBL:KQS28127.1};
OS Dyadobacter sp. Leaf189.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Dyadobacter.
OX NCBI_TaxID=1736295 {ECO:0000313|EMBL:KQS28127.1, ECO:0000313|Proteomes:UP000051810};
RN [1] {ECO:0000313|EMBL:KQS28127.1, ECO:0000313|Proteomes:UP000051810}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf189 {ECO:0000313|EMBL:KQS28127.1,
RC ECO:0000313|Proteomes:UP000051810};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQS28127.1, ECO:0000313|Proteomes:UP000051810}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf189 {ECO:0000313|EMBL:KQS28127.1,
RC ECO:0000313|Proteomes:UP000051810};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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:KQS28127.1}.
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DR EMBL; LMPS01000005; KQS28127.1; -; Genomic_DNA.
DR RefSeq; WP_056287842.1; NZ_LMPS01000005.1.
DR AlphaFoldDB; A0A0Q5SYI8; -.
DR STRING; 1736295.ASG33_17230; -.
DR OrthoDB; 909834at2; -.
DR Proteomes; UP000051810; 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; 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 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:UP000051810};
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 55..74
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 86..103
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 115..141
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 284..304
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 316..337
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 611..631
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 637..656
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..45
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 663 AA; 71425 MW; 3E850D7A6A33F689 CRC64;
MELENKNKAQ TEADDCCSGP NAHQHKKSHE HSHDHDHDGH DHGDSGDTGL LQSRWMLWLS
LAILLGTLSA TFIFKIEIIR PVEIALMLIA YLLAGNKTIL TAGRRVMRGD FFNEFTLMTI
ATLGAFYIGE FSEGVAVMIF YEIGELFQDL AVSRSKNSIK ALLDIRPDSV TVIRNLENVQ
TTPGQVRIGE SILVKAGEKV ALDGRLLSES GVFNTAALTG EPRPDVITSG KPVLAGMINT
EKAVEVEVTA LFKDSKLSRI LEMVQDATAR KAPTQLMISK LAKIYTPIVF LLAVLIIFVP
YLFTPDYNFD QWLYRGMVFL VIACPCALTV SIPLGYFGGI GLASRNGILV KGANFLDVMT
KIDTVVSDKT GTLTKGVFQV QQVQTTMYEA DFVQLAASLE SYSTHPVAKA VVTFAAEQRL
DKPAQVEELS GLGLKGVVNQ KQVLAGNLRL LEKFSVTFPP SLSDIPETIV AVAVDGTYAG
HFIIADEIKE DAAATVSELA KMGIETIMLS GDKQAVVTST ASRLNIAKSY GGLLPEDKVR
VVEQLKAEGR RIAFVGDGVN DAPVIALADA GIAMGALGSD AAIETADIVI QNDQPSRIVS
AIRAGKVTRS IVYQNITLAM GVKLAVMIMG AGGIATLWEA VFADVGVALL AILNAFRIQG
RKI
//
