ID F7SAJ9_9PROT Unreviewed; 573 AA.
AC F7SAJ9;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 24-JAN-2024, entry version 64.
DE SubName: Full=Heavy metal translocating P-type ATPase {ECO:0000313|EMBL:EGO93819.1};
GN ORFNames=APM_3422 {ECO:0000313|EMBL:EGO93819.1};
OS Acidiphilium sp. PM.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acidiphilium.
OX NCBI_TaxID=1043206 {ECO:0000313|EMBL:EGO93819.1, ECO:0000313|Proteomes:UP000004823};
RN [1] {ECO:0000313|EMBL:EGO93819.1, ECO:0000313|Proteomes:UP000004823}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PM {ECO:0000313|EMBL:EGO93819.1,
RC ECO:0000313|Proteomes:UP000004823};
RX PubMed=21914891; DOI=10.1128/JB.05386-11;
RA San Martin-Uriz P., Gomez M.J., Arcas A., Bargiela R., Amils R.;
RT "Draft Genome Sequence of the Electricigen Acidiphilium sp. Strain PM (DSM
RT 24941).";
RL J. Bacteriol. 193:5585-5586(2011).
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:EGO93819.1}.
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; AFPR01000513; EGO93819.1; -; Genomic_DNA.
DR AlphaFoldDB; F7SAJ9; -.
DR HOGENOM; CLU_001771_0_3_5; -.
DR Proteomes; UP000004823; 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 GO; GO:0015662; F:P-type ion transporter activity; IEA:UniProt.
DR CDD; cd00371; HMA; 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; 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; 1.
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; PR00943; CUATPASE.
DR SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 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; 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 103..125
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 131..152
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 164..185
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 197..215
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 350..372
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 378..398
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 17..81
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 573 AA; 60394 MW; 819777793063183A CRC64;
MLETALSSRH PSLPQTDVLD LGIEGMTCAS CVGRVEKAIR RLPGVADVAV NLGTERARIT
GADIDVSILI AAIEKAGYDA HAIPEGGEAD AEAAKRQEIQ RDLMHVGIAA ALTAPLLVAM
IFHVAGIRMA LPGWAELALA TPVQFWLGAR FYRAGWTAVR AHTGNMDLLV ALGTSAAYLL
SLYTLLKSWS YGGTPTLYFD SSAIVITLIL FGKWLEARAK RQTGAALRAL SALRPERARL
RATDGSEREV PIDRVAVGNL VVVWPGERIP VDGLIREGES SADESMLTGE SLPVTKSVGH
KVTGGAINGD GLLLIETTAV GAESMLARIV RLVENAQAAK APIQKQVDRV AAVFVPVVLV
IAWIAFVGWW LVTGDIEQAI LSAVAVLVIA CPCSLGLATP TAVMAGTGVA ARYGILIRDA
ETLEEAHGID TVAFDKTGTL TEGNPSIVAI EPAEGIDCPE LLRLAAAVQH GSEHPLAKAV
RIRAEAEGVR APAATAVKAL PGRGITAMVE SRNLVLGSGR LLSEHGIDAD VLTGRADALQ
REGRTVSWLL DVGGAPARPR PDRLRRRAET DGA
//
