ID A0A2K8U616_9GAMM Unreviewed; 836 AA.
AC A0A2K8U616;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Copper-translocating P-type ATPase {ECO:0000313|EMBL:AUB81038.1};
GN ORFNames=THSYN_08790 {ECO:0000313|EMBL:AUB81038.1};
OS Candidatus Thiodictyon syntrophicum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Thiodictyon.
OX NCBI_TaxID=1166950 {ECO:0000313|EMBL:AUB81038.1, ECO:0000313|Proteomes:UP000232638};
RN [1] {ECO:0000313|EMBL:AUB81038.1, ECO:0000313|Proteomes:UP000232638}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cad16T {ECO:0000313|EMBL:AUB81038.1,
RC ECO:0000313|Proteomes:UP000232638};
RA Luedin S.M., Pothier J.F., Danza F., Storelli N., Wittwer M., Tonolla M.;
RT "Complete genome sequence of Candidatus 'Thiodictyon syntrophicum' sp. nov.
RT strain Cad16T, a photolithoautotroph purple sulfur bacterium isolated from
RT an alpine meromictic lake.";
RL Submitted (MAR-2017) 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; CP020370; AUB81038.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K8U616; -.
DR KEGG; tsy:THSYN_08790; -.
DR OrthoDB; 9814270at2; -.
DR Proteomes; UP000232638; Chromosome.
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; IPR021993; ATPase-cat-bd.
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 InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01511; ATPase-IB1_Cu; 1.
DR NCBIfam; TIGR01525; ATPase-IB_hvy; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR43520; ATP7, ISOFORM B; 1.
DR PANTHER; PTHR43520:SF5; CATION-TRANSPORTING P-TYPE ATPASE-RELATED; 1.
DR Pfam; PF12156; ATPase-cat_bd; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00403; HMA; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00120; HATPASE.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 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 SUPFAM; SSF55008; HMA, heavy metal-associated domain; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS01229; COF_2; 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 Reference proteome {ECO:0000313|Proteomes:UP000232638};
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 182..203
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 215..236
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 248..267
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 279..296
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 430..452
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 458..487
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 785..802
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 98..164
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 836 AA; 88766 MW; 5FAC72B9B6ED67E9 CRC64;
MVSRSAPEGT RSGCFHCGLP LNPGSEVTAV IRGGERAFCC IGCRSVCEAI HTAGLDGFYR
RTTAGEPLGP PPELPRDLRL YDLDAVQEEF VDIAVDDREI NLLVEGIHCA ACVWLIETGL
KTLPGVTEAR VNLTGRRLRV RWDNGRLKLS TLLRRLGDLG FSAVPFDPES AEGALRRQGR
DLLYRMAFAG FAMMNLLWVS IALYSGADRG EFRGLFQWVG CALATPTLLY SGYPFYQGAW
AGLRSGRLGM DLPIAIGASI TYVYSLYVTV SGTRAGEVYW DTVVNFLFVI LLGRFLEGLS
RRAAVASTQR LLDLQPKVAT VLRDDTETLV PIRSIARDEL VLVRPGERVP VDGAVVEGLS
EVDESMLTGE SRPVRKTQGE TVCAGTINGA GVLKVRATAT LRDTALGRII RLVEDAQASR
APIQRLADRI VPWFVALTLG LAALTFIAWV GVDLQTAILA GTAVLIITCP CAFGMATPMA
VAVAAGLGAS RGILIKNGAV LERLSSIEHF VFDKTGTLTT GRPEVTGWRF GSAPWQSLGS
EPLVLADDRR DLLRRVGALE RLSEHPAAAA VLALCERLDI ATAPARVASV EVVPGLGIRG
QVDGALVVVG SADWLADNAL APAALDGAAP RSDGSREGGL IHCAVAGLGT LVLATADRLR
PGAAAVIARM RAQGLRVTLL TGDRCAAAEH IATELGAIEV IAEVLPADKD RVIAELQTKG
RRVAMIGDGV NDAPALVRAD VGIAMGSGTD VSIASADIVL MSNELERVAE AAELSRRTLR
TIRQNIGISI VYNLIMVPLA MAAVLTPLIA AIAMPLSSLA VIGNSARIRG LFKGRP
//
