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Database: UniProt
Entry: A0A1B0VLN9_FERIS
LinkDB: A0A1B0VLN9_FERIS
Original site: A0A1B0VLN9_FERIS 
ID   A0A1B0VLN9_FERIS        Unreviewed;       865 AA.
AC   A0A1B0VLN9;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2023, sequence version 2.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Cadmium-translocating P-type ATPase {ECO:0000313|EMBL:AMW33644.2};
GN   Name=cadA {ECO:0000313|EMBL:AMW33644.2};
GN   ORFNames=NA23_01330 {ECO:0000313|EMBL:AMW33644.2};
OS   Fervidobacterium islandicum.
OC   Bacteria; Thermotogota; Thermotogae; Thermotogales; Fervidobacteriaceae;
OC   Fervidobacterium.
OX   NCBI_TaxID=2423 {ECO:0000313|EMBL:AMW33644.2, ECO:0000313|Proteomes:UP000093740};
RN   [1] {ECO:0000313|EMBL:AMW33644.2, ECO:0000313|Proteomes:UP000093740}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AW-1 {ECO:0000313|EMBL:AMW33644.2,
RC   ECO:0000313|Proteomes:UP000093740};
RX   PubMed=26421103; DOI=10.1186/s40793-015-0063-4;
RA   Lee Y.J., Jeong H., Park G.S., Kwak Y., Lee S.J., Lee S.J., Park M.K.,
RA   Kim J.Y., Kang H.K., Shin J.H., Lee D.W.;
RT   "Genome sequence of a native-feather degrading extremely thermophilic
RT   Eubacterium, Fervidobacterium islandicum AW-1.";
RL   Stand. Genomic Sci. 10:71-71(2015).
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; CP014334; AMW33644.2; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1B0VLN9; -.
DR   STRING; 2423.NA23_01330; -.
DR   KEGG; fia:NA23_01330; -.
DR   eggNOG; COG2217; Bacteria.
DR   Proteomes; UP000093740; 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   CDD; cd00371; HMA; 3.
DR   CDD; cd07548; P-type_ATPase-Cd_Zn_Co_like; 1.
DR   Gene3D; 3.30.70.100; -; 3.
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; 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; 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; PF00403; HMA; 3.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00941; CDATPASE.
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; 3.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
DR   PROSITE; PS01047; HMA_1; 1.
DR   PROSITE; PS50846; HMA_2; 3.
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   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        280..296
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        480..500
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        512..533
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        817..836
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   DOMAIN          2..70
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
FT   DOMAIN          80..149
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
FT   DOMAIN          159..228
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
SQ   SEQUENCE   865 AA;  93425 MW;  8C74FA3FF12B54B8 CRC64;
     MLKKEVILEG LDCANCAAKI EEEVNKLNGV KAYMNFMNKT LTLEIESEQE YKNILQQVKT
     IVHKHEPDVV VKEKSVNKSN KKVLILEGLD CANCAAKIEA QTQSLEGVNS ATVDFVSKKL
     TIEAVDKKEF GKILGEVTSI VNKLEPDVKI VDAEKKKVNK SIVMLEGLGC ANCAAKIEKE
     ISGLEGVEFA AVDFVSKKLT LEISPKVNRS ELNEKIEGIV KKIEPDVKVI FEENTSKANV
     KENNEEEEEG VNKKEIIRLV VGGAIFAVGI IFNFQNWLEL TLFIISYIIV GGEVVLRAIK
     GIARGQVFSE HFLMSIATIG AFFVGEYPEG VAVMLFYLVG ELLQNIAVGH SRKSISALMD
     IRPDYANLKV GDEIRKVSPE EVNIGDIIIV KPGEKVPLDG KVIEGNSMVD TAALTGESVP
     REVGPGDDVL SGFINKNGVL TIEVTKDYGD STVSKILDLV QNASSRKAPT EKFITKFARF
     YTPIVVFGAL ALAIIPPLVI PGATFSTWIY RALVFLVISC PCALVVSIPL GFFGGIGGAA
     KRGILVKGSN YLDALNNVET VVFDKTGTLT KGVFEVVSIN PQSDFTKEEL IEYAAYAESH
     SSHPIALSIL KAYNKDVDIT KIEDYEEIAG HGIRAKVGGK EILVGNSKLM NKENIKYQEV
     ETLGTVVHVA VDKKYAGNIV ISDAVKEDSA DAIKGLKALG VRNIVMLTGD SKAVGEKIAT
     QLGIDEVYTE LLPADKVEKI EALDAKKSHK GKIVFVGDGI NDAPVLARAD IGVAMGGLGS
     DAAIEAADIV IMTDEPSKIV TAIKIAKRTR KIVMQNIVFA LGVKAIFLAL GAVGVATMWE
     AVFADTGVAI IAILNAMRVM NTKSI
//
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