ID A7HMR1_FERNB Unreviewed; 730 AA.
AC A7HMR1;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 110.
DE SubName: Full=Heavy metal translocating P-type ATPase {ECO:0000313|EMBL:ABS61194.1};
GN OrderedLocusNames=Fnod_1347 {ECO:0000313|EMBL:ABS61194.1};
OS Fervidobacterium nodosum (strain ATCC 35602 / DSM 5306 / Rt17-B1).
OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Fervidobacteriaceae;
OC Fervidobacterium.
OX NCBI_TaxID=381764 {ECO:0000313|EMBL:ABS61194.1, ECO:0000313|Proteomes:UP000002415};
RN [1] {ECO:0000313|EMBL:ABS61194.1, ECO:0000313|Proteomes:UP000002415}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35602 / DSM 5306 / Rt17-B1
RC {ECO:0000313|Proteomes:UP000002415};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Detter J.C.,
RA Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P.;
RT "Complete sequence of Fervidobacterium nodosum Rt17-B1.";
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABS61194.1, ECO:0000313|Proteomes:UP000002415}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35602 / DSM 5306 / Rt17-B1
RC {ECO:0000313|Proteomes:UP000002415};
RX PubMed=19307556; DOI=10.1073/pnas.0901260106;
RA Zhaxybayeva O., Swithers K.S., Lapierre P., Fournier G.P., Bickhart D.M.,
RA DeBoy R.T., Nelson K.E., Nesbo C.L., Doolittle W.F., Gogarten J.P.,
RA Noll K.M.;
RT "On the chimeric nature, thermophilic origin, and phylogenetic placement of
RT the Thermotogales.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:5865-5870(2009).
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; CP000771; ABS61194.1; -; Genomic_DNA.
DR RefSeq; WP_011994503.1; NC_009718.1.
DR AlphaFoldDB; A7HMR1; -.
DR STRING; 381764.Fnod_1347; -.
DR KEGG; fno:Fnod_1347; -.
DR eggNOG; COG2217; Bacteria.
DR HOGENOM; CLU_001771_0_3_0; -.
DR OrthoDB; 9760802at2; -.
DR Proteomes; UP000002415; 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; 1.
DR CDD; cd02094; P-type_ATPase_Cu-like; 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; 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; TIGR01525; ATPase-IB_hvy; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
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; 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 SUPFAM; SSF55008; HMA, heavy metal-associated domain; 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 Reference proteome {ECO:0000313|Proteomes:UP000002415};
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 90..107
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 177..194
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 328..349
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 375..404
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 677..694
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 6..71
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 730 AA; 80093 MW; 308B005AFD659AEF CRC64;
MELKEEKRTL KITGMTCANC ARIVEKSLSK VEGVKFAAVN LATNTAFVVL EKEVDEEKLK
KAVENVGYGV SDEPIEMIEE KRLKRIKSNM IIALALTIPL MILMFLHTSG KHIPYFKEIE
LIVSAIVIFY AGRDTIKGAS IALLHKHSNM DTLILFGSAT AWSTNILTYF GTNILPFGTI
GAVIVSLHLL GRYIESYLRD RASKQVRELI NLQAKEALVI TDKGEILMPV EAIKEGSIVV
VKPGERIPVD GIIVEGSTSI DESMITGESI PVSKEVNDEV VGGSLNLTGA IKIKVTKVGE
DTFLSKIINL IQEAQGAKVP IQALADRITN WFVPMIISLA TISAFVWYFN FENLNMLTQS
IRSFLPWTLH TSDPLSFAVF VFLTTVVIAC PCALGLATPM ALIVGTSLAA KKGLLIRNAE
AIQTAKEVGY VLFDKTGTLT EGKPQVIYTD LPESEYEKIL AIENLSNHPL AKAVVDYLRT
QINNKNNDIE IEKFEELHGK GVRARVNGDF YFIGKTENIS AYEDYTINGC SIVEVRKNEN
ILGFFAIQDV IRHDSREAIY KLSKMGITPV MVTGDNENTA RFVAEKLGIK EVFANVKPEE
KLDIVRKFQA KGKKVIMVGD GINDAAALKS ADIGIAVSSG SDIALDNSDI IITKGGISKV
VDAIEISKLT FKAIKTNLLF AFFYNVLAIP LAMFGLLHPA IAEGAMAMSS ITVIINSMRI
RKEKKPSCCS
//
