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Database: UniProt
Entry: F7NS70_9GAMM
LinkDB: F7NS70_9GAMM
Original site: F7NS70_9GAMM 
ID   F7NS70_9GAMM            Unreviewed;       724 AA.
AC   F7NS70;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   24-JAN-2024, entry version 62.
DE   SubName: Full=Copper/silver-translocating P-type ATPase {ECO:0000313|EMBL:EGM79216.1};
GN   ORFNames=Rhein_0604 {ECO:0000313|EMBL:EGM79216.1};
OS   Rheinheimera sp. A13L.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Rheinheimera.
OX   NCBI_TaxID=506534 {ECO:0000313|EMBL:EGM79216.1, ECO:0000313|Proteomes:UP000004282};
RN   [1] {ECO:0000313|EMBL:EGM79216.1, ECO:0000313|Proteomes:UP000004282}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A13L {ECO:0000313|EMBL:EGM79216.1,
RC   ECO:0000313|Proteomes:UP000004282};
RX   PubMed=21742876; DOI=10.1128/JB.05636-11;
RA   Gupta H.K., Gupta R.D., Singh A., Chauhan N.S., Sharma R.;
RT   "Genome Sequence of Rheinheimera sp. Strain A13L, Isolated from Pangong
RT   Lake, India.";
RL   J. Bacteriol. 193:5873-5874(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:EGM79216.1}.
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DR   EMBL; AFHI01000004; EGM79216.1; -; Genomic_DNA.
DR   RefSeq; WP_008897497.1; NZ_AFHI01000004.1.
DR   AlphaFoldDB; F7NS70; -.
DR   STRING; 506534.Rhein_0604; -.
DR   eggNOG; COG2217; Bacteria.
DR   OrthoDB; 9814270at2; -.
DR   Proteomes; UP000004282; 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   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; TIGR01511; ATPase-IB1_Cu; 1.
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   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   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        87..111
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        117..136
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        148..172
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        184..202
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        336..358
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        364..389
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        675..694
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        700..717
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   DOMAIN          3..67
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
SQ   SEQUENCE   724 AA;  76385 MW;  7D524468D06C5A3A CRC64;
     MSEQIQLSIS GMSCASCVGR IEKALAKVSG VQQASVNLAT ETATIQGESL TSQLLIAAVE
     QAGYQASVPA EAPIAEVTRT AFYQQEYWPA VASIVLTLPL VLPMLGLLFG LDWMLPALWQ
     WLLATPVQFY FGARFYKAGW AALKAGSGTM DLLVAIGTSA AYGLSLYLWW SFDAHQGQHG
     APHLYFESSS AVLSLVLLGK YLEQKAKRRT TDALRALENL KPAVATLFQG GLWLEVKAET
     VQQGDLVLVK PGERIAVDAL VEQGQSHVDE ALISGESVPV SKSPGDKVTG GSVNLDGVLQ
     LRATAVGAES TLSRIIQLVE QAQGAKAPVQ ALVDKISAVF VPVVLVIALV TLLGWGLITA
     DWVAGILNAV AVLVIACPCA LGLATPAAIM AGTGSAARSG ILIKDATALE QATAISLVVF
     DKTGTLTQGK PVLQQFSTFA DEPELLLWAA SLQQHSEHPL AKALLCYATE HQVTAVETEQ
     FQVVAGKGVL GKVEGRHLVL GSSHWMQQLG LALPLDQIAT SAASVSWLAE QQGESYQLLA
     LFCFTDQLKP DALHAVSLLK QQGITVAMLT GDSKNSAAAI AAELELSLWK AEVLPAEKAA
     AIGLWQQQGY TVAMVGDGIN DAPALAQADL GVAMASGTEV AVSASAMTLM RSKPVLVSAA
     LQIARLSYRK IQQNLFWAFI FNIVGIPLAA LGYLNPVIAG AAMASSSLLV ISNALLLQRW
     KAKE
//
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