ID H2FTM2_OCESG Unreviewed; 798 AA.
AC H2FTM2;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=Heavy metal translocating P-type ATPase {ECO:0000313|EMBL:AEY02580.1};
GN OrderedLocusNames=GU3_14135 {ECO:0000313|EMBL:AEY02580.1};
OS Oceanimonas sp. (strain GK1 / IBRC-M 10197).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Oceanimonas.
OX NCBI_TaxID=511062 {ECO:0000313|EMBL:AEY02580.1, ECO:0000313|Proteomes:UP000007742};
RN [1] {ECO:0000313|EMBL:AEY02580.1, ECO:0000313|Proteomes:UP000007742}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GK1 {ECO:0000313|EMBL:AEY02580.1,
RC ECO:0000313|Proteomes:UP000007742};
RX PubMed=22461556; DOI=10.1128/JB.00023-12;
RA Parsa Yeganeh L., Azarbaijani R., Sarikhan S., Mousavi H., Ramezani M.,
RA Amoozegar M.A., Shahzadeh Fazeli A., Salekdeh G.H.;
RT "Complete genome sequence of Oceanimonas sp. GK1, a halotolerant bacterium
RT from Gavkhouni Wetland in Iran.";
RL J. Bacteriol. 194:2123-2124(2012).
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; CP003171; AEY02580.1; -; Genomic_DNA.
DR AlphaFoldDB; H2FTM2; -.
DR STRING; 511062.GU3_14135; -.
DR KEGG; oce:GU3_14135; -.
DR eggNOG; COG2217; Bacteria.
DR HOGENOM; CLU_001771_0_3_6; -.
DR Proteomes; UP000007742; 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; 2.
DR CDD; cd02094; P-type_ATPase_Cu-like; 1.
DR Gene3D; 3.30.70.100; -; 2.
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; 2.
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; 2.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS01047; HMA_1; 1.
DR PROSITE; PS50846; HMA_2; 2.
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:UP000007742};
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 143..161
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 181..200
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 220..240
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 246..264
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 398..420
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 426..449
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 742..761
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 767..789
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 1..51
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 53..119
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 798 AA; 84266 MW; 712E56AEEB0BF80A CRC64;
MSRVEKSLNA VPGVRSASVN LASNSAELTL DQDTAAGELV AAVEQAGYQC PVERVELVIG
GMSCASCTGR VEKVLGRLPG VLSATVNLAA GRAYVELLSG SQDMSALVAA VEKAGFSAEA
AEDASNADEQ DGREREQQSL KHALMMAAVL TLPVFVLEMG SHFVPGMHHW IERTLGQSLN
WQLQFVLATL VLFGPGLLFL KKGLPALLRG EPEMNSLVAL GGLAAWGYST VATFAGHWLP
EGSRQVYFEA AAVIVTLILL GRFLEARAKG RTGEAIQKLL SLQAPTARVE RDGNTEEVPL
ERVRVRDPVR VRPGERIPVD GTVMEGSSWV DESMLTGEPD PVEKSQGSEV TGGTVNNKGS
LLIEVTRVGK QTRLSQIIRM VEQAQGAKLP IQALVDKVTA VFVPVVISLA LLTFALWWWL
GPEPALSFAL VNGVAVLIIA CPCAMGLATP TSIMVGTGRA AELGVLFRRG EALQSLRGVR
VVAFDKTGTL TEGKPELTDL ETLDGVDKDS VLARIAAVEQ RSEHPIAEAL LAAAKERNLK
LPEVSEFDTV TGMGVQAKVD GVRVEVGADR YLKSLKMDLS DFADTAARLA SEGKTPLYAA
IDGRAVAILA VADRVKEGTP DAIAALHEQG LKVAMITGDN QGTADAIARQ LGIDAVEAEV
MPDGKVEALE HLRKQHGTVA FVGDGINDAP ALAAADVGLA IGTGTDIAIE AAQVVLMRGD
LRAVPQALAI SHATLRNIRQ NLFWAFAYNV GLIPVAAGVL YPAFGVLLSP MLAAGAMALS
SVFVVSNALR LKRFSPAG
//
