ID B8GPE4_THISH Unreviewed; 838 AA.
AC B8GPE4;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE SubName: Full=Heavy metal translocating P-type ATPase {ECO:0000313|EMBL:ACL74064.1};
GN OrderedLocusNames=Tgr7_2994 {ECO:0000313|EMBL:ACL74064.1};
OS Thioalkalivibrio sulfidiphilus (strain HL-EbGR7).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Thioalkalivibrio.
OX NCBI_TaxID=396588 {ECO:0000313|EMBL:ACL74064.1, ECO:0000313|Proteomes:UP000002383};
RN [1] {ECO:0000313|EMBL:ACL74064.1, ECO:0000313|Proteomes:UP000002383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HL-EbGR7 {ECO:0000313|EMBL:ACL74064.1,
RC ECO:0000313|Proteomes:UP000002383};
RX PubMed=21475584;
RA Muyzer G., Sorokin D.Y., Mavromatis K., Lapidus A., Clum A., Ivanova N.,
RA Pati A., d'Haeseleer P., Woyke T., Kyrpides N.C.;
RT "Complete genome sequence of 'Thioalkalivibrio sulfidophilus' HL-EbGr7.";
RL Stand. Genomic Sci. 4:23-35(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}.
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DR EMBL; CP001339; ACL74064.1; -; Genomic_DNA.
DR RefSeq; WP_012639527.1; NC_011901.1.
DR AlphaFoldDB; B8GPE4; -.
DR STRING; 396588.Tgr7_2994; -.
DR KEGG; tgr:Tgr7_2994; -.
DR eggNOG; COG2217; Bacteria.
DR HOGENOM; CLU_001771_0_3_6; -.
DR Proteomes; UP000002383; 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 CDD; cd02079; P-type_ATPase_HM; 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; 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; 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; 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|RuleBase:RU362081};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362081};
KW Reference proteome {ECO:0000313|Proteomes:UP000002383};
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 203..223
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 235..256
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 268..290
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 296..314
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 450..470
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 476..500
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 787..804
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 115..181
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 838 AA; 89855 MW; 9293BE43664C0C82 CRC64;
MSADPAARDT SSPDASTPDR QGAEASCFHC GQPIPPGAHY GVTIHTQPRA MCCPGCQAVA
QAIVDAGLSD YYLHRTETPA GPADAMPAAL RDELALYDRP ELQRSFVRVD DANVREAALI
LEGIVCAACV WLNERHVKSL PGVLEFAVNY STHRARLRWD DSRIHLSDIL KAIRDIGYRA
HPFDPGRQEE VYQRERNAAL RRLAVAGLGM MQVMMLAVAL WIGGDEPDYE GMMQFIRWVA
FLVATPVVLY AGSSFFTSAW RDLRQRQLGM DVPVALAIGS TYLASGWATI TASGEVYFES
VTMFVFFLLT GRYLEMGARQ RAGQATEALG KLLPAMAIRI TDQGDVPVPV ADLAPGDRVR
IRPGDTVPAD GTVLEGRSSV NEAMITGESL PRLRQSGDEL TGGTVNVESP LVMRVDKVGA
DTLLSAIQRL LDRAQTEKPR LARMAERGTG HFVAAVLLLT AIVGAVWWFW IDPSRAFWVM
VAMLVVTCPC ALALATPVAL TAATGSLTGR GVLVTRGHAL ETLAEATDVV FDKTGTLTEG
RLARAETLVL GDRGEAACLA LAAVLEQGSE HPVARVFQRA GTPAGQLTEQ RSTPGLGMEG
RVDGARYRIG AADFVAALAP AQPWPTQALA ELAHRHPTGS LVLLGGESGP LAAFVLEDRL
REDAAECVAV LKARGLGVHL FSGDHPDTVR HVAAGLGIDQ ARGGLRPEDK LQALAELQAR
PGAVVAMVGD GINDAPVLSR AHVSIAMAEG THLAQASADM ILYGDRLGQL PNAHRLSRRM
VQIVRQNIRW AIGYNVIALP VAASGVLTPW MAALGMSLSS LIVVVNSLRL RENPSPRR
//
