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Database: UniProt
Entry: A0A2A2GUR6_9HELI
LinkDB: A0A2A2GUR6_9HELI
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ID   A0A2A2GUR6_9HELI        Unreviewed;       702 AA.
AC   A0A2A2GUR6;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Cadmium-translocating P-type ATPase {ECO:0000313|EMBL:PAV00764.1};
GN   ORFNames=B9T66_01990 {ECO:0000313|EMBL:PAV00764.1};
OS   Helicobacter sp. TUL.
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=1848928 {ECO:0000313|EMBL:PAV00764.1, ECO:0000313|Proteomes:UP000218502};
RN   [1] {ECO:0000313|EMBL:PAV00764.1, ECO:0000313|Proteomes:UP000218502}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TUL {ECO:0000313|EMBL:PAV00764.1,
RC   ECO:0000313|Proteomes:UP000218502};
RA   Van Der Mee-Marquet N., Benejat L., Diene S.M., Gaia N., Cherkaoui A.,
RA   Lemaignen A., Ducournau A., Lacomme S., Gontier E., Bernard L., Megraud F.,
RA   Goudeau A., Lehours P., Francois P.;
RT   "Helicobacter caesarodunum: a novel human pathogen identified in a
RT   bloodstream infection.";
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
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:PAV00764.1}.
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DR   EMBL; NESU01000002; PAV00764.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A2GUR6; -.
DR   Proteomes; UP000218502; 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   CDD; cd00371; HMA; 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; 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 HMA4-RELATED; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF00403; HMA; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
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; 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   Reference proteome {ECO:0000313|Proteomes:UP000218502};
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        88..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        120..139
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        326..347
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        353..378
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        651..672
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   DOMAIN          11..73
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
SQ   SEQUENCE   702 AA;  76739 MW;  75A236530C32881A CRC64;
     MITAMNFWRA CMQTFHITNL ECPSCADTLE RKLRNIKGVR FVQISFATNT LTIDCDDIES
     IKQAISSLEP KVKITKKPQK SYIFTPQLFI LLGLIALFLA SLGCMHWLTS LEQKTSDFWI
     FSIKLLWILI YLVSGRNVIK GAIQSFKHKE FFDENVLMLT ASIAAFCLGA WEEAVSIMLF
     FATGEYLQEV SVKKSKQAIN ESANLIPPKA HIIDTTTHQT QDIDPKDLAI GDHIILYAGE
     MLSCDCVLMQ ESASFNTAAI SGESLPIESK QGDEILSGAI ALNQAITLQV LRPFATSQIA
     KIADLIASAT TQKSPTENFI TTFARYYTPI VFALALALAL IPPIFFGASF EEWIYRALVV
     LMVSCPCALV ISVPIGYFGG LAAASKRGAL IKGSNYLEAL SKLSIIAFDK TGTLTKGVFE
     VLDIIPNTGF SKDEVLATAL CAHNLSNHPI AQSIKDAYHK LGHTHHISEY EELSGLGVRA
     VCDNHEILAG NDKILHTFDI AHNTCHVQGS VVHIVRDKQY LGYILIADVL KDEAPQVINT
     LHKLHIDSIM LSGDGEYPCK QVAQKLGCNY RHSLLPQDKA QIMRELKANN SGKVAFVGDG
     INDAPTLALA DVGIAMGSGS DISIQNADVI ITNNSLKTLL QSIQIAKKTK IIIYQNIALA
     LGIKAVFIVL GLCGFATIWE AIFGDVGVAL LALANAMRCM RI
//
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