ID Q7VIL8_HELHP Unreviewed; 695 AA.
AC Q7VIL8;
DT 01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2003, sequence version 1.
DT 27-MAR-2024, entry version 147.
DE SubName: Full=Cation transport ATPase {ECO:0000313|EMBL:AAP77183.1};
GN OrderedLocusNames=HH_0586 {ECO:0000313|EMBL:AAP77183.1};
OS Helicobacter hepaticus (strain ATCC 51449 / 3B1).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=235279 {ECO:0000313|EMBL:AAP77183.1, ECO:0000313|Proteomes:UP000002495};
RN [1] {ECO:0000313|EMBL:AAP77183.1, ECO:0000313|Proteomes:UP000002495}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51449 / 3B1 {ECO:0000313|Proteomes:UP000002495};
RX PubMed=12810954; DOI=10.1073/pnas.1332093100;
RA Suerbaum S., Josenhans C., Sterzenbach T., Drescher B., Brandt P., Bell M.,
RA Droege M., Fartmann B., Fischer H.-P., Ge Z., Hoerster A., Holland R.,
RA Klein K., Koenig J., Macko L., Mendz G.L., Nyakatura G., Schauer D.B.,
RA Shen Z., Weber J., Frosch M., Fox J.G.;
RT "The complete genome sequence of the carcinogenic bacterium Helicobacter
RT hepaticus.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7901-7906(2003).
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; AE017125; AAP77183.1; -; Genomic_DNA.
DR RefSeq; WP_011115428.1; NC_004917.1.
DR AlphaFoldDB; Q7VIL8; -.
DR STRING; 235279.HH_0586; -.
DR GeneID; 82135183; -.
DR KEGG; hhe:HH_0586; -.
DR eggNOG; COG2217; Bacteria.
DR HOGENOM; CLU_001771_6_2_7; -.
DR OrthoDB; 2490525at2; -.
DR Proteomes; UP000002495; 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; cd07548; P-type_ATPase-Cd_Zn_Co_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 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 HMA2; 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 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:UP000002495};
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 86..103
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 109..128
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 149..173
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 316..335
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 347..369
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 656..685
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 2..64
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 695 AA; 76648 MW; 315049E4C37229A4 CRC64;
MKQHILILKG IDCANCAQRI EDALNALPNT KEANIDFSTN MLYIYTDNLT KVIHTITHIE
PQVSVLETSS SYISPLQEDT KHSHELLSIS IFIAIFIFCM AALHIDSLYI PPIVAYILLS
IVYIGSGIPI FSATWRNCKN KLFFDEHSLM LFATLAALCI GEISEAVAVM LFFRVGEFLE
SLAVQKSKRS INALLQIMPD IAHKKHNDTL QDLHPQELSV GDIIVIKVGE KIPTDGIVLK
GKSYLDMRSI NGESVPVSIN EGQSIIAGAI NTTAMLEVRV EKPFKDSHIA KIAKLTQEAS
ANKAKTQKVI TSFARIYTPI IFFLSLSLAL IPPLFDEQWH EWVYRALVVM MISCPCALVI
AVPLGYFAAI GQASAKGILF KGSTYLETLA QVKNIIFDKT GTLTLGTFEI LSIVPNEGYT
QQDLLEIASL AEQNSNHPIA TCIKNHLNTM CHIESYEEIS GKGVRLLSDK GEILAGNAAL
MQENHISFTP IHTPHTTIYV ALKGTYVGHI LIGDKIKEGI KDDLKMLKHY GIKHFAILSG
DNQTNVDCLA KELGISHAYG NLLPAQKEQK LAEFMEQWQE KIAFVGDGIN DAIVLRRSDV
GISINTGETS NDISKESADI ILQHNSLQGL VQAFKIAHHT RSITWQNISF ALASKLVLII
LSIMGIANMW LAVFGDVGIA LLALLNAMRP PRSKN
//
