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Database: UniProt
Entry: A6TF88_KLEP7
LinkDB: A6TF88_KLEP7
Original site: A6TF88_KLEP7 
ID   A6TF88_KLEP7            Unreviewed;       736 AA.
AC   A6TF88;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-2007, sequence version 1.
DT   27-MAR-2024, entry version 109.
DE   SubName: Full=Pb/Cd/Zn/Hg transporting ATPase (P-type ATPase family) {ECO:0000313|EMBL:ABR79222.1};
GN   Name=zntA {ECO:0000313|EMBL:ABR79222.1};
GN   ORFNames=KPN_03835 {ECO:0000313|EMBL:ABR79222.1};
OS   Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=272620 {ECO:0000313|EMBL:ABR79222.1, ECO:0000313|Proteomes:UP000000265};
RN   [1] {ECO:0000313|EMBL:ABR79222.1, ECO:0000313|Proteomes:UP000000265}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700721 / MGH 78578 {ECO:0000313|Proteomes:UP000000265};
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
RN   [2] {ECO:0000313|EMBL:ABR79222.1, ECO:0000313|Proteomes:UP000000265}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700721 / MGH 78578 {ECO:0000313|Proteomes:UP000000265};
RG   The Klebsiella pneumonia Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P.,
RA   Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.;
RL   Submitted (SEP-2006) 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: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|RuleBase:RU362081}.
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DR   EMBL; CP000647; ABR79222.1; -; Genomic_DNA.
DR   RefSeq; WP_015959106.1; NC_009648.1.
DR   AlphaFoldDB; A6TF88; -.
DR   SMR; A6TF88; -.
DR   STRING; 272620.KPN_03835; -.
DR   PaxDb; 272620-KPN_03835; -.
DR   EnsemblBacteria; ABR79222; ABR79222; KPN_03835.
DR   KEGG; kpn:KPN_03835; -.
DR   HOGENOM; CLU_001771_6_4_6; -.
DR   Proteomes; UP000000265; 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; cd07546; P-type_ATPase_Pb_Zn_Cd2-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; 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   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; 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   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
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        356..381
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        387..414
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        689..707
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   DOMAIN          49..113
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
SQ   SEQUENCE   736 AA;  77095 MW;  1865ABAD3548CD82 CRC64;
     MSTPDAQDKK VPQFSSFTMR PATAPAESCC TDHACATESA PAAEALSDAR YSWQVDGMDC
     AACARKVETA VRQVPGVSQV QVLFATEKLL VHAEGDVRAQ VENAVRQAGY TLRDADAPAA
     EQTRGSLLRD NLPLLTLVIM MALSWGLEQA NHPAGQLAFI ATTLVGLWPV ARQALRLIKS
     GSWFAIETLM SVAAIGALFI GATAEAAMVL LLFLIGERLE GWAASRARQG VSALMALKPD
     TAIRLRNGVR ETVAQRDLRP GDVIEVAAGG RLPADGQLLS PFASFDESAL TGESVPVERQ
     AGERVAAGAT SVDRLVQLTV ISEPGDSAID RILKLIEEAE ERRAPIERFI DRFSRIYTPA
     IMVVALLVAI VPPLFFASAW LPWIYKGLTL LLIGCPCALV ISTPAAITSG LAVAARRGAL
     IKGGAALEQL GQVRQVAFDK TGTLTVGQPQ VTSVIATAEV DDNALLALAA AVEQGSSHPL
     AQAIVREAQR RQLSIPLASG QRALAGSGIE AEVNGSRILI CAASKAAPAE HEAQIQQLES
     AGQTVVLVMR GETLLGILAL RDTLRDDARQ AVDALHQLGV QGVILTGDNP RAAAAIASEL
     GLEFRAGLLP ADKVNAVIAL NADAPLAMVG DGINDAPAMK AATIGIAMGS GTDVALETAD
     AALTHNRLTG LAQMISLARA THANIRQNIA IALGLKGIFL VTTLLGLTGL WLAVLADTGA
     TVLVTANALR LLRKKL
//
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