ID U4KE79_9VIBR Unreviewed; 762 AA.
AC U4KE79;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Lead, cadmium, zinc and mercury-transporting ATPase {ECO:0000313|EMBL:CCO57208.1};
DE EC=3.6.3.3 {ECO:0000313|EMBL:CCO57208.1};
DE EC=3.6.3.5 {ECO:0000313|EMBL:CCO57208.1};
GN Name=zntA {ECO:0000313|EMBL:CCO57208.1};
GN ORFNames=VIBNI_A1056 {ECO:0000313|EMBL:CCO57208.1};
OS Vibrio nigripulchritudo.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=28173 {ECO:0000313|EMBL:CCO57208.1, ECO:0000313|Proteomes:UP000016895};
RN [1] {ECO:0000313|EMBL:CCO57208.1, ECO:0000313|Proteomes:UP000016895}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SnF1 {ECO:0000313|Proteomes:UP000016895};
RX PubMed=23739050; DOI=10.1038/ismej.2013.90;
RA Goudenege D., Labreuche Y., Krin E., Ansquer D., Mangenot S., Calteau A.,
RA Medigue C., Mazel D., Polz M.F., Le Roux F.;
RT "Comparative genomics of pathogenic lineages of Vibrio nigripulchritudo
RT identifies virulence-associated traits.";
RL ISME J. 7:1985-1996(2013).
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; FO203526; CCO57208.1; -; Genomic_DNA.
DR RefSeq; WP_022550201.1; NC_022528.1.
DR AlphaFoldDB; U4KE79; -.
DR STRING; 28173.VIBNI_A1056; -.
DR KEGG; vni:VIBNI_A1056; -.
DR PATRIC; fig|1260221.3.peg.1020; -.
DR eggNOG; COG2217; Bacteria.
DR OrthoDB; 9814270at2; -.
DR Proteomes; UP000016895; Chromosome 1.
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; TIGR01511; ATPase-IB1_Cu; 1.
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 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU362081};
KW Cell membrane {ECO:0000256|RuleBase:RU362081};
KW Hydrolase {ECO:0000313|EMBL:CCO57208.1};
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:UP000016895};
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 175..192
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 377..397
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 409..433
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 713..731
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 65..130
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 762 AA; 80458 MW; 2F16EB51BFB8C9E5 CRC64;
MCIKHESCKS KHTGPTLSIS SCAPIAPLES NTESGHCCNG DSCSGGGETA SIEEEGERSP
GGDMLSGSWK ILGMDCPSCA RKVENAVSAI KDVSHTKVLF ATEKLVVQYQ EAATLPLIEQ
AVRKAGFQFE QPKKQVEPKT TENRTLTFLK SNLNIISLSA AMAISTIINQ VSPQVGAWMF
TFVCIAGLYP VAKKALQLAK SGTPFAIETL MSVAALGALY LGETIEAAMV LLLFLLGERL
EAYAASRARS GVQSLMALVP ENTIRIENGI RVEVAASELS VGDIIEVAPG DRLPADGKLV
DTNASFDESA LTGESVPVGR DIGDQVMAGS VVVDKVVRLS ITSEQGENAI DRILHLIEEA
ESRKAPLERF LDKFSRWYTP LMMLVSLLVI ITPPLFFEQP WETWVYRGLA LLLIACPCAL
VISTPAAITS GLATAAKRGA LIKGGAALEQ LGKIEAVAFD KTGTLTLGKP QVTDVKPVNE
LDANTLLTLA AAIEVGSSHP LAKSLVQKAE SSGLVLPEAK NKQAQIGSGI SGEVDGKPVI
LISPSKFQGQ VSSDLKTEIE SLESRGKTVV LVSVSGALEG LIAWQDTLRD DAAPAVEKLK
KLGIDSVMLT GDNPLAAKEM ASKVAMDFKA SLLPADKVSY VNELAQHKHV AMVGDGINDA
PAMKAASVGI AMGGGTDVAL ETADAALTHS RLEELPAMIE LSKATLRNIQ QNVALALGLK
GVFLFTSLFG ITGLWVAVLA DSGATALVTL NALRLLRFTP KD
//
