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3.A.3.6.2 Zn²⁺-, Cd²⁺-, Co²⁺-, Hg²⁺-, Ni²⁺-, Cu²⁺, Pb²⁺-ATPase (efflux), ZntA, of 732 aas and 8 TMSs (Hou and Mitra, 2003). The first four TMSs in ZntA and presumably other P1B-type ATPases play an important role in maintaining the correct dimer structure (Roberts et al. 2020).
Accession Number:	P37617
Protein Name:	ATZN aka ZntA aka B3469
Length:	732
Molecular Weight:	76840.00
Species:	Escherichia coli [83333]
Number of TMSs:	7
Location¹ / Topology² / Orientation³:	Cell inner membrane¹ / Multi-pass membrane protein²
Substrate	cadmium(2+), lead(2+), cobalt(2+), copper(2+), mercury(2+), nickel(2+), zinc(2+)

Structure:
DIP:	DIP-12947N
RefSeq:	AP_004323.1 NP_417926.1
Entrez Gene ID:	947972
Pfam:	PF00122 PF00403 PF00702
BioCyc:	EcoCyc:YHHO-MONOMER ECOL168927:B3469-MONOMER
KEGG:	ecj:JW3434 eco:b3469
Gene Ontology GO:0016021 C:integral to membrane GO:0005886 C:plasma membrane GO:0005524 F:ATP binding GO:0008551 F:cadmium-exporting ATPase activity GO:0046872 F:metal ion binding GO:0016463 F:zinc-exporting ATPase activity GO:0006754 P:ATP biosynthetic process GO:0010312 P:detoxification of zinc ion GO:0030001 P:metal ion transport GO:0046686 P:response to cadmium ion
References (8) [1] “Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes.” Sofia H.J.et.al. 8041620 [2] “The complete genome sequence of Escherichia coli K-12.” Blattner F.R.et.al. 9278503 [3] “Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.” Hayashi K.et.al. 16738553 [4] “The zntA gene of Escherichia coli encodes a Zn(II)-translocating P-type ATPase.” Rensing C.et.al. 9405611 [5] “Zinc(II) tolerance in Escherichia coli K-12: evidence that the zntA gene (o732) encodes a cation transport ATPase.” Beard S.J.et.al. 9364914 [6] “The ATP hydrolytic activity of purified ZntA, a Pb(II)/Cd(II)/Zn(II)-translocating ATPase from Escherichia coli.” Sharma R.et.al. 10660539 [7] “Global topology analysis of the Escherichia coli inner membrane proteome.” Daley D.O.et.al. 15919996 [8] “A new zinc-protein coordination site in intracellular metal trafficking: solution structure of the Apo and Zn(II) forms of ZntA(46-118).” Banci L.et.al. 12417201
1MWY 1MWZ 4umv

UniProt (Universal Protein Resource)
CDD Search (Conserved Domain Database)

Predict TMSs (Predict number of transmembrane segments)

FASTA formatted sequence

1:	MSTPDNHGKK APQFAAFKPL TTVQNANDCC CDGACSSTPT LSENVSGTRY SWKVSGMDCA 
61:	ACARKVENAV RQLAGVNQVQ VLFATEKLVV DADNDIRAQV ESALQKAGYS LRDEQAAEEP 
121:	QASRLKENLP LITLIVMMAI SWGLEQFNHP FGQLAFIATT LVGLYPIARQ ALRLIKSGSY 
181:	FAIETLMSVA AIGALFIGAT AEAAMVLLLF LIGERLEGWA ASRARQGVSA LMALKPETAT 
241:	RLRKGEREEV AINSLRPGDV IEVAAGGRLP ADGKLLSPFA SFDESALTGE SIPVERATGD 
301:	KVPAGATSVD RLVTLEVLSE PGASAIDRIL KLIEEAEERR APIERFIDRF SRIYTPAIMA 
361:	VALLVTLVPP LLFAASWQEW IYKGLTLLLI GCPCALVIST PAAITSGLAA AARRGALIKG 
421:	GAALEQLGRV TQVAFDKTGT LTVGKPRVTA IHPATGISES ELLTLAAAVE QGATHPLAQA 
481:	IVREAQVAEL AIPTAESQRA LVGSGIEAQV NGERVLICAA GKHPADAFTG LINELESAGQ 
541:	TVVLVVRNDD VLGVIALQDT LRADAATAIS ELNALGVKGV ILTGDNPRAA AAIAGELGLE 
601:	FKAGLLPEDK VKAVTELNQH APLAMVGDGI NDAPAMKAAA IGIAMGSGTD VALETADAAL 
661:	THNHLRGLVQ MIELARATHA NIRQNITIAL GLKGIFLVTT LLGMTGLWLA VLADTGATVL 
721:	VTANALRLLR RR

3.A.3.6.2
Zn²⁺-, Cd²⁺-, Co²⁺-, Hg²⁺-, Ni²⁺-, Cu²⁺, Pb²⁺-ATPase (efflux), ZntA, of 732 aas and 8 TMSs (Hou and Mitra, 2003). The first four TMSs in ZntA and presumably other P1B-type ATPases play an important role in maintaining the correct dimer structure (Roberts et al. 2020).

Cross database links:

Gene Ontology

References (8)

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3.A.3.6.2Zn2+-, Cd2+-, Co2+-, Hg2+-, Ni2+-, Cu2+, Pb2+-ATPase (efflux), ZntA, of 732 aas and 8 TMSs (Hou and Mitra, 2003). The first four TMSs in ZntA and presumably other P1B-type ATPases play an important role in maintaining the correct dimer structure (Roberts et al. 2020).

Cross database links:

Gene Ontology

References (8)

External Searches:

Analyze:

3.A.3.6.2
Zn²⁺-, Cd²⁺-, Co²⁺-, Hg²⁺-, Ni²⁺-, Cu²⁺, Pb²⁺-ATPase (efflux), ZntA, of 732 aas and 8 TMSs (Hou and Mitra, 2003). The first four TMSs in ZntA and presumably other P1B-type ATPases play an important role in maintaining the correct dimer structure (Roberts et al. 2020).