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3.A.3.6.1 Zn²⁺-, Cd²⁺-, Pb²⁺-ATPase (efflux). The enzyme from S. aureus strain 17810R, of 726 aas, functions as a Cd²⁺:H⁺ antiporter, using both the pmf and ATP hydrolysis to drive Cd²⁺ expulsion (Tynecka et al. 2016).
Accession Number:	P20021
Protein Name:	CadA
Length:	727
Molecular Weight:	78812.00
Species:	Staphylococcus aureus [1280]
Number of TMSs:	9
Location¹ / Topology² / Orientation³:	Cell membrane¹ / Multi-pass membrane protein²
Substrate	cadmium(2+), lead(2+), zinc(2+), hydron

Pfam:	PF00122 PF00403 PF00702
Gene Ontology GO:0016021 C:integral to membrane GO:0005886 C:plasma membrane GO:0015297 F:antiporter activity GO:0005524 F:ATP binding GO:0008551 F:cadmium-exporting ATPase activity GO:0005261 F:cation channel activity GO:0046872 F:metal ion binding GO:0006754 P:ATP biosynthetic process GO:0030001 P:metal ion transport GO:0046686 P:response to cadmium ion
References (1) [1] “Cadmium resistance from Staphylococcus aureus plasmid pI258 cadA gene results from a cadmium-efflux ATPase.” Nucifora G.et.al. 2524829

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

Predict TMSs (Predict number of transmembrane segments)

FASTA formatted sequence

1:	MSEQKVKLME EEMNVYRVQG FTCANCAGKF EKNVKKIPGV QDAKVNFGAS KIDVYGNASV 
61:	EELEKAGAFE NLKVSPEKLA NQTIQRVKDD TKAHKEEKTP FYKKHSTLLF ATLLIAFGYL 
121:	SHFVNGEDNL VTSMLFVGSI VIGGYSLFKV GFQNLIRFDF DMKTLMTVAV IGATIIGKWA 
181:	EASIVVILFA ISEALERFSM DRSRQSIRSL MDIAPKEALV RRNGQEIIIH VDDIAVGDIM 
241:	IVKPGEKIAM DGIIVNGLSA VNQAAITGES VPVSKAVDDE VFAGTLNEEG LIEVKITKYV 
301:	EDTTITKIIH LVEEAQGERA PAQAFVDKFA KYYTPIIMVI AALVAVVPPL FFGGSWDTWV 
361:	YQGLAVLVVG CPCALVISTP ISIVSAIGNA AKKGVLVKGG VYLEKLGAIK TVAFDKTGTL 
421:	TKGVPVVTDF EVLNDQVEEK ELFSIITALE YRSQHPLASA IMKKAEQDNI PYSNVQVEEF 
481:	TSITGRGIKG IVNGTTYYIG SPKLFKELNV SDFSLGFENN VKILQNQGKT AMIIGTEKTI 
541:	LGVIAVADEV RETSKNVIQK LHQLGIKQTI MLTGDNQGTA NAIGTHVGVS DIQSELMPQD 
601:	KLDYIKKMQS EYDNVAMIGD GVNDAPALAA STVGIAMGGA GTDTAIETAD IALMGDDLSK 
661:	LPFAVRLSRK TLNIIKANIT FAIGIKIIAL LLVIPGWLTL WIAILSDMGA TILVALNSLR 
721:	LMRVKDK

3.A.3.6.1
Zn²⁺-, Cd²⁺-, Pb²⁺-ATPase (efflux). The enzyme from S. aureus strain 17810R, of 726 aas, functions as a Cd²⁺:H⁺ antiporter, using both the pmf and ATP hydrolysis to drive Cd²⁺ expulsion (Tynecka et al. 2016).

Cross database links:

Gene Ontology

References (1)

External Searches:

Analyze:

3.A.3.6.1Zn2+-, Cd2+-, Pb2+-ATPase (efflux). The enzyme from S. aureus strain 17810R, of 726 aas, functions as a Cd2+:H+ antiporter, using both the pmf and ATP hydrolysis to drive Cd2+ expulsion (Tynecka et al. 2016).

Cross database links:

Gene Ontology

References (1)

External Searches:

Analyze:

3.A.3.6.1
Zn²⁺-, Cd²⁺-, Pb²⁺-ATPase (efflux). The enzyme from S. aureus strain 17810R, of 726 aas, functions as a Cd²⁺:H⁺ antiporter, using both the pmf and ATP hydrolysis to drive Cd²⁺ expulsion (Tynecka et al. 2016).