Probable cadmium-transporting ATPase - Listeria monocytogenes

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Q60048 (CADA2_LISMO) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 85. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Probable cadmium-transporting ATPase
EC=3.6.3.3

Alternative name(s):
Cadmium efflux ATPase

Gene names

Name:

cadA

Encoded on

Plasmid pLm74

Organism

Listeria monocytogenes

Taxonomic identifier

1639 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Listeriaceae › Listeria

Protein attributes

Sequence length	711 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	This electroneutral antiporter ejects one cadmium ion while accumulating two protons by an energy-dependent efflux mechanism.
Catalytic activity	ATP + H₂O + Cd²⁺(In) = ADP + phosphate + Cd²⁺(Out).
Subcellular location	Cell membrane; Multi-pass membrane protein.
Sequence similarities	Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IB subfamily. [View classification] Contains 1 HMA domain.

Ontologies

Keywords
Biological process	Antiport Cadmium resistance Ion transport Transport
Cellular component	Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Ligand	ATP-binding Cadmium Magnesium Metal-binding Nucleotide-binding
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	3D-structure Plasmid Transposable element
Gene Ontology (GO)
Biological process	ATP biosynthetic process Inferred from electronic annotation. Source: InterPro response to cadmium ion Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW antiporter activity Inferred from electronic annotation. Source: UniProtKB-KW cadmium-exporting ATPase activity Inferred from electronic annotation. Source: EC cation channel activity Inferred from electronic annotation. Source: InterPro copper-exporting ATPase activity Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 711

711

Probable cadmium-transporting ATPase

PRO_0000046247

Regions

Transmembrane

89 – 109

Helical; Potential

Transmembrane

111 – 131

Helical; Potential

Transmembrane

151 – 171

Helical; Potential

Transmembrane

317 – 337

Helical; Potential

Transmembrane

347 – 367

Helical; Potential

Transmembrane

669 – 689

Helical; Potential

Domain

4 – 67

HMA

Sites

Active site

398

4-aspartylphosphate intermediate Probable

Metal binding

Cadmium Potential

Metal binding

Cadmium Potential

Secondary structure

711

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

Q60048 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: C23BFEB7E20CFE9A
Show »

FASTA

711

77,089

        10         20         30         40         50         60 
MAEKTVYRVD GLSCTNCAAK FERNVKEIEG VTEAIVNFGA SKITVTGEAS IQQVEQAGAF 

        70         80         90        100        110        120 
EHLKIIPEKE SFTDPEHFTD HQSFIRKNWR LLLSGLFIAV GYASQIMNGE DFYLTNALFI 

       130        140        150        160        170        180 
FAIFIGGYSL FKEGFKNLLK FEFTMETLMT IAIIGAAFIG EWAEGSIVVI LFAVSEALER 

       190        200        210        220        230        240 
YSMDKARQSI RSLMDIAPKE ALVRRSGTDR MVHVDDIQIG DIMIIKPGQK IAMDGHVVKG 

       250        260        270        280        290        300 
YSAVNQAAIT GESIPVEKNI DDSVFAGTLN EEGLLEVAVT KRVEDTTISK IIHLVEEAQG 

       310        320        330        340        350        360 
ERAPAQAFVD TFAKYYTPAI IVIAALIATV PPLLFGGNWE TWVYQGLSVL VVGCPCALVV 

       370        380        390        400        410        420 
STPVAIVTAI GNAAKNGVLV KGGVYLEEIG GLKAIAFDKT GTLTKGVPVV TDYIELTEAT 

       430        440        450        460        470        480 
NIQHNKNYII MAALEQLSQH PLASAIIKYG ETREMDLTSI NVNDFTSITG KGIRGTVDGN 

       490        500        510        520        530        540 
TYYVGSPVLF KELLASQFTD SIHRQVSDLQ LKGKTAMLFG TNQKLISIVA VADEVRSSSQ 

       550        560        570        580        590        600 
HVIKRLHELG IEKTIMLTGD NQATAQAIGQ QVGVSEIEGE LMPQDKLDYI KQLKINFGKV 

       610        620        630        640        650        660 
AMVGDGINDA PALAAATVGI AMGGAGTDTA IETADVALMG DDLQKLPFTV KLSRKTLQII 

       670        680        690        700        710 
KQNITFSLVI KLIALLLVIP GWLTLWIAIM ADMGATLLVT LNGLRLMKVK D

« Hide

References

[1]	"Plasmid-borne cadmium resistance genes in Listeria monocytogenes are similar to cadA and cadC of Staphylococcus aureus and are induced by cadmium." Lebrun M., Audurier A., Cossart P. J. Bacteriol. 176:3040-3048(1994) [PubMed: 8188605] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: LM74.
[2]	"Plasmid-borne cadmium resistance genes in Listeria monocytogenes are present on Tn5422, a novel transposon closely related to Tn917." Lebrun M., Audurier A., Cossart P. J. Bacteriol. 176:3049-3061(1994) [PubMed: 8188606] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: LM74. Transposon: Tn5422.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L28104 Genomic DNA. Translation: AAA25275.1.

RefSeq

YP_003728018.1. NC_014255.1.
YP_003877857.1. NC_014495.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2AJ0	NMR	-	A	1-70	[»]
2AJ1	NMR	-	A	1-70	[»]

ProteinModelPortal

Q60048.

SMR

Q60048. Positions 1-71.

ModBase

Search...

Protein family/group databases

TCDB

3.A.3.6.8. P-type ATPase (P-ATPase) superfamily.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

9350447.
9728357.

Phylogenomic databases

ProtClustDB

CLSK793380.

Family and domain databases

InterPro

IPR008250. ATPase_P-typ_ATPase-assoc-dom.
IPR006403. ATPase_P-typ_cat/Cu-transptr.
IPR001366. ATPase_P-typ_Cd-transp.
IPR006404. ATPase_P-typ_Cd/Co/Hg/Pb/Zn.
IPR023300. ATPase_P-typ_cyto_domA.
IPR023299. ATPase_P-typ_cyto_domN.
IPR006416. ATPase_P-typ_heavy-metal.
IPR001757. ATPase_P-typ_ion-transptr.
IPR018303. ATPase_P-typ_P_site.
IPR005834. Dehalogen-like_hydro.
IPR023214. HAD-like_dom.
IPR017969. Heavy-metal-associated_CS.
IPR006121. HeavyMe-assoc_HMA.
[Graphical view]

Gene3D

G3DSA:2.70.150.10. ATPase_P-typ_cyto_domA. 1 hit.
G3DSA:3.40.1110.10. ATPase_P-typ_cyto_domN. 1 hit.
G3DSA:3.40.50.1000. HAD-like_dom. 2 hits.

Pfam

PF00122. E1-E2_ATPase. 1 hit.
PF00403. HMA. 1 hit.
PF00702. Hydrolase. 1 hit.
[Graphical view]

PRINTS

PR00119. CATATPASE.
PR00941. CDATPASE.

SUPFAM

SSF56784. HAD-like_dom. 1 hit.
SSF55008. HeavyMe_transpt. 1 hit.

TIGRFAMs

TIGR01511. ATPase-IB1_Cu. 1 hit.
TIGR01512. ATPase-IB2_Cd. 1 hit.
TIGR01525. ATPase-IB_hvy. 1 hit.
TIGR01494. ATPase_P-type. 1 hit.

PROSITE

PS00154. ATPASE_E1_E2. 1 hit.
PS01047. HMA_1. 1 hit.
PS50846. HMA_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

CADA2_LISMO

Accession

Primary (citable) accession number: Q60048

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	November 1, 1996
Last modified:	September 21, 2011
This is version 85 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents