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Q2G506

- ATM1_NOVAD

UniProt

Q2G506 - ATM1_NOVAD

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Protein

ATM1-type heavy metal exporter

Gene

atm1

Organism
Novosphingobium aromaticivorans (strain DSM 12444 / F199)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Mediates the ATP-dependent export of glutathione-conjugated substrates, such as heavy metal-glutathione conjugates. ATP hydrolysis is stimulated by glutathione binding. Protects cells against toxic heavy metal ions, such as silver and mercury ions. May also mediate the transport of glutathione-conjugated aromatic hydrocarbons, such as dinitrobenzene.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei319 – 3191Glutathione; via amide nitrogen
Binding sitei370 – 3701ATPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi394 – 40512ATPPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. ATPase activity, coupled to transmembrane movement of substances Source: InterPro
  2. ATP binding Source: UniProtKB-KW

GO - Biological processi

  1. ion transport Source: UniProtKB-KW
  2. response to mercury ion Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Ion transport, Mercuric resistance, Transport

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciNARO279238:GHBU-2695-MONOMER.

Protein family/group databases

TCDBi3.A.1.210.11. the atp-binding cassette (abc) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
ATM1-type heavy metal exporter
Alternative name(s):
ATP-binding cassette transporter Atm1
Short name:
NaAtm1
Gene namesi
Name:atm1
Ordered Locus Names:Saro_2631
OrganismiNovosphingobium aromaticivorans (strain DSM 12444 / F199)
Taxonomic identifieri279238 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaSphingomonadalesSphingomonadaceaeNovosphingobium
ProteomesiUP000009134: Chromosome

Subcellular locationi

Cell inner membrane 1 Publication; Multi-pass membrane protein 1 PublicationPROSITE-ProRule annotation

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 3838Cytoplasmic1 PublicationAdd
BLAST
Transmembranei39 – 6022HelicalAdd
BLAST
Topological domaini61 – 8222Periplasmic1 PublicationAdd
BLAST
Transmembranei83 – 10523HelicalAdd
BLAST
Topological domaini106 – 15449Cytoplasmic1 PublicationAdd
BLAST
Transmembranei155 – 17824HelicalAdd
BLAST
Topological domaini179 – 1791Periplasmic1 Publication
Transmembranei180 – 20223HelicalAdd
BLAST
Topological domaini203 – 26664Cytoplasmic1 PublicationAdd
BLAST
Transmembranei267 – 28519HelicalAdd
BLAST
Topological domaini286 – 30015Periplasmic1 PublicationAdd
BLAST
Transmembranei301 – 32222HelicalAdd
BLAST
Topological domaini323 – 608286Cytoplasmic1 PublicationAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi195 – 1951Y → F: Strongly increases basal rate of ATP hydrolysis. 1 Publication
Mutagenesisi269 – 2691N → A: Increases basal rate of ATP hydrolysis and abolishes stimulation of ATP hydrolysis by glutathione. 1 Publication
Mutagenesisi272 – 2721Q → A: Abolishes glutathione-dependent ATP hydrolysis. 1 Publication
Mutagenesisi319 – 3191G → L: Abolishes glutathione-dependent ATP hydrolysis. 1 Publication
Mutagenesisi523 – 5231E → Q: Abolishes transporter activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 608608ATM1-type heavy metal exporterPRO_0000429375Add
BLAST

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi279238.Saro_2631.

Structurei

Secondary structure

1
608
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi10 – 123Combined sources
Helixi16 – 2712Combined sources
Helixi34 – 6835Combined sources
Turni70 – 723Combined sources
Beta strandi73 – 753Combined sources
Helixi76 – 12651Combined sources
Helixi129 – 1313Combined sources
Helixi137 – 16024Combined sources
Helixi162 – 17918Combined sources
Helixi183 – 22947Combined sources
Helixi231 – 2366Combined sources
Helixi240 – 29253Combined sources
Helixi299 – 31214Combined sources
Helixi314 – 3174Combined sources
Helixi318 – 34023Combined sources
Beta strandi361 – 3688Combined sources
Beta strandi377 – 3848Combined sources
Beta strandi389 – 3935Combined sources
Helixi400 – 4023Combined sources
Helixi403 – 4075Combined sources
Beta strandi414 – 4207Combined sources
Helixi425 – 4273Combined sources
Helixi430 – 4356Combined sources
Beta strandi437 – 4437Combined sources
Beta strandi448 – 4503Combined sources
Helixi451 – 4566Combined sources
Helixi464 – 47310Combined sources
Helixi477 – 4815Combined sources
Beta strandi483 – 4853Combined sources
Helixi486 – 4883Combined sources
Beta strandi490 – 4923Combined sources
Helixi500 – 51415Combined sources
Beta strandi517 – 5237Combined sources
Turni524 – 5274Combined sources
Helixi530 – 54314Combined sources
Turni544 – 5463Combined sources
Beta strandi547 – 5526Combined sources
Helixi556 – 5594Combined sources
Beta strandi563 – 5697Combined sources
Beta strandi572 – 5776Combined sources
Helixi579 – 5857Combined sources
Helixi588 – 60518Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4MRNX-ray2.50A/B1-608[»]
4MRPX-ray2.50A/B1-608[»]
4MRRX-ray2.97A/B1-608[»]
4MRSX-ray2.35A/B1-608[»]
4MRVX-ray2.50A/B1-608[»]
ProteinModelPortaliQ2G506.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini39 – 327289ABC transmembrane type-1PROSITE-ProRule annotationAdd
BLAST
Domaini361 – 595235ABC transporterPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni206 – 2105Glutathione binding
Regioni269 – 2724Glutathione binding

Sequence similaritiesi

Contains 1 ABC transmembrane type-1 domain.PROSITE-ProRule annotation
Contains 1 ABC transporter domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG5265.
KOiK06147.
OMAiFLPYLWP.
OrthoDBiEOG6T7N3V.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR011527. ABC1_TM_dom.
IPR003439. ABC_transporter-like.
IPR017871. ABC_transporter_CS.
IPR001140. ABC_transptr_TM_dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00664. ABC_membrane. 1 hit.
PF00005. ABC_tran. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
SSF90123. SSF90123. 1 hit.
PROSITEiPS50929. ABC_TM1F. 1 hit.
PS00211. ABC_TRANSPORTER_1. 1 hit.
PS50893. ABC_TRANSPORTER_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q2G506-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPPETATNPK DARHDGWQTL KRFLPYLWPA DNAVLRRRVV GAILMVLLGK
60 70 80 90 100
ATTLALPFAY KKAVDAMTLG GGAQPALTVA LAFVLAYALG RFSGVLFDNL
110 120 130 140 150
RNIVFERVGQ DATRHLAENV FARLHKLSLR FHLARRTGEV TKVIERGTKS
160 170 180 190 200
IDTMLYFLLF NIAPTVIELT AVIVIFWLNF GLGLVTATIL AVIAYVWTTR
210 220 230 240 250
TITEWRTHLR EKMNRLDGQA LARAVDSLLN YETVKYFGAE SREEARYASA
260 270 280 290 300
ARAYADAAVK SENSLGLLNI AQALIVNLLM AGAMAWTVYG WSQGKLTVGD
310 320 330 340 350
LVFVNTYLTQ LFRPLDMLGM VYRTIRQGLI DMAEMFRLID THIEVADVPN
360 370 380 390 400
APALVVNRPS VTFDNVVFGY DRDREILHGL SFEVAAGSRV AIVGPSGAGK
410 420 430 440 450
STIARLLFRF YDPWEGRILI DGQDIAHVTQ TSLRAALGIV PQDSVLFNDT
460 470 480 490 500
IGYNIAYGRD GASRAEVDAA AKGAAIADFI ARLPQGYDTE VGERGLKLSG
510 520 530 540 550
GEKQRVAIAR TLVKNPPILL FDEATSALDT RTEQDILSTM RAVASHRTTI
560 570 580 590 600
SIAHRLSTIA DSDTILVLDQ GRLAEQGSHL DLLRRDGLYA EMWARQAAES

AEVSEAAE
Length:608
Mass (Da):66,867
Last modified:March 21, 2006 - v1
Checksum:iC6D669186EFC501E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000248 Genomic DNA. Translation: ABD27067.1.
RefSeqiWP_011446273.1. NC_007794.1.
YP_497901.1. NC_007794.1.

Genome annotation databases

EnsemblBacteriaiABD27067; ABD27067; Saro_2631.
GeneIDi3917064.
KEGGinar:Saro_2631.
PATRICi22788070. VBINovAro50627_2694.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000248 Genomic DNA. Translation: ABD27067.1 .
RefSeqi WP_011446273.1. NC_007794.1.
YP_497901.1. NC_007794.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4MRN X-ray 2.50 A/B 1-608 [» ]
4MRP X-ray 2.50 A/B 1-608 [» ]
4MRR X-ray 2.97 A/B 1-608 [» ]
4MRS X-ray 2.35 A/B 1-608 [» ]
4MRV X-ray 2.50 A/B 1-608 [» ]
ProteinModelPortali Q2G506.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 279238.Saro_2631.

Protein family/group databases

TCDBi 3.A.1.210.11. the atp-binding cassette (abc) superfamily.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABD27067 ; ABD27067 ; Saro_2631 .
GeneIDi 3917064.
KEGGi nar:Saro_2631.
PATRICi 22788070. VBINovAro50627_2694.

Phylogenomic databases

eggNOGi COG5265.
KOi K06147.
OMAi FLPYLWP.
OrthoDBi EOG6T7N3V.

Enzyme and pathway databases

BioCyci NARO279238:GHBU-2695-MONOMER.

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
InterProi IPR003593. AAA+_ATPase.
IPR011527. ABC1_TM_dom.
IPR003439. ABC_transporter-like.
IPR017871. ABC_transporter_CS.
IPR001140. ABC_transptr_TM_dom.
IPR027417. P-loop_NTPase.
[Graphical view ]
Pfami PF00664. ABC_membrane. 1 hit.
PF00005. ABC_tran. 1 hit.
[Graphical view ]
SMARTi SM00382. AAA. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
SSF90123. SSF90123. 1 hit.
PROSITEi PS50929. ABC_TM1F. 1 hit.
PS00211. ABC_TRANSPORTER_1. 1 hit.
PS50893. ABC_TRANSPORTER_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 12444 / F199.
  2. "Structural basis for heavy metal detoxification by an Atm1-type ABC exporter."
    Lee J.Y., Yang J.G., Zhitnitsky D., Lewinson O., Rees D.C.
    Science 343:1133-1136(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) IN COMPLEXES WITH GLUTATHIONE AND PHOSPHATE, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, TOPOLOGY, MUTAGENESIS OF TYR-195; ASN-269; GLN-272; GLY-319 AND GLU-523.
    Strain: DSM 12444 / F199.

Entry informationi

Entry nameiATM1_NOVAD
AccessioniPrimary (citable) accession number: Q2G506
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 11, 2014
Last sequence update: March 21, 2006
Last modified: November 26, 2014
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3