ATM1_NOVAD
ID ATM1_NOVAD Reviewed; 608 AA.
AC Q2G506;
DT 11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=ATM1-type heavy metal exporter {ECO:0000305};
DE EC=7.-.-.- {ECO:0000269|PubMed:24604198};
DE AltName: Full=ATP-binding cassette transporter Atm1 {ECO:0000305};
DE Short=NaAtm1 {ECO:0000303|PubMed:24604198};
GN Name=atm1; OrderedLocusNames=Saro_2631;
OS Novosphingobium aromaticivorans (strain ATCC 700278 / DSM 12444 / CCUG
OS 56034 / CIP 105152 / NBRC 16084 / F199).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=279238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700278 / DSM 12444 / CCUG 56034 / CIP 105152 / NBRC 16084 /
RC F199;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N.,
RA Fredrickson J., Balkwill D., Romine M.F., Richardson P.;
RT "Complete sequence of Novosphingobium aromaticivorans DSM 12444.";
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) IN COMPLEXES WITH GLUTATHIONE AND
RP PHOSPHATE, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, TOPOLOGY, AND
RP MUTAGENESIS OF TYR-195; ASN-269; GLN-272; GLY-319 AND GLU-523.
RC STRAIN=ATCC 700278 / DSM 12444 / CCUG 56034 / CIP 105152 / NBRC 16084 /
RC F199;
RX PubMed=24604198; DOI=10.1126/science.1246489;
RA Lee J.Y., Yang J.G., Zhitnitsky D., Lewinson O., Rees D.C.;
RT "Structural basis for heavy metal detoxification by an Atm1-type ABC
RT exporter.";
RL Science 343:1133-1136(2014).
CC -!- FUNCTION: Mediates the ATP-dependent export of glutathione-conjugated
CC substrates, such as heavy metal-glutathione conjugates. ATP hydrolysis
CC is stimulated by glutathione binding. Protects cells against toxic
CC heavy metal ions, such as silver and mercury ions. May also mediate the
CC transport of glutathione-conjugated aromatic hydrocarbons, such as
CC dinitrobenzene. {ECO:0000269|PubMed:24604198}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:24604198}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:24604198}; Multi-pass membrane protein
CC {ECO:0000255|PROSITE-ProRule:PRU00441, ECO:0000269|PubMed:24604198}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB family.
CC Heavy Metal importer (TC 3.A.1.210) subfamily. {ECO:0000305}.
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DR EMBL; CP000248; ABD27067.1; -; Genomic_DNA.
DR RefSeq; WP_011446273.1; NC_007794.1.
DR PDB; 4MRN; X-ray; 2.50 A; A/B=1-608.
DR PDB; 4MRP; X-ray; 2.50 A; A/B=1-608.
DR PDB; 4MRR; X-ray; 2.97 A; A/B=1-608.
DR PDB; 4MRS; X-ray; 2.35 A; A/B=1-608.
DR PDB; 4MRV; X-ray; 2.50 A; A/B=1-608.
DR PDB; 6PAM; X-ray; 3.70 A; A/B/C/D/E/F/G/H=1-608.
DR PDB; 6PAN; X-ray; 3.40 A; A/B=1-608.
DR PDB; 6PAO; X-ray; 3.65 A; A/B=1-608.
DR PDB; 6PAQ; X-ray; 3.30 A; A/B=1-608.
DR PDB; 6PAR; X-ray; 3.35 A; A/B/C/D/E/F=1-608.
DR PDB; 6VQT; EM; 3.03 A; A/B=1-608.
DR PDB; 6VQU; EM; 3.88 A; A/B=1-608.
DR PDBsum; 4MRN; -.
DR PDBsum; 4MRP; -.
DR PDBsum; 4MRR; -.
DR PDBsum; 4MRS; -.
DR PDBsum; 4MRV; -.
DR PDBsum; 6PAM; -.
DR PDBsum; 6PAN; -.
DR PDBsum; 6PAO; -.
DR PDBsum; 6PAQ; -.
DR PDBsum; 6PAR; -.
DR PDBsum; 6VQT; -.
DR PDBsum; 6VQU; -.
DR AlphaFoldDB; Q2G506; -.
DR SMR; Q2G506; -.
DR DIP; DIP-61368N; -.
DR STRING; 279238.Saro_2631; -.
DR TCDB; 3.A.1.210.11; the atp-binding cassette (abc) superfamily.
DR EnsemblBacteria; ABD27067; ABD27067; Saro_2631.
DR KEGG; nar:Saro_2631; -.
DR eggNOG; COG5265; Bacteria.
DR HOGENOM; CLU_000604_84_1_5; -.
DR OMA; VTEWRTH; -.
DR OrthoDB; 643917at2; -.
DR PRO; PR:Q2G506; -.
DR Proteomes; UP000009134; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR GO; GO:0046689; P:response to mercury ion; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1560.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
DR InterPro; IPR036640; ABC1_TM_sf.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039421; Type_1_exporter.
DR PANTHER; PTHR24221; PTHR24221; 1.
DR Pfam; PF00664; ABC_membrane; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF90123; SSF90123; 1.
DR PROSITE; PS50929; ABC_TM1F; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell inner membrane; Cell membrane;
KW Ion transport; Membrane; Mercuric resistance; Nucleotide-binding;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..608
FT /note="ATM1-type heavy metal exporter"
FT /id="PRO_0000429375"
FT TOPO_DOM 1..38
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:24604198"
FT TRANSMEM 39..60
FT /note="Helical"
FT TOPO_DOM 61..82
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:24604198"
FT TRANSMEM 83..105
FT /note="Helical"
FT TOPO_DOM 106..154
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:24604198"
FT TRANSMEM 155..178
FT /note="Helical"
FT TOPO_DOM 179
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:24604198"
FT TRANSMEM 180..202
FT /note="Helical"
FT TOPO_DOM 203..266
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:24604198"
FT TRANSMEM 267..285
FT /note="Helical"
FT TOPO_DOM 286..300
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:24604198"
FT TRANSMEM 301..322
FT /note="Helical"
FT TOPO_DOM 323..608
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:24604198"
FT DOMAIN 39..327
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 361..595
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 206..210
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT BINDING 269..272
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:24604198,
FT ECO:0007744|PDB:4MRP"
FT BINDING 316..319
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:24604198,
FT ECO:0007744|PDB:4MRP"
FT BINDING 370
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9NP58"
FT BINDING 394..405
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT MUTAGEN 195
FT /note="Y->F: Strongly increases basal rate of ATP
FT hydrolysis."
FT /evidence="ECO:0000269|PubMed:24604198"
FT MUTAGEN 269
FT /note="N->A: Increases basal rate of ATP hydrolysis and
FT abolishes stimulation of ATP hydrolysis by glutathione."
FT /evidence="ECO:0000269|PubMed:24604198"
FT MUTAGEN 272
FT /note="Q->A: Abolishes glutathione-dependent ATP
FT hydrolysis."
FT /evidence="ECO:0000269|PubMed:24604198"
FT MUTAGEN 319
FT /note="G->L: Abolishes glutathione-dependent ATP
FT hydrolysis."
FT /evidence="ECO:0000269|PubMed:24604198"
FT MUTAGEN 523
FT /note="E->Q: Abolishes transporter activity."
FT /evidence="ECO:0000269|PubMed:24604198"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:4MRS"
FT HELIX 16..27
FT /evidence="ECO:0007829|PDB:4MRS"
FT HELIX 28..32
FT /evidence="ECO:0007829|PDB:6PAR"
FT HELIX 34..68
FT /evidence="ECO:0007829|PDB:4MRS"
FT TURN 70..72
FT /evidence="ECO:0007829|PDB:4MRN"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:4MRN"
FT HELIX 76..126
FT /evidence="ECO:0007829|PDB:4MRS"
FT HELIX 129..131
FT /evidence="ECO:0007829|PDB:4MRS"
FT HELIX 137..160
FT /evidence="ECO:0007829|PDB:4MRS"
FT HELIX 162..179
FT /evidence="ECO:0007829|PDB:4MRS"
FT HELIX 183..229
FT /evidence="ECO:0007829|PDB:4MRS"
FT HELIX 231..236
FT /evidence="ECO:0007829|PDB:4MRS"
FT HELIX 240..292
FT /evidence="ECO:0007829|PDB:4MRS"
FT STRAND 295..297
FT /evidence="ECO:0007829|PDB:6PAQ"
FT HELIX 299..312
FT /evidence="ECO:0007829|PDB:4MRS"
FT HELIX 314..317
FT /evidence="ECO:0007829|PDB:4MRS"
FT HELIX 318..340
FT /evidence="ECO:0007829|PDB:4MRS"
FT STRAND 361..368
FT /evidence="ECO:0007829|PDB:4MRS"
FT STRAND 377..384
FT /evidence="ECO:0007829|PDB:4MRS"
FT STRAND 389..393
FT /evidence="ECO:0007829|PDB:4MRS"
FT HELIX 400..402
FT /evidence="ECO:0007829|PDB:4MRS"
FT HELIX 403..407
FT /evidence="ECO:0007829|PDB:4MRS"
FT STRAND 414..420
FT /evidence="ECO:0007829|PDB:4MRS"
FT HELIX 425..427
FT /evidence="ECO:0007829|PDB:4MRS"
FT HELIX 430..435
FT /evidence="ECO:0007829|PDB:4MRS"
FT STRAND 437..443
FT /evidence="ECO:0007829|PDB:4MRS"
FT STRAND 448..450
FT /evidence="ECO:0007829|PDB:4MRS"
FT HELIX 451..456
FT /evidence="ECO:0007829|PDB:4MRS"
FT HELIX 464..473
FT /evidence="ECO:0007829|PDB:4MRS"
FT HELIX 477..481
FT /evidence="ECO:0007829|PDB:4MRS"
FT STRAND 483..485
FT /evidence="ECO:0007829|PDB:4MRR"
FT HELIX 486..488
FT /evidence="ECO:0007829|PDB:4MRS"
FT STRAND 490..492
FT /evidence="ECO:0007829|PDB:4MRS"
FT HELIX 493..495
FT /evidence="ECO:0007829|PDB:6VQT"
FT HELIX 500..514
FT /evidence="ECO:0007829|PDB:4MRS"
FT STRAND 517..523
FT /evidence="ECO:0007829|PDB:4MRS"
FT TURN 524..527
FT /evidence="ECO:0007829|PDB:4MRS"
FT HELIX 530..543
FT /evidence="ECO:0007829|PDB:4MRS"
FT TURN 544..546
FT /evidence="ECO:0007829|PDB:4MRS"
FT STRAND 547..552
FT /evidence="ECO:0007829|PDB:4MRS"
FT HELIX 556..559
FT /evidence="ECO:0007829|PDB:4MRS"
FT STRAND 563..569
FT /evidence="ECO:0007829|PDB:4MRS"
FT STRAND 572..577
FT /evidence="ECO:0007829|PDB:4MRS"
FT HELIX 579..585
FT /evidence="ECO:0007829|PDB:4MRS"
FT HELIX 588..605
FT /evidence="ECO:0007829|PDB:4MRS"
SQ SEQUENCE 608 AA; 66867 MW; C6D669186EFC501E CRC64;
MPPETATNPK DARHDGWQTL KRFLPYLWPA DNAVLRRRVV GAILMVLLGK ATTLALPFAY
KKAVDAMTLG GGAQPALTVA LAFVLAYALG RFSGVLFDNL RNIVFERVGQ DATRHLAENV
FARLHKLSLR FHLARRTGEV TKVIERGTKS IDTMLYFLLF NIAPTVIELT AVIVIFWLNF
GLGLVTATIL AVIAYVWTTR TITEWRTHLR EKMNRLDGQA LARAVDSLLN YETVKYFGAE
SREEARYASA ARAYADAAVK SENSLGLLNI AQALIVNLLM AGAMAWTVYG WSQGKLTVGD
LVFVNTYLTQ LFRPLDMLGM VYRTIRQGLI DMAEMFRLID THIEVADVPN APALVVNRPS
VTFDNVVFGY DRDREILHGL SFEVAAGSRV AIVGPSGAGK STIARLLFRF YDPWEGRILI
DGQDIAHVTQ TSLRAALGIV PQDSVLFNDT IGYNIAYGRD GASRAEVDAA AKGAAIADFI
ARLPQGYDTE VGERGLKLSG GEKQRVAIAR TLVKNPPILL FDEATSALDT RTEQDILSTM
RAVASHRTTI SIAHRLSTIA DSDTILVLDQ GRLAEQGSHL DLLRRDGLYA EMWARQAAES
AEVSEAAE
