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   27-MAR-2024, entry version 110.
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; Pseudomonadota; 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   EMDB; EMD-21356; -.
DR   EMDB; EMD-21357; -.
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   KEGG; nar:Saro_2631; -.
DR   eggNOG; COG5265; Bacteria.
DR   HOGENOM; CLU_000604_84_1_5; -.
DR   PRO; PR:Q2G506; -.
DR   Proteomes; UP000009134; Chromosome.
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:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0006811; P:monoatomic ion transport; IEA:UniProtKB-KW.
DR   GO; GO:0046689; P:response to mercury ion; IEA:UniProtKB-KW.
DR   CDD; cd18582; ABC_6TM_ATM1_ABCB7; 1.
DR   Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; ATP-BINDING CASSETTE SUB-FAMILY B; 1.
DR   PANTHER; PTHR24221:SF644; OS07G0464600 PROTEIN; 1.
DR   Pfam; PF00664; ABC_membrane; 1.
DR   Pfam; PF00005; ABC_tran; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF90123; ABC transporter transmembrane region; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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
//