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ATM1-type heavy metal exporter (ATP-binding cassette transporter Atm1) (NaAtm1)

 ATM1_NOVAD              Reviewed;         608 AA.
Q2G506;
11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
21-MAR-2006, sequence version 1.
28-FEB-2018, entry version 87.
RecName: Full=ATM1-type heavy metal exporter;
AltName: Full=ATP-binding cassette transporter Atm1;
Short=NaAtm1;
Name=atm1; OrderedLocusNames=Saro_2631;
Novosphingobium aromaticivorans (strain ATCC 700278 / DSM 12444 / CIP
105152 / NBRC 16084 / F199).
Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
Sphingomonadaceae; Novosphingobium.
NCBI_TaxID=279238;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 700278 / DSM 12444 / CIP 105152 / NBRC 16084 / F199;
US DOE Joint Genome Institute;
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N.,
Fredrickson J., Balkwill D., Romine M.F., Richardson P.;
"Complete sequence of Novosphingobium aromaticivorans DSM 12444.";
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
[2]
X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) IN COMPLEXES WITH GLUTATHIONE
AND PHOSPHATE, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, TOPOLOGY, AND
MUTAGENESIS OF TYR-195; ASN-269; GLN-272; GLY-319 AND GLU-523.
STRAIN=ATCC 700278 / DSM 12444 / CIP 105152 / NBRC 16084 / F199;
PubMed=24604198; DOI=10.1126/science.1246489;
Lee J.Y., Yang J.G., Zhitnitsky D., Lewinson O., Rees D.C.;
"Structural basis for heavy metal detoxification by an Atm1-type ABC
exporter.";
Science 343:1133-1136(2014).
-!- FUNCTION: 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.
{ECO:0000269|PubMed:24604198}.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:24604198}.
-!- SUBCELLULAR LOCATION: Cell inner membrane
{ECO:0000269|PubMed:24604198}; Multi-pass membrane protein
{ECO:0000255|PROSITE-ProRule:PRU00441,
ECO:0000269|PubMed:24604198}.
-!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB
family. Heavy Metal importer (TC 3.A.1.210) subfamily.
{ECO:0000305}.
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EMBL; CP000248; ABD27067.1; -; Genomic_DNA.
RefSeq; WP_011446273.1; NC_007794.1.
PDB; 4MRN; X-ray; 2.50 A; A/B=1-608.
PDB; 4MRP; X-ray; 2.50 A; A/B=1-608.
PDB; 4MRR; X-ray; 2.97 A; A/B=1-608.
PDB; 4MRS; X-ray; 2.35 A; A/B=1-608.
PDB; 4MRV; X-ray; 2.50 A; A/B=1-608.
PDBsum; 4MRN; -.
PDBsum; 4MRP; -.
PDBsum; 4MRR; -.
PDBsum; 4MRS; -.
PDBsum; 4MRV; -.
ProteinModelPortal; Q2G506; -.
SMR; Q2G506; -.
DIP; DIP-61368N; -.
STRING; 279238.Saro_2631; -.
TCDB; 3.A.1.210.11; the atp-binding cassette (abc) superfamily.
EnsemblBacteria; ABD27067; ABD27067; Saro_2631.
KEGG; nar:Saro_2631; -.
eggNOG; ENOG4108JJ7; Bacteria.
eggNOG; COG5265; LUCA.
KO; K06147; -.
OMA; YEAQRYD; -.
OrthoDB; POG091H00DB; -.
BioCyc; NARO279238:G1G5T-2692-MONOMER; -.
PRO; PR:Q2G506; -.
Proteomes; UP000009134; Chromosome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0042626; F:ATPase activity, coupled to transmembrane movement of substances; IEA:InterPro.
GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
GO; GO:0046689; P:response to mercury ion; IEA:UniProtKB-KW.
Gene3D; 1.20.1560.10; -; 1.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR011527; ABC1_TM_dom.
InterPro; IPR036640; ABC1_TM_sf.
InterPro; IPR003439; ABC_transporter-like.
InterPro; IPR017871; ABC_transporter_CS.
InterPro; IPR027417; P-loop_NTPase.
Pfam; PF00664; ABC_membrane; 1.
Pfam; PF00005; ABC_tran; 1.
SMART; SM00382; AAA; 1.
SUPFAM; SSF52540; SSF52540; 1.
SUPFAM; SSF90123; SSF90123; 1.
PROSITE; PS50929; ABC_TM1F; 1.
PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Cell inner membrane; Cell membrane;
Complete proteome; Ion transport; Membrane; Mercuric resistance;
Nucleotide-binding; Reference proteome; Transmembrane;
Transmembrane helix; Transport.
CHAIN 1 608 ATM1-type heavy metal exporter.
/FTId=PRO_0000429375.
TOPO_DOM 1 38 Cytoplasmic.
{ECO:0000269|PubMed:24604198}.
TRANSMEM 39 60 Helical.
TOPO_DOM 61 82 Periplasmic.
{ECO:0000269|PubMed:24604198}.
TRANSMEM 83 105 Helical.
TOPO_DOM 106 154 Cytoplasmic.
{ECO:0000269|PubMed:24604198}.
TRANSMEM 155 178 Helical.
TOPO_DOM 179 179 Periplasmic.
{ECO:0000269|PubMed:24604198}.
TRANSMEM 180 202 Helical.
TOPO_DOM 203 266 Cytoplasmic.
{ECO:0000269|PubMed:24604198}.
TRANSMEM 267 285 Helical.
TOPO_DOM 286 300 Periplasmic.
{ECO:0000269|PubMed:24604198}.
TRANSMEM 301 322 Helical.
TOPO_DOM 323 608 Cytoplasmic.
{ECO:0000269|PubMed:24604198}.
DOMAIN 39 327 ABC transmembrane type-1.
{ECO:0000255|PROSITE-ProRule:PRU00441}.
DOMAIN 361 595 ABC transporter. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
NP_BIND 394 405 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
REGION 206 210 Glutathione binding.
REGION 269 272 Glutathione binding.
BINDING 319 319 Glutathione; via amide nitrogen.
BINDING 370 370 ATP. {ECO:0000250}.
MUTAGEN 195 195 Y->F: Strongly increases basal rate of
ATP hydrolysis.
{ECO:0000269|PubMed:24604198}.
MUTAGEN 269 269 N->A: Increases basal rate of ATP
hydrolysis and abolishes stimulation of
ATP hydrolysis by glutathione.
{ECO:0000269|PubMed:24604198}.
MUTAGEN 272 272 Q->A: Abolishes glutathione-dependent ATP
hydrolysis.
{ECO:0000269|PubMed:24604198}.
MUTAGEN 319 319 G->L: Abolishes glutathione-dependent ATP
hydrolysis.
{ECO:0000269|PubMed:24604198}.
MUTAGEN 523 523 E->Q: Abolishes transporter activity.
{ECO:0000269|PubMed:24604198}.
STRAND 10 12 {ECO:0000244|PDB:4MRS}.
HELIX 16 27 {ECO:0000244|PDB:4MRS}.
HELIX 34 68 {ECO:0000244|PDB:4MRS}.
TURN 70 72 {ECO:0000244|PDB:4MRN}.
STRAND 73 75 {ECO:0000244|PDB:4MRN}.
HELIX 76 126 {ECO:0000244|PDB:4MRS}.
HELIX 129 131 {ECO:0000244|PDB:4MRS}.
HELIX 137 160 {ECO:0000244|PDB:4MRS}.
HELIX 162 179 {ECO:0000244|PDB:4MRS}.
HELIX 183 229 {ECO:0000244|PDB:4MRS}.
HELIX 231 236 {ECO:0000244|PDB:4MRS}.
HELIX 240 292 {ECO:0000244|PDB:4MRS}.
HELIX 299 312 {ECO:0000244|PDB:4MRS}.
HELIX 314 317 {ECO:0000244|PDB:4MRS}.
HELIX 318 340 {ECO:0000244|PDB:4MRS}.
STRAND 361 368 {ECO:0000244|PDB:4MRS}.
STRAND 377 384 {ECO:0000244|PDB:4MRS}.
STRAND 389 393 {ECO:0000244|PDB:4MRS}.
HELIX 400 402 {ECO:0000244|PDB:4MRS}.
HELIX 403 407 {ECO:0000244|PDB:4MRS}.
STRAND 414 420 {ECO:0000244|PDB:4MRS}.
HELIX 425 427 {ECO:0000244|PDB:4MRS}.
HELIX 430 435 {ECO:0000244|PDB:4MRS}.
STRAND 437 443 {ECO:0000244|PDB:4MRS}.
STRAND 448 450 {ECO:0000244|PDB:4MRS}.
HELIX 451 456 {ECO:0000244|PDB:4MRS}.
HELIX 464 473 {ECO:0000244|PDB:4MRS}.
HELIX 477 481 {ECO:0000244|PDB:4MRS}.
STRAND 483 485 {ECO:0000244|PDB:4MRR}.
HELIX 486 488 {ECO:0000244|PDB:4MRS}.
STRAND 490 492 {ECO:0000244|PDB:4MRS}.
HELIX 500 514 {ECO:0000244|PDB:4MRS}.
STRAND 517 523 {ECO:0000244|PDB:4MRS}.
TURN 524 527 {ECO:0000244|PDB:4MRS}.
HELIX 530 543 {ECO:0000244|PDB:4MRS}.
TURN 544 546 {ECO:0000244|PDB:4MRS}.
STRAND 547 552 {ECO:0000244|PDB:4MRS}.
HELIX 556 559 {ECO:0000244|PDB:4MRS}.
STRAND 563 569 {ECO:0000244|PDB:4MRS}.
STRAND 572 577 {ECO:0000244|PDB:4MRS}.
HELIX 579 585 {ECO:0000244|PDB:4MRS}.
HELIX 588 605 {ECO:0000244|PDB:4MRS}.
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


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