ATM1_KLULA
ID ATM1_KLULA Reviewed; 720 AA.
AC Q6CX96;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Iron-sulfur clusters transporter ATM1, mitochondrial {ECO:0000305};
DE EC=7.-.-.- {ECO:0000250|UniProtKB:Q2G506};
DE Flags: Precursor;
GN Name=ATM1 {ECO:0000305}; OrderedLocusNames=KLLA0A10131g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Performs an essential function in the generation of
CC cytoplasmic iron-sulfur proteins by mediating the ATP-dependent export
CC of Fe/S cluster precursors synthesized by NFS1 and other mitochondrial
CC proteins (By similarity). Hydrolyzes ATP (By similarity). Binds
CC glutathione and may function by transporting a glutathione-conjugated
CC iron-sulfur compound (By similarity). {ECO:0000250|UniProtKB:P40416}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P40416}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P40416}; Multi-pass membrane protein
CC {ECO:0000255|PROSITE-ProRule:PRU00441}.
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; CR382121; CAH03031.1; -; Genomic_DNA.
DR RefSeq; XP_451443.1; XM_451443.1.
DR AlphaFoldDB; Q6CX96; -.
DR SMR; Q6CX96; -.
DR STRING; 28985.XP_451443.1; -.
DR EnsemblFungi; CAH03031; CAH03031; KLLA0_A10131g.
DR GeneID; 2896392; -.
DR KEGG; kla:KLLA0_A10131g; -.
DR eggNOG; KOG0057; Eukaryota.
DR HOGENOM; CLU_000604_84_1_1; -.
DR InParanoid; Q6CX96; -.
DR OMA; VTEWRTH; -.
DR Proteomes; UP000000598; Chromosome A.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner 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:EnsemblFungi.
DR GO; GO:0055072; P:iron ion homeostasis; IEA:UniProtKB-KW.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:EnsemblFungi.
DR GO; GO:0140466; P:iron-sulfur cluster export from the mitochondrion; IEA:EnsemblFungi.
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 3: Inferred from homology;
KW ATP-binding; Ion transport; Iron; Iron transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Nucleotide-binding; Reference proteome;
KW Transit peptide; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT TRANSIT 1..36
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 37..720
FT /note="Iron-sulfur clusters transporter ATM1,
FT mitochondrial"
FT /id="PRO_0000255447"
FT TOPO_DOM 37..129
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT TRANSMEM 130..151
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 152..175
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT TRANSMEM 176..199
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 200..248
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT TRANSMEM 249..272
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 273
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT TRANSMEM 274..294
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 295..360
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT TRANSMEM 361..379
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 380..394
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT TRANSMEM 395..416
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 417..720
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT DOMAIN 130..421
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 456..692
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 64..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..79
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 300..304
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT BINDING 363..366
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT BINDING 413
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:Q2G506"
FT BINDING 465
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9NP58"
FT BINDING 489..500
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 720 AA; 80495 MW; 66636028469AC4AE CRC64;
MIMFRSLSVT PVWKAGLSLS HRSIPINSRL SSVRNYISIG CANKTGSRLL RSAGVSSQYK
DFRRFNSSSN GNGTDKNASV APKTEVKKIV PPKPSTNGKS KTPTISELRI MKDLFKYIWP
SGDNKVKIRV LIALALLIGA KLLNVQVPFF FKQTIDSMNI EWGPDVATVL PVAITMTILS
YGAARFGAVM FGELRNAVFA KVAQNAIRKV SLQTFQHLMK LDLGWHLSRQ TGGLTRAMDR
GTKGISYVLS AMVFHMIPIT FEISVVCGIL TYQFGSSFAA MTFVTMLLYS FFTFKTTAWR
TEFRRSANRA DNKAASVALD SLINFEAVKY FNNEEYLANK YHQSLSKYRD SQIKVAQSLA
FLNAGQNFIF TSALTAMMYM GASGVMEGAL TVGDLVLINQ LVFQLSVPLN FLGSVYRELK
QSLIDMESLF KLQKNPILIK NTERPLMLPE HLPCEIKFEN VTFGYQPDRN ILKNATFTIA
PGKKTAIVGP SGSGKSTILR LVFRFYDPQQ GRILLDGKDI RELDLDELRR IVGVVPQDTP
LFNDTIWENV KFGRINATDN EIVTAIEKAQ LSDLIHKLPK GTETIVGERG LMISGGEKQR
LAIARVLLKD TPIMFFDEAT SALDTHTEQS LLKTIKENFS DVAKTSVYIA HRLRTIADAD
KIIVLENGAV REEGTHNALL ANPNSLYSEL WNIQENLDML EDELEDELKL EKEPRTSKKD
