ID   C5DDA0_LACTC            Unreviewed;       694 AA.
AC   C5DDA0;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   02-SEP-2026, entry version 91.
DE   RecName: Full=Iron-sulfur clusters transporter ATM1, mitochondrial {ECO:0000256|ARBA:ARBA00039906};
DE   AltName: Full=Iron-sulfur clusters transporter atm1, mitochondrial {ECO:0000256|ARBA:ARBA00040792};
GN   OrderedLocusNames=KLTH0B09482g {ECO:0000313|EMBL:CAR21761.1};
OS   Lachancea thermotolerans (strain ATCC 56472 / CBS 6340 / NRRL Y-8284)
OS   (Yeast) (Kluyveromyces thermotolerans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=559295 {ECO:0000313|EMBL:CAR21761.1, ECO:0000313|Proteomes:UP000002036};
RN   [1] {ECO:0000313|EMBL:CAR21761.1, ECO:0000313|Proteomes:UP000002036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 56472 / CBS 6340 / NRRL Y-8284
RC   {ECO:0000313|Proteomes:UP000002036};
RX   PubMed=19525356; DOI=10.1101/gr.091546.109;
RG   The Genolevures Consortium;
RA   Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA   Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P., Jubin C.,
RA   Poulain J., Barbe V., Segurens B., Artiguenave F., Anthouard V.,
RA   Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R., Durrens P.,
RA   Jean G., Marck C., Martin T., Nikolski M., Rolland T., Seret M.-L.,
RA   Casaregola S., Despons L., Fairhead C., Fischer G., Lafontaine I., Leh V.,
RA   Lemaire M., de Montigny J., Neuveglise C., Thierry A., Blanc-Lenfle I.,
RA   Bleykasten C., Diffels J., Fritsch E., Frangeul L., Goeffon A.,
RA   Jauniaux N., Kachouri-Lafond R., Payen C., Potier S., Pribylova L.,
RA   Ozanne C., Richard G.-F., Sacerdot C., Straub M.-L., Talla E.;
RT   "Comparative genomics of protoploid Saccharomycetaceae.";
RL   Genome Res. 19:1696-1709(2009).
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. Hydrolyzes ATP. Binds glutathione and may function by
CC       transporting a glutathione-conjugated iron-sulfur compound.
CC       {ECO:0000256|ARBA:ARBA00045666}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000256|ARBA:ARBA00004448}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004448}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB family.
CC       Heavy Metal importer (TC 3.A.1.210) subfamily.
CC       {ECO:0000256|ARBA:ARBA00024363}.
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DR   EMBL; CU928166; CAR21761.1; -; Genomic_DNA.
DR   AlphaFoldDB; C5DDA0; -.
DR   FunCoup; C5DDA0; 702.
DR   STRING; 559295.C5DDA0; -.
DR   KEGG; lth:KLTH0B09482g; -.
DR   eggNOG; KOG0057; Eukaryota.
DR   HOGENOM; CLU_000604_84_1_1; -.
DR   InParanoid; C5DDA0; -.
DR   OMA; VFHIIPI; -.
DR   OrthoDB; 6500128at2759; -.
DR   Proteomes; UP000002036; Chromosome B.
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:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0006879; P:intracellular iron ion homeostasis; IEA:TreeGrafter.
DR   GO; GO:0140466; P:iron-sulfur cluster export from the mitochondrion; IEA:UniProtKB-ARBA.
DR   CDD; cd18582; ABC_6TM_ATM1_ABCB7; 1.
DR   CDD; cd03253; ABCC_ATM1_transporter; 1.
DR   FunFam; 1.20.1560.10:FF:000004; ATP-binding cassette sub-family B member 7; 1.
DR   FunFam; 3.40.50.300:FF:000287; Multidrug ABC transporter ATP-binding protein; 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:SF402; IRON-SULFUR CLUSTERS TRANSPORTER ABCB7, MITOCHONDRIAL; 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   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00434};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00434}; Reference proteome {ECO:0000313|Proteomes:UP000002036};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   TRANSMEM        110..131
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        151..170
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        224..251
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        257..278
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        347..369
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          111..400
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50929"
FT   DOMAIN          435..671
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   REGION          58..80
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        58..67
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         468..475
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   694 AA;  77007 MW;  8B0AC82D918192F7 CRC64;
     MRPVDSIKLG GLVFRSLKPL PVRTSLCSRA FSLSPTARVS STIPTINSLR LYSTKNSPKI
     QENTVKSSPA PAKPKANEAS KTPTIGELKI LKDLFKYIWP NGDNKVKARV LIALSLLVGS
     KVLNVQVPFF FKQIVDSMNI EWADPTAVLP IAVTAMILSY GAARFGSVLF GELRNAIFAS
     VAQSAITRVS LQTFQHLMKL DLGWHLSRQT GGLTRAMDRG TKGISYVLSA MVFHIIPITV
     EIGAVCGILT YQFGASFAAM TFTTMLLYSI FTFKTTAWRT EFRKSANKAD NKAATVAVDS
     LINFEAVKYF NNEQFLANKY HNSLAQYRDS QIKVAQSLAF LNAGQNFIFT SALTAMMYMG
     CTGVISGTLS VGDLVLINQL VFQLSVPLNF LGSVYRELKQ SLIDMESLFQ LQRNKVKIQN
     KEKPLMLSSQ RPSKIVFENV SFGYDPDRMI LKNSSFTMPA GWKTAIVGPS GSGKSTILKL
     VFRFYDPQEG RILVDGKDVR ELDIESLRRA IGVVPQDTPL FNDSIWENVR FGKISASDEE
     IRLAVEKAQL ESLVDQLPKG RDTIVGERGL MISGGEKQRL AIARVLLKDA PIMFFDEATS
     ALDTHTEQAL LRTIKDNFPT GSKTSVYIAH RLRTIADADK IIVIQQGQVK EEGKHAELLA
     KPGSLYAELW NVQENLDVLN EELQREETQE KGDK
//