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Database: UniProt
Entry: A0A0K0DVY5_STRER
LinkDB: A0A0K0DVY5_STRER
Original site: A0A0K0DVY5_STRER 
ID   A0A0K0DVY5_STRER        Unreviewed;       587 AA.
AC   A0A0K0DVY5;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Iron-sulfur clusters transporter ABCB7, mitochondrial {ECO:0000256|ARBA:ARBA00041016};
DE   AltName: Full=ATP-binding cassette sub-family B member 7, mitochondrial {ECO:0000256|ARBA:ARBA00042945};
OS   Strongyloides stercoralis (Threadworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC   Strongyloides.
OX   NCBI_TaxID=6248 {ECO:0000313|WBParaSite:SSTP_0000140200.1};
RN   [1] {ECO:0000313|WBParaSite:SSTP_0000140200.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (AUG-2015) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(glutathione)4[2Fe(III)-2S] cluster(in) + ATP + H2O =
CC         (glutathione)4[2Fe(III)-2S] cluster(out) + ADP + H(+) + phosphate;
CC         Xref=Rhea:RHEA:67028, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:167627,
CC         ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00036789};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67029;
CC         Evidence={ECO:0000256|ARBA:ARBA00036789};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion
CC       inner membrane {ECO:0000256|ARBA:ARBA00004448}; Multi-pass membrane
CC       protein {ECO:0000256|ARBA:ARBA00004448}.
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DR   AlphaFoldDB; A0A0K0DVY5; -.
DR   STRING; 6248.A0A0K0DVY5; -.
DR   WBParaSite; SSTP_0000140200.1; SSTP_0000140200.1; SSTP_0000140200.
DR   Proteomes; UP000035681; Unassembled WGS sequence.
DR   GO; GO:0016020; C: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:0042221; P:response to chemical; IEA:UniProt.
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: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   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035681};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        24..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        105..130
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        136..155
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        214..241
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1..279
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50929"
FT   DOMAIN          315..549
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
SQ   SEQUENCE   587 AA;  65314 MW;  C9A645BD7399B38C CRC64;
     MKDIINYYNE KVPENLKLSI DEDASKTILT AGFCLIIAYG LARSGSALFN ELRNAVFARV
     SQHSVRNIAQ KIFLHLHSLD LKFHLNRQTG ALSKAIDRGT RGMSYVLSAL VFNVIPTVVE
     VSLVSGILYA KCGPQFSQAT LACLGTYAVS TLAITRWRTK FRHEMNQADN DAGNKAVDSL
     INYETVKYFN NEQFEAKRYD FFLKKYQDSS LKTLTSLAFL NFTQNVIFSA GLVGVMGLAA
     QEIQNGTMNV ADLVMINTLF FQLSVPLNFL GSVYREVRQG LVDMSTMFSL MSLKSNIQDR
     PGALPLKIDN EHSTVVMKDI HFGYTPDQPI LKGLDLEIPT GKKVAIVGGS GCGKSTIVRL
     LYRLYDSNSG TITINGQSSK DVTIKSLRES ISVVPQDCVL FHDTIFYNLK YGNPEATDEE
     VYEAAKMADL HEAVLRMPNG YQTIVGERGL KLSGGEKQRV AIARAILKNA NIVIYDEATS
     SLDAKTEENI MRSLRSAFAN RTSLFIAHRL ATIVDADIIY VLEDGKVIEK GNHHTLLSDS
     NSKYSELWKF QNINPDILLP KIKKREDDDL LLDLENNKCC GNSACNK
//
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