ID   BCS1_XENLA              Reviewed;         419 AA.
AC   Q7ZTL7;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Mitochondrial chaperone BCS1;
DE   AltName: Full=BCS1-like protein;
GN   Name=bcs1l;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Chaperone necessary for the assembly of mitochondrial
CC       respiratory chain complex III. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC       Single-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family. BCS1 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; BC045021; AAH45021.1; -; mRNA.
DR   RefSeq; NP_001080674.1; NM_001087205.1.
DR   AlphaFoldDB; Q7ZTL7; -.
DR   SMR; Q7ZTL7; -.
DR   DNASU; 380366; -.
DR   GeneID; 380366; -.
DR   KEGG; xla:380366; -.
DR   CTD; 380366; -.
DR   Xenbase; XB-GENE-1015032; bcs1l.L.
DR   OrthoDB; 532729at2759; -.
DR   Proteomes; UP000186698; Chromosome 9_10L.
DR   Bgee; 380366; Expressed in ovary and 19 other tissues.
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:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR003960; ATPase_AAA_CS.
DR   InterPro; IPR014851; BCS1_N.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF08740; BCS1_N; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM01024; BCS1_N; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00674; AAA; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Chaperone; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Nucleotide-binding; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..419
FT                   /note="Mitochondrial chaperone BCS1"
FT                   /id="PRO_0000084775"
FT   TOPO_DOM        1..15
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        16..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        33..419
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   BINDING         230..237
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   419 AA;  47118 MW;  6B0644149C8655C2 CRC64;
     MPFADFVAAL KDNPYFGAGF GLVGVGTALA LTRKGAQFGM IAFRRHYMIT LEVPSKDKSY
     QWLLSWISHY AKNTQHLSVE TSYLQHESGR ISTKFDFVPS PGNHFIWYRS KWIRIERNRE
     KQMIDLHTGT PWESVTFTAL GTNRNIFFNI LQEARELALK QQVGKTVMYN AVGAEWRQFG
     FPRRRRPLSS VVLEQGISEK IVQDVKGFIE NPKWYSDRGI PYRRGYLLYG PPGCGKSSFI
     TALAGELEYS ICLMSLSDSS LSDDRLNHLL SVAPQQSIIL LEDVDAAFVS RDLNKQNPTA
     YQGMGRLTFS GLLNALDGVA STEARIVFMT TNHIDRLDPA LIRPGRVDVK QYVGHCTNWQ
     LSQMFLRFYP DQTAGQSEAF ASAALSSSDK ISAAQVQGHF MMHKTDPDGA IQNVCLATM