ID   BCS1A_DICDI             Reviewed;         421 AA.
AC   Q54HY8;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Probable mitochondrial chaperone BCS1-A;
DE   AltName: Full=BCS1-like protein 1;
GN   Name=bcs1la; ORFNames=DDB_G0289135;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
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; AAFI02000130; EAL62875.1; -; Genomic_DNA.
DR   RefSeq; XP_636375.1; XM_631283.1.
DR   AlphaFoldDB; Q54HY8; -.
DR   SMR; Q54HY8; -.
DR   STRING; 44689.DDB0266725; -.
DR   PaxDb; Q54HY8; -.
DR   EnsemblProtists; EAL62875; EAL62875; DDB_G0289135.
DR   GeneID; 8626976; -.
DR   KEGG; ddi:DDB_G0289135; -.
DR   dictyBase; DDB_G0289135; bcs1lA.
DR   eggNOG; KOG0743; Eukaryota.
DR   HOGENOM; CLU_010189_6_2_1; -.
DR   InParanoid; Q54HY8; -.
DR   OMA; FITNESW; -.
DR   PhylomeDB; Q54HY8; -.
DR   PRO; PR:Q54HY8; -.
DR   Proteomes; UP000002195; Chromosome 5.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; ISS:dictyBase.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0008320; F:protein transmembrane transporter activity; ISS:dictyBase.
DR   GO; GO:0051131; P:chaperone-mediated protein complex assembly; ISS:dictyBase.
DR   GO; GO:0034551; P:mitochondrial respiratory chain complex III assembly; IBA:GO_Central.
DR   GO; GO:0032979; P:protein insertion into mitochondrial inner membrane from matrix; IBA:GO_Central.
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   3: Inferred from homology;
KW   ATP-binding; Chaperone; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Nucleotide-binding; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..421
FT                   /note="Probable mitochondrial chaperone BCS1-A"
FT                   /id="PRO_0000327920"
FT   TOPO_DOM        1..10
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        11..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        32..421
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   BINDING         228..235
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   421 AA;  47356 MW;  873BC73A902982DA CRC64;
     MNHLKDQSKS IVLGISSGIG IFLISGGINI FKNVGQYILN RINSNIYYRI DVDSKDKSFE
     WLLYWLSEND SIKVSNHLNA ETVYNLVGKN PKVILVPSVG KHRIVYKGKW IWIDRVRDQQ
     FDMGAGAPFE SISISTYKSN AQLINQLLQE AMTLSLNRDI GKTVIYINGG NGNWERFGNP
     RSIRSLSSVI LADDLKSKLI EDIKSFITNE SWYRNRGIPY RRGYLLYGEP GNGKSSLINA
     IAGELNLDIC IVSLSSKDID DKQINHLLNN APPKSILLIE DIDAAFKSHR DNVDSNNNNS
     NNNNSLTYSG LLNALDGVAS QEGRILFMTT NKIELLDSAL IREGRIDLKI KVSNATKSQA
     AQLFTHFYNL PTDNQLAIRF SENLHDHQLS MSQIQGFLLK YINSPEKAIE EVQSITPFNL
     N