ID   BCS1B_DICDI             Reviewed;         458 AA.
AC   Q54DY9;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Probable mitochondrial chaperone BCS1-B;
DE   AltName: Full=BCS1-like protein 2;
GN   Name=bcsl1b; ORFNames=DDB_G0291910;
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; AAFI02000186; EAL61485.1; -; Genomic_DNA.
DR   RefSeq; XP_629907.1; XM_629905.1.
DR   AlphaFoldDB; Q54DY9; -.
DR   SMR; Q54DY9; -.
DR   STRING; 44689.DDB0266726; -.
DR   PaxDb; Q54DY9; -.
DR   EnsemblProtists; EAL61485; EAL61485; DDB_G0291910.
DR   GeneID; 8628408; -.
DR   KEGG; ddi:DDB_G0291910; -.
DR   dictyBase; DDB_G0291910; bcs1lB.
DR   eggNOG; KOG0743; Eukaryota.
DR   HOGENOM; CLU_010189_6_2_1; -.
DR   InParanoid; Q54DY9; -.
DR   OMA; EWRQFGH; -.
DR   PhylomeDB; Q54DY9; -.
DR   PRO; PR:Q54DY9; -.
DR   Proteomes; UP000002195; Chromosome 6.
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; 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.
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..458
FT                   /note="Probable mitochondrial chaperone BCS1-B"
FT                   /id="PRO_0000327921"
FT   TOPO_DOM        1..26
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        27..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        48..458
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   BINDING         248..255
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   458 AA;  51361 MW;  218865B6C0AE4214 CRC64;
     MENVITNNNK GLPKSILKFI PEPIQPLFEN PFFSAGFGLI GVGSILAMGR KGFQQAMIQS
     RRYFFVSVEV PSKDKSFHWL MEWLATKKNK NTRHVSVETT FHQHESGDIV SRINFVPSVG
     THYVFYRGRV IKVERSREKN VIDMNSGNLW ESITLTTLGT GRQVFQNLIE EAKEMALEKE
     EGKTLIYTSM GTDWRRFGHP RRKRPISSVI LDKGKSELII QDVKKFLNNS DWYNDRGIPY
     RRGYLLYGPP GTGKSSFITA LAGELQLSIC ILNLAGKSVS DTSLNQLLAT APQRSIILLE
     DIDSAIQTGN HDLSAKSNSA NAPSISSGGL QYQGYYGNPS VSSGGSALTF SGLLNALDGV
     AASEGRILFM TTNHLEKLDK VLIRPGRVDL QIEIGLCSSY QMEQMFLKFY PTDFDLAKQF
     VEKLENYKFS PAQLQAYFMT YSNNSIEAIN NLNELIKK