BCS1_YEAST
ID BCS1_YEAST Reviewed; 456 AA.
AC P32839; D6VT07; Q06404;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Mitochondrial chaperone BCS1;
GN Name=BCS1; OrderedLocusNames=YDR375C; ORFNames=D9481.17;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1327750; DOI=10.1002/j.1460-2075.1992.tb05474.x;
RA Nobrega F.G., Nobrega M.P., Tzagoloff A.;
RT "BCS1, a novel gene required for the expression of functional Rieske iron-
RT sulfur protein in Saccharomyces cerevisiae.";
RL EMBO J. 11:3821-3829(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP TOPOLOGY.
RX PubMed=8599931; DOI=10.1002/j.1460-2075.1996.tb00380.x;
RA Foelsch H., Guiard B., Neupert W., Stuart R.A.;
RT "Internal targeting signal of the BCS1 protein: a novel mechanism of import
RT into mitochondria.";
RL EMBO J. 15:479-487(1996).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
CC -!- FUNCTION: Essential for the expression of the Rieske iron-sulfur
CC protein.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass
CC membrane protein.
CC -!- MISCELLANEOUS: Present with 1990 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. BCS1 subfamily.
CC {ECO:0000305}.
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DR EMBL; S47190; AAC09007.1; -; Genomic_DNA.
DR EMBL; U28373; AAB64811.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12217.1; -; Genomic_DNA.
DR PIR; S61170; S61170.
DR RefSeq; NP_010663.1; NM_001180683.1.
DR PDB; 6SH3; EM; 3.40 A; A/B/C/D/E/F/G=1-456.
DR PDB; 6SH4; EM; 4.40 A; A/B/C/D/E/F/G=1-456.
DR PDB; 6SH5; EM; 4.60 A; A/B/C/D/E/F/G=1-456.
DR PDBsum; 6SH3; -.
DR PDBsum; 6SH4; -.
DR PDBsum; 6SH5; -.
DR AlphaFoldDB; P32839; -.
DR SMR; P32839; -.
DR BioGRID; 32434; 221.
DR IntAct; P32839; 1.
DR STRING; 4932.YDR375C; -.
DR TCDB; 3.A.28.1.1; the aaa-atpase, bcs1 (bcs1) family.
DR iPTMnet; P32839; -.
DR MaxQB; P32839; -.
DR PaxDb; P32839; -.
DR PRIDE; P32839; -.
DR EnsemblFungi; YDR375C_mRNA; YDR375C; YDR375C.
DR GeneID; 851981; -.
DR KEGG; sce:YDR375C; -.
DR SGD; S000002783; BCS1.
DR VEuPathDB; FungiDB:YDR375C; -.
DR eggNOG; KOG0743; Eukaryota.
DR GeneTree; ENSGT00390000005415; -.
DR HOGENOM; CLU_010189_6_2_1; -.
DR InParanoid; P32839; -.
DR OMA; EWRQFGH; -.
DR BioCyc; YEAST:G3O-29925-MON; -.
DR ChiTaRS; BCS1; yeast.
DR PRO; PR:P32839; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P32839; protein.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:SGD.
DR GO; GO:0005758; C:mitochondrial intermembrane space; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IMP:SGD.
DR GO; GO:0008320; F:protein transmembrane transporter activity; IMP:SGD.
DR GO; GO:0051131; P:chaperone-mediated protein complex assembly; IMP:SGD.
DR GO; GO:0034551; P:mitochondrial respiratory chain complex III assembly; IMP:SGD.
DR GO; GO:0032979; P:protein insertion into mitochondrial inner membrane from matrix; IMP:SGD.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Nucleotide-binding; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..456
FT /note="Mitochondrial chaperone BCS1"
FT /id="PRO_0000084777"
FT TOPO_DOM 1..44
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305|PubMed:8599931"
FT TRANSMEM 45..68
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 69..456
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305|PubMed:8599931"
FT MOTIF 69..83
FT /note="Mitochondrial-targeting signal"
FT BINDING 267..274
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 119
FT /note="N -> F (in Ref. 1; AAC09007)"
FT /evidence="ECO:0000305"
FT CONFLICT 267
FT /note="G -> S (in Ref. 1; AAC09007)"
FT /evidence="ECO:0000305"
FT CONFLICT 349
FT /note="L -> Q (in Ref. 1; AAC09007)"
FT /evidence="ECO:0000305"
FT CONFLICT 351
FT /note="G -> S (in Ref. 1; AAC09007)"
FT /evidence="ECO:0000305"
FT HELIX 54..81
FT /evidence="ECO:0007829|PDB:6SH3"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:6SH3"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:6SH3"
FT HELIX 97..105
FT /evidence="ECO:0007829|PDB:6SH3"
FT STRAND 107..110
FT /evidence="ECO:0007829|PDB:6SH3"
FT STRAND 115..122
FT /evidence="ECO:0007829|PDB:6SH3"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:6SH3"
FT STRAND 128..135
FT /evidence="ECO:0007829|PDB:6SH3"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:6SH3"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:6SH3"
FT STRAND 150..161
FT /evidence="ECO:0007829|PDB:6SH3"
FT STRAND 163..175
FT /evidence="ECO:0007829|PDB:6SH3"
FT TURN 179..182
FT /evidence="ECO:0007829|PDB:6SH3"
FT HELIX 183..198
FT /evidence="ECO:0007829|PDB:6SH3"
FT STRAND 205..218
FT /evidence="ECO:0007829|PDB:6SH3"
FT HELIX 225..227
FT /evidence="ECO:0007829|PDB:6SH3"
FT HELIX 234..239
FT /evidence="ECO:0007829|PDB:6SH3"
FT HELIX 241..245
FT /evidence="ECO:0007829|PDB:6SH3"
FT HELIX 249..254
FT /evidence="ECO:0007829|PDB:6SH3"
FT STRAND 259..266
FT /evidence="ECO:0007829|PDB:6SH3"
FT HELIX 273..283
FT /evidence="ECO:0007829|PDB:6SH3"
FT STRAND 287..292
FT /evidence="ECO:0007829|PDB:6SH3"
FT HELIX 300..308
FT /evidence="ECO:0007829|PDB:6SH3"
FT STRAND 312..319
FT /evidence="ECO:0007829|PDB:6SH3"
FT HELIX 321..323
FT /evidence="ECO:0007829|PDB:6SH3"
FT HELIX 342..350
FT /evidence="ECO:0007829|PDB:6SH3"
FT STRAND 358..365
FT /evidence="ECO:0007829|PDB:6SH3"
FT STRAND 379..385
FT /evidence="ECO:0007829|PDB:6SH3"
FT HELIX 391..401
FT /evidence="ECO:0007829|PDB:6SH3"
FT HELIX 406..416
FT /evidence="ECO:0007829|PDB:6SH3"
FT HELIX 425..433
FT /evidence="ECO:0007829|PDB:6SH3"
FT TURN 434..437
FT /evidence="ECO:0007829|PDB:6SH3"
FT HELIX 439..445
FT /evidence="ECO:0007829|PDB:6SH3"
FT TURN 446..448
FT /evidence="ECO:0007829|PDB:6SH3"
SQ SEQUENCE 456 AA; 51107 MW; 17750D26B664ED04 CRC64;
MSDKPIDIQY DKQATPNLSG VITPPTNETG NDSVREKLSK LVGDAMSNNP YFAAGGGLMI
LGTGLAVARS GIIKASRVLY RQMIVDLEIQ SKDKSYAWFL TWMAKHPQRV SRHLSVRTNY
IQHDNGSVST KFSLVPGPGN HWIRYKGAFI LIKRERSAKM IDIANGSPFE TVTLTTLYRD
KHLFDDILNE AKDIALKTTE GKTVIYTSFG PEWRKFGQPK AKRMLPSVIL DSGIKEGILD
DVYDFMKNGK WYSDRGIPYR RGYLLYGPPG SGKTSFIQAL AGELDYNICI LNLSENNLTD
DRLNHLMNNM PERSILLLED IDAAFNKRSQ TGEQGFHSSV TFSGLLNALD GVTSSEETIT
FMTTNHPEKL DAAIMRPGRI DYKVFVGNAT PYQVEKMFMK FYPGETDICK KFVNSVKELD
ITVSTAQLQG LFVMNKDAPH DALKMVSSLR NANHIF
