SBA1_YEAST
ID SBA1_YEAST Reviewed; 216 AA.
AC P28707; D6VXH2;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Co-chaperone protein SBA1;
GN Name=SBA1; OrderedLocusNames=YKL117W; ORFNames=YKL518;
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=1561835; DOI=10.1002/yea.320080207;
RA Jacquier A., Legrain P., Dujon B.;
RT "Sequence of a 10.7 kb segment of yeast chromosome XI identifies the APN1
RT and the BAF1 loci and reveals one tRNA gene and several new open reading
RT frames including homologs to RAD2 and kinases.";
RL Yeast 8:121-132(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
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 ACETYLATION AT SER-2.
RX PubMed=9298649; DOI=10.1002/elps.1150180810;
RA Garrels J.I., McLaughlin C.S., Warner J.R., Futcher B., Latter G.I.,
RA Kobayashi R., Schwender B., Volpe T., Anderson D.S., Mesquita-Fuentes R.,
RA Payne W.E.;
RT "Proteome studies of Saccharomyces cerevisiae: identification and
RT characterization of abundant proteins.";
RL Electrophoresis 18:1347-1360(1997).
RN [5]
RP FUNCTION.
RX PubMed=10691735;
RA Freeman B.C., Felts S.J., Toft D.O., Yamamoto K.R.;
RT "The p23 molecular chaperones act at a late step in intracellular receptor
RT action to differentially affect ligand efficacies.";
RL Genes Dev. 14:422-434(2000).
RN [6]
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).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 2-135 IN COMPLEX WITH HSP82.
RX PubMed=16625188; DOI=10.1038/nature04716;
RA Ali M.M., Roe S.M., Vaughan C.K., Meyer P., Panaretou B., Piper P.W.,
RA Prodromou C., Pearl L.H.;
RT "Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone
RT complex.";
RL Nature 440:1013-1017(2006).
CC -!- FUNCTION: Acts as a co-chaperone. {ECO:0000269|PubMed:10691735}.
CC -!- SUBUNIT: Interacts with HSP82. {ECO:0000269|PubMed:16625188}.
CC -!- INTERACTION:
CC P28707; P02829: HSP82; NbExp=7; IntAct=EBI-26838, EBI-8659;
CC -!- MISCELLANEOUS: Present with 33700 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the p23/wos2 family. {ECO:0000305}.
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DR EMBL; S93804; AAB22000.1; -; Genomic_DNA.
DR EMBL; Z28117; CAA81957.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09042.1; -; Genomic_DNA.
DR PIR; S27382; S27382.
DR RefSeq; NP_012805.1; NM_001179683.1.
DR PDB; 2CG9; X-ray; 3.10 A; X/Y=2-135.
DR PDBsum; 2CG9; -.
DR AlphaFoldDB; P28707; -.
DR SMR; P28707; -.
DR BioGRID; 34018; 386.
DR DIP; DIP-2311N; -.
DR IntAct; P28707; 13.
DR MINT; P28707; -.
DR STRING; 4932.YKL117W; -.
DR iPTMnet; P28707; -.
DR SWISS-2DPAGE; P28707; -.
DR MaxQB; P28707; -.
DR PaxDb; P28707; -.
DR PRIDE; P28707; -.
DR TopDownProteomics; P28707; -.
DR EnsemblFungi; YKL117W_mRNA; YKL117W; YKL117W.
DR GeneID; 853743; -.
DR KEGG; sce:YKL117W; -.
DR SGD; S000001600; SBA1.
DR VEuPathDB; FungiDB:YKL117W; -.
DR eggNOG; KOG3158; Eukaryota.
DR GeneTree; ENSGT00880000138731; -.
DR HOGENOM; CLU_078883_0_1_1; -.
DR InParanoid; P28707; -.
DR OMA; DDYANNF; -.
DR BioCyc; YEAST:G3O-31901-MON; -.
DR Reactome; R-SCE-2162123; Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
DR Reactome; R-SCE-3371511; HSF1 activation.
DR EvolutionaryTrace; P28707; -.
DR PRO; PR:P28707; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P28707; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0051087; F:chaperone binding; IMP:SGD.
DR GO; GO:0051879; F:Hsp90 protein binding; IBA:GO_Central.
DR GO; GO:0051131; P:chaperone-mediated protein complex assembly; IBA:GO_Central.
DR GO; GO:0043392; P:negative regulation of DNA binding; IDA:SGD.
DR GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; IDA:SGD.
DR GO; GO:0006457; P:protein folding; IMP:SGD.
DR GO; GO:0051972; P:regulation of telomerase activity; IDA:SGD.
DR Gene3D; 2.60.40.790; -; 1.
DR InterPro; IPR007052; CS_dom.
DR InterPro; IPR008978; HSP20-like_chaperone.
DR InterPro; IPR045250; p23-like.
DR PANTHER; PTHR22932; PTHR22932; 1.
DR SUPFAM; SSF49764; SSF49764; 1.
DR PROSITE; PS51203; CS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Chaperone; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9298649"
FT CHAIN 2..216
FT /note="Co-chaperone protein SBA1"
FT /id="PRO_0000218959"
FT DOMAIN 5..108
FT /note="CS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00547"
FT REPEAT 141..156
FT REPEAT 160..174
FT REGION 169..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..216
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:9298649"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:2CG9"
FT STRAND 23..29
FT /evidence="ECO:0007829|PDB:2CG9"
FT STRAND 33..37
FT /evidence="ECO:0007829|PDB:2CG9"
FT STRAND 44..49
FT /evidence="ECO:0007829|PDB:2CG9"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:2CG9"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:2CG9"
FT STRAND 77..84
FT /evidence="ECO:0007829|PDB:2CG9"
FT STRAND 91..96
FT /evidence="ECO:0007829|PDB:2CG9"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:2CG9"
FT STRAND 107..110
FT /evidence="ECO:0007829|PDB:2CG9"
FT STRAND 115..119
FT /evidence="ECO:0007829|PDB:2CG9"
FT TURN 121..123
FT /evidence="ECO:0007829|PDB:2CG9"
FT STRAND 127..131
FT /evidence="ECO:0007829|PDB:2CG9"
SQ SEQUENCE 216 AA; 24082 MW; C51CDE30BF2FA945 CRC64;
MSDKVINPQV AWAQRSSTTD PERNYVLITV SIADCDAPEL TIKPSYIELK AQSKPHVGDE
NVHHYQLHID LYKEIIPEKT MHKVANGQHY FLKLYKKDLE SEYWPRLTKE KVKYPYIKTD
FDKWVDEDEQ DEVEAEGNDA AQGMDFSQMM GGAGGAGGAG GMDFSQMMGG AGGAGSPDMA
QLQQLLAQSG GNLDMGDFKE NDEEDEEEEI EPEVKA
