SSB1_YEAST
ID SSB1_YEAST Reviewed; 613 AA.
AC P11484; D6VRC7; Q05834;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 213.
DE RecName: Full=Ribosome-associated molecular chaperone SSB1 {ECO:0000303|PubMed:11739779};
DE EC=3.6.4.10 {ECO:0000269|PubMed:9860955};
DE AltName: Full=Cold-inducible protein YG101 {ECO:0000303|PubMed:6761581};
DE AltName: Full=Heat shock protein SSB1 {ECO:0000303|PubMed:3302682};
DE AltName: Full=Hsp70 chaperone Ssb {ECO:0000303|PubMed:8994035};
GN Name=SSB1 {ECO:0000303|PubMed:3302682};
GN Synonyms=YG101 {ECO:0000303|PubMed:6761581};
GN OrderedLocusNames=YDL229W {ECO:0000312|SGD:S000002388};
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].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=2664714; DOI=10.1093/nar/17.12.4891;
RA Slater M.R., Craig E.A.;
RT "The SSB1 heat shock cognate gene of the yeast Saccharomyces cerevisiae.";
RL Nucleic Acids Res. 17:4891-4891(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2661019; DOI=10.1016/0092-8674(89)90059-7;
RA Normington K., Kohno K., Kozutsumi Y., Gething M.J., Sambrook J.;
RT "S. cerevisiae encodes an essential protein homologous in sequence and
RT function to mammalian BiP.";
RL Cell 57:1223-1236(1989).
RN [3]
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 [4]
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 [5]
RP PROTEIN SEQUENCE OF 39-49 AND 431-439.
RC STRAIN=ATCC 38531 / Y41;
RX PubMed=7737086; DOI=10.1002/elps.1150160124;
RA Norbeck J., Blomberg A.;
RT "Gene linkage of two-dimensional polyacrylamide gel electrophoresis
RT resolved proteins from isogene families in Saccharomyces cerevisiae by
RT microsequencing of in-gel trypsin generated peptides.";
RL Electrophoresis 16:149-156(1995).
RN [6]
RP PROTEIN SEQUENCE OF 145-159.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7895733; DOI=10.1002/elps.11501501210;
RA Garrels J.I., Futcher B., Kobayashi R., Latter G.I., Schwender B.,
RA Volpe T., Warner J.R., McLaughlin C.S.;
RT "Protein identifications for a Saccharomyces cerevisiae protein database.";
RL Electrophoresis 15:1466-1486(1994).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 180-403, AND INDUCTION.
RX PubMed=6761581; DOI=10.1128/mcb.2.11.1388-1398.1982;
RA Ingolia T.D., Slater M.R., Craig E.A.;
RT "Saccharomyces cerevisiae contains a complex multigene family related to
RT the major heat shock-inducible gene of Drosophila.";
RL Mol. Cell. Biol. 2:1388-1398(1982).
RN [8]
RP GENE FAMILY.
RX PubMed=3302682; DOI=10.1128/mcb.7.7.2568-2577.1987;
RA Werner-Washburne M., Stone D.E., Craig E.A.;
RT "Complex interactions among members of an essential subfamily of hsp70
RT genes in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 7:2568-2577(1987).
RN [9]
RP INDUCTION.
RX PubMed=2651414; DOI=10.1128/jb.171.5.2680-2688.1989;
RA Werner-Washburne M., Becker J., Kosic-Smithers J., Craig E.A.;
RT "Yeast Hsp70 RNA levels vary in response to the physiological status of the
RT cell.";
RL J. Bacteriol. 171:2680-2688(1989).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=1394434; DOI=10.1016/0092-8674(92)90269-i;
RA Nelson R.J., Ziegelhoffer T., Nicolet C., Werner-Washburne M., Craig E.A.;
RT "The translation machinery and 70 kd heat shock protein cooperate in
RT protein synthesis.";
RL Cell 71:97-105(1992).
RN [11]
RP INDUCTION.
RX PubMed=7646503; DOI=10.1006/bbrc.1995.2157;
RA Iwahashi H., Wu Y., Tanguay R.M.;
RT "Detection and expression of the 70 kDa heat shock protein SSB1P at
RT different temperatures in Saccharomyces cerevisiae.";
RL Biochem. Biophys. Res. Commun. 213:484-489(1995).
RN [12]
RP ACETYLATION AT ALA-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 [13]
RP FUNCTION.
RX PubMed=8994035; DOI=10.1126/science.275.5298.387;
RA James P., Pfund C., Craig E.A.;
RT "Functional specificity among Hsp70 molecular chaperones.";
RL Science 275:387-389(1997).
RN [14]
RP FUNCTION, AND SUBUNIT.
RX PubMed=9670014; DOI=10.1093/emboj/17.14.3981;
RA Pfund C., Lopez-Hoyo N., Ziegelhoffer T., Schilke B.A., Lopez-Buesa P.,
RA Walter W.A., Wiedmann M., Craig E.A.;
RT "The molecular chaperone Ssb from Saccharomyces cerevisiae is a component
RT of the ribosome-nascent chain complex.";
RL EMBO J. 17:3981-3989(1998).
RN [15]
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=9860955; DOI=10.1073/pnas.95.26.15253;
RA Lopez-Buesa P., Pfund C., Craig E.A.;
RT "The biochemical properties of the ATPase activity of a 70-kDa heat shock
RT protein (Hsp70) are governed by the C-terminal domains.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:15253-15258(1998).
RN [16]
RP INDUCTION.
RX PubMed=10322015; DOI=10.1128/jb.181.10.3136-3143.1999;
RA Lopez N., Halladay J., Walter W., Craig E.A.;
RT "SSB, encoding a ribosome-associated chaperone, is coordinately regulated
RT with ribosomal protein genes.";
RL J. Bacteriol. 181:3136-3143(1999).
RN [17]
RP SUBCELLULAR LOCATION.
RX PubMed=10347213; DOI=10.1074/jbc.274.23.16501;
RA Shulga N., James P., Craig E.A., Goldfarb D.S.;
RT "A nuclear export signal prevents Saccharomyces cerevisiae Hsp70 Ssb1p from
RT stimulating nuclear localization signal-directed nuclear transport.";
RL J. Biol. Chem. 274:16501-16507(1999).
RN [18]
RP FUNCTION.
RX PubMed=11739779; DOI=10.1091/mbc.12.12.3773;
RA Pfund C., Huang P., Lopez-Hoyo N., Craig E.A.;
RT "Divergent functional properties of the ribosome-associated molecular
RT chaperone Ssb compared with other Hsp70s.";
RL Mol. Biol. Cell 12:3773-3782(2001).
RN [19]
RP FUNCTION, AND SUBUNIT.
RX PubMed=11929994; DOI=10.1073/pnas.062048599;
RA Gautschi M., Mun A., Ross S., Rospert S.;
RT "A functional chaperone triad on the yeast ribosome.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:4209-4214(2002).
RN [20]
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 [21]
RP FUNCTION, AND INTERACTION WITH SSE1.
RX PubMed=16219770; DOI=10.1074/jbc.m503615200;
RA Yam A.Y., Albanese V., Lin H.T., Frydman J.;
RT "Hsp110 cooperates with different cytosolic HSP70 systems in a pathway for
RT de novo folding.";
RL J. Biol. Chem. 280:41252-41261(2005).
RN [22]
RP FUNCTION, AND INTERACTION WITH SSE1.
RX PubMed=16221677; DOI=10.1074/jbc.m503614200;
RA Shaner L., Wegele H., Buchner J., Morano K.A.;
RT "The yeast Hsp110 Sse1 functionally interacts with the Hsp70 chaperones Ssa
RT and Ssb.";
RL J. Biol. Chem. 280:41262-41269(2005).
RN [23]
RP INTERACTION WITH FES1.
RX PubMed=17132105; DOI=10.1515/bc.2006.198;
RA Dragovic Z., Shomura Y., Tzvetkov N., Hartl F.U., Bracher A.;
RT "Fes1p acts as a nucleotide exchange factor for the ribosome-associated
RT molecular chaperone Ssb1p.";
RL Biol. Chem. 387:1593-1600(2006).
RN [24]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [25]
RP INTERACTION WITH NAP1, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18086883; DOI=10.1128/mcb.01035-07;
RA Calvert M.E.K., Keck K.M., Ptak C., Shabanowitz J., Hunt D.F.,
RA Pemberton L.F.;
RT "Phosphorylation by casein kinase 2 regulates Nap1 localization and
RT function.";
RL Mol. Cell. Biol. 28:1313-1325(2008).
RN [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-47, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-431, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [28]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH RAC AND SSE1.
RX PubMed=23332755; DOI=10.1016/j.cell.2012.12.001;
RA Willmund F., del Alamo M., Pechmann S., Chen T., Albanese V., Dammer E.B.,
RA Peng J., Frydman J.;
RT "The cotranslational function of ribosome-associated Hsp70 in eukaryotic
RT protein homeostasis.";
RL Cell 152:196-209(2013).
RN [29]
RP INTERACTION WITH RPL35; RPL39 AND RPL19, AND MUTAGENESIS OF
RP 567-LYS-ARG-568; 596-ARG-LYS-597 AND 603-LYS-ARG-604.
RX PubMed=27882919; DOI=10.1038/ncomms13563;
RA Gumiero A., Conz C., Gese G.V., Zhang Y., Weyer F.A., Lapouge K.,
RA Kappes J., von Plehwe U., Schermann G., Fitzke E., Woelfle T., Fischer T.,
RA Rospert S., Sinning I.;
RT "Interaction of the cotranslational Hsp70 Ssb with ribosomal proteins and
RT rRNA depends on its lid domain.";
RL Nat. Commun. 7:13563-13563(2016).
RN [30]
RP SUBUNIT.
RX PubMed=27917864; DOI=10.1038/ncomms13695;
RA Hanebuth M.A., Kityk R., Fries S.J., Jain A., Kriel A., Albanese V.,
RA Frickey T., Peter C., Mayer M.P., Frydman J., Deuerling E.;
RT "Multivalent contacts of the Hsp70 Ssb contribute to its architecture on
RT ribosomes and nascent chain interaction.";
RL Nat. Commun. 7:13695-13695(2016).
RN [31]
RP X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) OF 1-384.
RA Osipiuk J., Li H., Bargassa M., Sahi C., Craig E.A., Joachimiak A.;
RT "Crystal structure of ATPase domain of Ssb1 chaperone, member of the HSP70
RT family from Saccharomyces cerevisiae.";
RL Submitted (MAR-2009) to the PDB data bank.
CC -!- FUNCTION: Ribosome-bound, Hsp70-type chaperone that assists in the
CC cotranslational folding of newly synthesized proteins in the cytosol.
CC Stimulates folding by interacting with nascent chains, binding to
CC short, largely hydrophobic sequences exposed by unfolded proteins,
CC thereby stabilizing longer, more slowly translated, and aggregation-
CC prone nascent polypeptides and domains that cannot fold stably until
CC fully synthesized. The Hsp70-protein substrate interaction depends on
CC ATP-binding and on allosteric regulation between the NBD and the SBD.
CC The ATP-bound state is characterized by a fast exchange rate of
CC substrate (low affinity state), while in the ADP-bound state exchange
CC is much slower (high affinity state). During the Hsp70 cycle, the
CC chaperone switches between the ATP-bound state (open conformation) and
CC the ADP-bound state (closed conformation) by major conformational
CC rearrangements involving mainly the lid domain. Ssb cooperates with a
CC specific Hsp40/Hsp70 co-chaperone termed the ribosome-associated
CC complex (RAC), which stimulates the ATPase activity of the ribosome-
CC associated pool of Ssbs and switches it to the high affinity substrate
CC binding state. Hsp110 chaperone SSE1 and FES1 act as nucleotide
CC exchange factors that cause substrate release.
CC {ECO:0000269|PubMed:11739779, ECO:0000269|PubMed:11929994,
CC ECO:0000269|PubMed:1394434, ECO:0000269|PubMed:16219770,
CC ECO:0000269|PubMed:16221677, ECO:0000269|PubMed:23332755,
CC ECO:0000269|PubMed:8994035, ECO:0000269|PubMed:9670014}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.10;
CC Evidence={ECO:0000269|PubMed:9860955};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=270 uM for ATP (at 2.5 mM potassium acetate)
CC {ECO:0000269|PubMed:9860955};
CC KM=147 uM for ATP (at 100 mM potassium acetate)
CC {ECO:0000269|PubMed:9860955};
CC Note=kcat is 0.95 min(-1) with ATP as substrate (at 2.5 mM potassium
CC acetate) and 0.81 min(-1) with ATP as substrate (at 100 mM potassium
CC acetate). {ECO:0000269|PubMed:9860955};
CC -!- SUBUNIT: Binds to ribosomes (PubMed:9670014, PubMed:1394434,
CC PubMed:27917864). Binds close to the ribosomal tunnel exit via contacts
CC with both ribosomal proteins RPL35, RPL39 and RPL19, and rRNA
CC (PubMed:27882919). Directly interacts with nascent polypeptides. This
CC interaction is dependent on the ribosome-associated complex (RAC)
CC (PubMed:11929994, PubMed:23332755). Interacts with SSE1
CC (PubMed:16219770, PubMed:16221677, PubMed:23332755). Interacts with
CC FES1 (PubMed:17132105). Interacts with NAP1 (PubMed:18086883).
CC {ECO:0000269|PubMed:11929994, ECO:0000269|PubMed:1394434,
CC ECO:0000269|PubMed:16219770, ECO:0000269|PubMed:16221677,
CC ECO:0000269|PubMed:17132105, ECO:0000269|PubMed:18086883,
CC ECO:0000269|PubMed:23332755, ECO:0000269|PubMed:27882919,
CC ECO:0000269|PubMed:27917864, ECO:0000269|PubMed:9670014}.
CC -!- INTERACTION:
CC P11484; P43573: BUD27; NbExp=3; IntAct=EBI-8627, EBI-22787;
CC P11484; P40433: PFK26; NbExp=2; IntAct=EBI-8627, EBI-1956;
CC P11484; P32589: SSE1; NbExp=2; IntAct=EBI-8627, EBI-8648;
CC P11484; P38825: TOM71; NbExp=2; IntAct=EBI-8627, EBI-24694;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10347213,
CC ECO:0000269|PubMed:23332755, ECO:0000305|PubMed:1394434}. Note=About
CC 50% of the protein is associated with translating ribosomes, but
CC sufficient Ssb exists in the cell for each ribosome to be associated
CC with at least one Ssb molecule. {ECO:0000269|PubMed:1394434,
CC ECO:0000269|PubMed:23332755, ECO:0000269|PubMed:9670014}.
CC -!- INDUCTION: Expression decreases after heat shock or during growth to
CC stationary phase (PubMed:6761581, PubMed:2651414). Degraded during heat
CC shock treatment (at protein level) (PubMed:7646503). Up-regulated upon
CC carbon upshift and down-regulated upon amino acid limitation in an
CC HSF1-dependent manner (PubMed:10322015). {ECO:0000269|PubMed:10322015,
CC ECO:0000269|PubMed:2651414, ECO:0000269|PubMed:6761581,
CC ECO:0000269|PubMed:7646503}.
CC -!- MISCELLANEOUS: Present with 170000 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. Ssb-type Hsp70
CC subfamily. {ECO:0000305}.
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DR EMBL; X13713; CAA31995.1; -; Genomic_DNA.
DR EMBL; M25395; AAA35099.1; -; mRNA.
DR EMBL; Z74277; CAA98807.1; -; Genomic_DNA.
DR EMBL; M17585; AAA34692.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11637.1; -; Genomic_DNA.
DR PIR; S20149; S20149.
DR RefSeq; NP_010052.1; NM_001180289.1.
DR PDB; 3GL1; X-ray; 1.92 A; A/B=1-384.
DR PDBsum; 3GL1; -.
DR AlphaFoldDB; P11484; -.
DR SMR; P11484; -.
DR BioGRID; 31882; 838.
DR DIP; DIP-2254N; -.
DR IntAct; P11484; 779.
DR MINT; P11484; -.
DR STRING; 4932.YDL229W; -.
DR CarbonylDB; P11484; -.
DR iPTMnet; P11484; -.
DR COMPLUYEAST-2DPAGE; P11484; -.
DR SWISS-2DPAGE; P11484; -.
DR UCD-2DPAGE; P11484; -.
DR MaxQB; P11484; -.
DR PaxDb; P11484; -.
DR PRIDE; P11484; -.
DR TopDownProteomics; P11484; -.
DR DNASU; 851369; -.
DR EnsemblFungi; YDL229W_mRNA; YDL229W; YDL229W.
DR GeneID; 851369; -.
DR KEGG; sce:YDL229W; -.
DR SGD; S000002388; SSB1.
DR VEuPathDB; FungiDB:YDL229W; -.
DR eggNOG; KOG0101; Eukaryota.
DR GeneTree; ENSGT00940000154813; -.
DR HOGENOM; CLU_005965_2_1_1; -.
DR InParanoid; P11484; -.
DR OMA; HQTTVQF; -.
DR BioCyc; YEAST:G3O-29608-MON; -.
DR EvolutionaryTrace; P11484; -.
DR PRO; PR:P11484; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P11484; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005886; C:plasma membrane; HDA:SGD.
DR GO; GO:0005844; C:polysome; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:SGD.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0005516; F:calmodulin binding; IDA:SGD.
DR GO; GO:0031072; F:heat shock protein binding; IBA:GO_Central.
DR GO; GO:0051787; F:misfolded protein binding; IBA:GO_Central.
DR GO; GO:0044183; F:protein folding chaperone; IBA:GO_Central.
DR GO; GO:0051082; F:unfolded protein binding; IDA:SGD.
DR GO; GO:0051083; P:'de novo' cotranslational protein folding; IDA:SGD.
DR GO; GO:0042149; P:cellular response to glucose starvation; IGI:SGD.
DR GO; GO:0034620; P:cellular response to unfolded protein; IBA:GO_Central.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR GO; GO:0002181; P:cytoplasmic translation; IMP:SGD.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR GO; GO:0006450; P:regulation of translational fidelity; IMP:SGD.
DR GO; GO:0000054; P:ribosomal subunit export from nucleus; IGI:SGD.
DR GO; GO:0006364; P:rRNA processing; IGI:SGD.
DR GO; GO:0006452; P:translational frameshifting; IMP:SGD.
DR GO; GO:0006415; P:translational termination; IMP:SGD.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 2.60.34.10; -; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR029048; HSP70_C_sf.
DR InterPro; IPR029047; HSP70_peptide-bd_sf.
DR InterPro; IPR013126; Hsp_70_fam.
DR PANTHER; PTHR19375; PTHR19375; 1.
DR Pfam; PF00012; HSP70; 1.
DR SUPFAM; SSF100920; SSF100920; 1.
DR SUPFAM; SSF100934; SSF100934; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR PROSITE; PS00297; HSP70_1; 1.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Chaperone; Cytoplasm;
KW Direct protein sequencing; Hydrolase; Nucleotide-binding; Phosphoprotein;
KW Protein biosynthesis; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9298649"
FT CHAIN 2..613
FT /note="Ribosome-associated molecular chaperone SSB1"
FT /id="PRO_0000078389"
FT REGION 2..391
FT /note="Nucleotide binding domain (NBD)"
FT /evidence="ECO:0000250|UniProtKB:G0SCU5"
FT REGION 392..402
FT /note="Inter-domain linker"
FT /evidence="ECO:0000250|UniProtKB:G0SCU5"
FT REGION 403..613
FT /note="Substrate binding domain (SBD)"
FT /evidence="ECO:0000250|UniProtKB:G0SCU5"
FT REGION 516..612
FT /note="Lid domain (SBDalpha)"
FT /evidence="ECO:0000250|UniProtKB:G0SCU5"
FT REGION 601..613
FT /note="Required for interaction with ribosomes"
FT /evidence="ECO:0000269|PubMed:27917864"
FT MOTIF 428..430
FT /note="Contributes to ribosome binding"
FT /evidence="ECO:0000269|PubMed:27917864"
FT MOTIF 574..582
FT /note="Nuclear export signal"
FT /evidence="ECO:0000305|PubMed:10347213"
FT BINDING 16..18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:G0SCU5"
FT BINDING 73
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:G0SCU5"
FT BINDING 205..207
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:G0SCU5"
FT BINDING 271..278
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:G0SCU5"
FT BINDING 342
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:G0SCU5"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:9298649"
FT MOD_RES 47
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 431
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MUTAGEN 73
FT /note="K->A: Unable to hydrolyze ATP and moderately reduces
FT ribosome binding."
FT /evidence="ECO:0000269|PubMed:27882919"
FT MUTAGEN 567..568
FT /note="KR->EE: In SSB1-L(BC): Reduces ribosome-binding to
FT less than 50%."
FT /evidence="ECO:0000269|PubMed:27882919"
FT MUTAGEN 596..597
FT /note="RK->DD: In SSB1-D1: Reduces ribosome-binding to less
FT than 50%."
FT /evidence="ECO:0000269|PubMed:27882919"
FT MUTAGEN 603..604
FT /note="KR->DD: In SSB1-D2: Reduces ribosome-binding to less
FT than 50%."
FT /evidence="ECO:0000269|PubMed:27882919"
FT CONFLICT 180..184
FT /note="AAAIA -> VVVIV (in Ref. 7; AAA34692)"
FT /evidence="ECO:0000305"
FT CONFLICT 189
FT /note="A -> V (in Ref. 7; AAA34692)"
FT /evidence="ECO:0000305"
FT CONFLICT 192
FT /note="S -> F (in Ref. 7; AAA34692)"
FT /evidence="ECO:0000305"
FT STRAND 10..13
FT /evidence="ECO:0007829|PDB:3GL1"
FT STRAND 16..30
FT /evidence="ECO:0007829|PDB:3GL1"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:3GL1"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:3GL1"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:3GL1"
FT HELIX 55..59
FT /evidence="ECO:0007829|PDB:3GL1"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:3GL1"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:3GL1"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:3GL1"
FT TURN 75..77
FT /evidence="ECO:0007829|PDB:3GL1"
FT HELIX 83..89
FT /evidence="ECO:0007829|PDB:3GL1"
FT STRAND 93..99
FT /evidence="ECO:0007829|PDB:3GL1"
FT STRAND 102..109
FT /evidence="ECO:0007829|PDB:3GL1"
FT STRAND 112..116
FT /evidence="ECO:0007829|PDB:3GL1"
FT HELIX 118..137
FT /evidence="ECO:0007829|PDB:3GL1"
FT STRAND 143..148
FT /evidence="ECO:0007829|PDB:3GL1"
FT HELIX 154..166
FT /evidence="ECO:0007829|PDB:3GL1"
FT STRAND 170..176
FT /evidence="ECO:0007829|PDB:3GL1"
FT HELIX 177..184
FT /evidence="ECO:0007829|PDB:3GL1"
FT TURN 185..190
FT /evidence="ECO:0007829|PDB:3GL1"
FT STRAND 196..203
FT /evidence="ECO:0007829|PDB:3GL1"
FT STRAND 208..216
FT /evidence="ECO:0007829|PDB:3GL1"
FT STRAND 219..228
FT /evidence="ECO:0007829|PDB:3GL1"
FT HELIX 233..252
FT /evidence="ECO:0007829|PDB:3GL1"
FT HELIX 260..276
FT /evidence="ECO:0007829|PDB:3GL1"
FT TURN 277..279
FT /evidence="ECO:0007829|PDB:3GL1"
FT STRAND 280..291
FT /evidence="ECO:0007829|PDB:3GL1"
FT STRAND 294..301
FT /evidence="ECO:0007829|PDB:3GL1"
FT HELIX 302..308
FT /evidence="ECO:0007829|PDB:3GL1"
FT HELIX 310..315
FT /evidence="ECO:0007829|PDB:3GL1"
FT HELIX 317..327
FT /evidence="ECO:0007829|PDB:3GL1"
FT HELIX 331..333
FT /evidence="ECO:0007829|PDB:3GL1"
FT STRAND 336..341
FT /evidence="ECO:0007829|PDB:3GL1"
FT HELIX 342..345
FT /evidence="ECO:0007829|PDB:3GL1"
FT HELIX 347..356
FT /evidence="ECO:0007829|PDB:3GL1"
FT TURN 357..359
FT /evidence="ECO:0007829|PDB:3GL1"
FT TURN 368..370
FT /evidence="ECO:0007829|PDB:3GL1"
FT HELIX 371..383
FT /evidence="ECO:0007829|PDB:3GL1"
SQ SEQUENCE 613 AA; 66602 MW; F16FA7C25A40321A CRC64;
MAEGVFQGAI GIDLGTTYSC VATYESSVEI IANEQGNRVT PSFVAFTPEE RLIGDAAKNQ
AALNPRNTVF DAKRLIGRRF DDESVQKDMK TWPFKVIDVD GNPVIEVQYL EETKTFSPQE
ISAMVLTKMK EIAEAKIGKK VEKAVITVPA YFNDAQRQAT KDAGAISGLN VLRIINEPTA
AAIAYGLGAG KSEKERHVLI FDLGGGTFDV SLLHIAGGVY TVKSTSGNTH LGGQDFDTNL
LEHFKAEFKK KTGLDISDDA RALRRLRTAA ERAKRTLSSV TQTTVEVDSL FDGEDFESSL
TRARFEDLNA ALFKSTLEPV EQVLKDAKIS KSQIDEVVLV GGSTRIPKVQ KLLSDFFDGK
QLEKSINPDE AVAYGAAVQG AILTGQSTSD ETKDLLLLDV APLSLGVGMQ GDMFGIVVPR
NTTVPTIKRR TFTTCADNQT TVQFPVYQGE RVNCKENTLL GEFDLKNIPM MPAGEPVLEA
IFEVDANGIL KVTAVEKSTG KSSNITISNA VGRLSSEEIE KMVNQAEEFK AADEAFAKKH
EARQRLESYV ASIEQTVTDP VLSSKLKRGS KSKIEAALSD ALAALQIEDP SADELRKAEV
GLKRVVTKAM SSR
