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Ribosome-associated molecular chaperone SSB1 (EC 3.6.4.10) (Cold-inducible protein YG101) (Heat shock protein SSB1) (Hsp70 chaperone Ssb)

 SSB1_YEAST              Reviewed;         613 AA.
P11484; D6VRC7; Q05834;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
25-OCT-2017, entry version 178.
RecName: Full=Ribosome-associated molecular chaperone SSB1 {ECO:0000303|PubMed:11739779};
EC=3.6.4.10 {ECO:0000269|PubMed:9860955};
AltName: Full=Cold-inducible protein YG101 {ECO:0000303|PubMed:6761581};
AltName: Full=Heat shock protein SSB1 {ECO:0000303|PubMed:3302682};
AltName: Full=Hsp70 chaperone Ssb {ECO:0000303|PubMed:8994035};
Name=SSB1 {ECO:0000303|PubMed:3302682};
Synonyms=YG101 {ECO:0000303|PubMed:6761581};
OrderedLocusNames=YDL229W {ECO:0000312|SGD:S000002388};
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=2664714; DOI=10.1093/nar/17.12.4891;
Slater M.R., Craig E.A.;
"The SSB1 heat shock cognate gene of the yeast Saccharomyces
cerevisiae.";
Nucleic Acids Res. 17:4891-4891(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2661019; DOI=10.1016/0092-8674(89)90059-7;
Normington K., Kohno K., Kozutsumi Y., Gething M.J., Sambrook J.;
"S. cerevisiae encodes an essential protein homologous in sequence and
function to mammalian BiP.";
Cell 57:1223-1236(1989).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169867;
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N.,
Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M.,
Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L.,
Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M.,
Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S.,
Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M.,
Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S.,
Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K.,
Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D.,
Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C.,
Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T.,
Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E.,
Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W.,
Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K.,
Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S.,
Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A.,
Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S.,
Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M.,
Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y.,
Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M.,
Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E.,
Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R.,
Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
Mewes H.-W., Zollner A., Zaccaria P.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
Nature 387:75-78(1997).
[4]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[5]
PROTEIN SEQUENCE OF 39-49 AND 431-439.
STRAIN=ATCC 38531 / Y41;
PubMed=7737086; DOI=10.1002/elps.1150160124;
Norbeck J., Blomberg A.;
"Gene linkage of two-dimensional polyacrylamide gel electrophoresis
resolved proteins from isogene families in Saccharomyces cerevisiae by
microsequencing of in-gel trypsin generated peptides.";
Electrophoresis 16:149-156(1995).
[6]
PROTEIN SEQUENCE OF 145-159.
STRAIN=ATCC 204508 / S288c;
PubMed=7895733; DOI=10.1002/elps.11501501210;
Garrels J.I., Futcher B., Kobayashi R., Latter G.I., Schwender B.,
Volpe T., Warner J.R., McLaughlin C.S.;
"Protein identifications for a Saccharomyces cerevisiae protein
database.";
Electrophoresis 15:1466-1486(1994).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 180-403, AND INDUCTION.
PubMed=6761581; DOI=10.1128/MCB.2.11.1388;
Ingolia T.D., Slater M.R., Craig E.A.;
"Saccharomyces cerevisiae contains a complex multigene family related
to the major heat shock-inducible gene of Drosophila.";
Mol. Cell. Biol. 2:1388-1398(1982).
[8]
GENE FAMILY.
PubMed=3302682; DOI=10.1128/MCB.7.7.2568;
Werner-Washburne M., Stone D.E., Craig E.A.;
"Complex interactions among members of an essential subfamily of hsp70
genes in Saccharomyces cerevisiae.";
Mol. Cell. Biol. 7:2568-2577(1987).
[9]
INDUCTION.
PubMed=2651414; DOI=10.1128/jb.171.5.2680-2688.1989;
Werner-Washburne M., Becker J., Kosic-Smithers J., Craig E.A.;
"Yeast Hsp70 RNA levels vary in response to the physiological status
of the cell.";
J. Bacteriol. 171:2680-2688(1989).
[10]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=1394434; DOI=10.1016/0092-8674(92)90269-I;
Nelson R.J., Ziegelhoffer T., Nicolet C., Werner-Washburne M.,
Craig E.A.;
"The translation machinery and 70 kd heat shock protein cooperate in
protein synthesis.";
Cell 71:97-105(1992).
[11]
INDUCTION.
PubMed=7646503; DOI=10.1006/bbrc.1995.2157;
Iwahashi H., Wu Y., Tanguay R.M.;
"Detection and expression of the 70 kDa heat shock protein SSB1P at
different temperatures in Saccharomyces cerevisiae.";
Biochem. Biophys. Res. Commun. 213:484-489(1995).
[12]
ACETYLATION AT ALA-2.
PubMed=9298649; DOI=10.1002/elps.1150180810;
Garrels J.I., McLaughlin C.S., Warner J.R., Futcher B., Latter G.I.,
Kobayashi R., Schwender B., Volpe T., Anderson D.S.,
Mesquita-Fuentes R., Payne W.E.;
"Proteome studies of Saccharomyces cerevisiae: identification and
characterization of abundant proteins.";
Electrophoresis 18:1347-1360(1997).
[13]
FUNCTION.
PubMed=8994035; DOI=10.1126/science.275.5298.387;
James P., Pfund C., Craig E.A.;
"Functional specificity among Hsp70 molecular chaperones.";
Science 275:387-389(1997).
[14]
FUNCTION, AND SUBUNIT.
PubMed=9670014; DOI=10.1093/emboj/17.14.3981;
Pfund C., Lopez-Hoyo N., Ziegelhoffer T., Schilke B.A.,
Lopez-Buesa P., Walter W.A., Wiedmann M., Craig E.A.;
"The molecular chaperone Ssb from Saccharomyces cerevisiae is a
component of the ribosome-nascent chain complex.";
EMBO J. 17:3981-3989(1998).
[15]
BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=9860955; DOI=10.1073/pnas.95.26.15253;
Lopez-Buesa P., Pfund C., Craig E.A.;
"The biochemical properties of the ATPase activity of a 70-kDa heat
shock protein (Hsp70) are governed by the C-terminal domains.";
Proc. Natl. Acad. Sci. U.S.A. 95:15253-15258(1998).
[16]
INDUCTION.
PubMed=10322015;
Lopez N., Halladay J., Walter W., Craig E.A.;
"SSB, encoding a ribosome-associated chaperone, is coordinately
regulated with ribosomal protein genes.";
J. Bacteriol. 181:3136-3143(1999).
[17]
SUBCELLULAR LOCATION.
PubMed=10347213; DOI=10.1074/jbc.274.23.16501;
Shulga N., James P., Craig E.A., Goldfarb D.S.;
"A nuclear export signal prevents Saccharomyces cerevisiae Hsp70 Ssb1p
from stimulating nuclear localization signal-directed nuclear
transport.";
J. Biol. Chem. 274:16501-16507(1999).
[18]
FUNCTION.
PubMed=11739779; DOI=10.1091/mbc.12.12.3773;
Pfund C., Huang P., Lopez-Hoyo N., Craig E.A.;
"Divergent functional properties of the ribosome-associated molecular
chaperone Ssb compared with other Hsp70s.";
Mol. Biol. Cell 12:3773-3782(2001).
[19]
FUNCTION, AND SUBUNIT.
PubMed=11929994; DOI=10.1073/pnas.062048599;
Gautschi M., Mun A., Ross S., Rospert S.;
"A functional chaperone triad on the yeast ribosome.";
Proc. Natl. Acad. Sci. U.S.A. 99:4209-4214(2002).
[20]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[21]
FUNCTION, AND INTERACTION WITH SSE1.
PubMed=16219770; DOI=10.1074/jbc.M503615200;
Yam A.Y., Albanese V., Lin H.T., Frydman J.;
"Hsp110 cooperates with different cytosolic HSP70 systems in a pathway
for de novo folding.";
J. Biol. Chem. 280:41252-41261(2005).
[22]
FUNCTION, AND INTERACTION WITH SSE1.
PubMed=16221677; DOI=10.1074/jbc.M503614200;
Shaner L., Wegele H., Buchner J., Morano K.A.;
"The yeast Hsp110 Sse1 functionally interacts with the Hsp70
chaperones Ssa and Ssb.";
J. Biol. Chem. 280:41262-41269(2005).
[23]
INTERACTION WITH FES1.
PubMed=17132105; DOI=10.1515/BC.2006.198;
Dragovic Z., Shomura Y., Tzvetkov N., Hartl F.U., Bracher A.;
"Fes1p acts as a nucleotide exchange factor for the ribosome-
associated molecular chaperone Ssb1p.";
Biol. Chem. 387:1593-1600(2006).
[24]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[25]
INTERACTION WITH NAP1, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=18086883; DOI=10.1128/MCB.01035-07;
Calvert M.E.K., Keck K.M., Ptak C., Shabanowitz J., Hunt D.F.,
Pemberton L.F.;
"Phosphorylation by casein kinase 2 regulates Nap1 localization and
function.";
Mol. Cell. Biol. 28:1313-1325(2008).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-47, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-431, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
[28]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH RAC AND SSE1.
PubMed=23332755; DOI=10.1016/j.cell.2012.12.001;
Willmund F., del Alamo M., Pechmann S., Chen T., Albanese V.,
Dammer E.B., Peng J., Frydman J.;
"The cotranslational function of ribosome-associated Hsp70 in
eukaryotic protein homeostasis.";
Cell 152:196-209(2013).
[29]
INTERACTION WITH RPL35; RPL39 AND RPL19, AND MUTAGENESIS OF
567-LYS-ARG-568; 596-ARG-LYS-597 AND 603-LYS-ARG-604.
PubMed=27882919; DOI=10.1038/ncomms13563;
Gumiero A., Conz C., Gese G.V., Zhang Y., Weyer F.A., Lapouge K.,
Kappes J., von Plehwe U., Schermann G., Fitzke E., Woelfle T.,
Fischer T., Rospert S., Sinning I.;
"Interaction of the cotranslational Hsp70 Ssb with ribosomal proteins
and rRNA depends on its lid domain.";
Nat. Commun. 7:13563-13563(2016).
[30]
SUBUNIT.
PubMed=27917864; DOI=10.1038/ncomms13695;
Hanebuth M.A., Kityk R., Fries S.J., Jain A., Kriel A., Albanese V.,
Frickey T., Peter C., Mayer M.P., Frydman J., Deuerling E.;
"Multivalent contacts of the Hsp70 Ssb contribute to its architecture
on ribosomes and nascent chain interaction.";
Nat. Commun. 7:13695-13695(2016).
[31]
X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) OF 1-384.
Osipiuk J., Li H., Bargassa M., Sahi C., Craig E.A., Joachimiak A.;
"Crystal structure of ATPase domain of Ssb1 chaperone, member of the
HSP70 family from Saccharomyces cerevisiae.";
Submitted (MAR-2009) to the PDB data bank.
-!- FUNCTION: Ribosome-bound, Hsp70-type chaperone that assists in the
cotranslational folding of newly synthesized proteins in the
cytosol. Stimulates folding by interacting with nascent chains,
binding to short, largely hydrophobic sequences exposed by
unfolded proteins, thereby stabilizing longer, more slowly
translated, and aggregation-prone nascent polypeptides and domains
that cannot fold stably until fully synthesized. The Hsp70-protein
substrate interaction depends on ATP-binding and on allosteric
regulation between the NBD and the SBD. The ATP-bound state is
characterized by a fast exchange rate of substrate (low affinity
state), while in the ADP-bound state exchange is much slower (high
affinity state). During the Hsp70 cycle, the chaperone switches
between the ATP-bound state (open conformation) and the ADP-bound
state (closed conformation) by major conformational rearrangements
involving mainly the lid domain. Ssb cooperates with a specific
Hsp40/Hsp70 co-chaperone termed the ribosome-associated complex
(RAC), which stimulates the ATPase activity of the ribosome-
associated pool of Ssbs and switches it to the high affinity
substrate binding state. Hsp110 chaperone SSE1 and FES1 act as
nucleotide exchange factors that cause substrate release.
{ECO:0000269|PubMed:11739779, ECO:0000269|PubMed:11929994,
ECO:0000269|PubMed:1394434, ECO:0000269|PubMed:16219770,
ECO:0000269|PubMed:16221677, ECO:0000269|PubMed:23332755,
ECO:0000269|PubMed:8994035, ECO:0000269|PubMed:9670014}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
{ECO:0000269|PubMed:9860955}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=270 uM for ATP (at 2.5 mM potassium acetate)
{ECO:0000269|PubMed:9860955};
KM=147 uM for ATP (at 100 mM potassium acetate)
{ECO:0000269|PubMed:9860955};
Note=kcat is 0.95 min(-1) with ATP as substrate (at 2.5 mM
potassium acetate) and 0.81 min(-1) with ATP as substrate (at
100 mM potassium acetate). {ECO:0000269|PubMed:9860955};
-!- SUBUNIT: Binds to ribosomes (PubMed:9670014, PubMed:1394434,
PubMed:27917864). Binds close to the ribosomal tunnel exit via
contacts with both ribosomal proteins RPL35, RPL39 and RPL19, and
rRNA (PubMed:27882919). Directly interacts with nascent
polypeptides. This interaction is dependent on the ribosome-
associated complex (RAC) (PubMed:11929994, PubMed:23332755).
Interacts with SSE1 (PubMed:16219770, PubMed:16221677,
PubMed:23332755). Interacts with FES1 (PubMed:17132105). Interacts
with NAP1 (PubMed:18086883). {ECO:0000269|PubMed:11929994,
ECO:0000269|PubMed:1394434, ECO:0000269|PubMed:16219770,
ECO:0000269|PubMed:16221677, ECO:0000269|PubMed:17132105,
ECO:0000269|PubMed:18086883, ECO:0000269|PubMed:23332755,
ECO:0000269|PubMed:27882919, ECO:0000269|PubMed:27917864,
ECO:0000269|PubMed:9670014}.
-!- INTERACTION:
P43573:BUD27; NbExp=3; IntAct=EBI-8627, EBI-22787;
P40433:PFK26; NbExp=2; IntAct=EBI-8627, EBI-1956;
P32589:SSE1; NbExp=2; IntAct=EBI-8627, EBI-8648;
P38825:TOM71; NbExp=2; IntAct=EBI-8627, EBI-24694;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10347213,
ECO:0000269|PubMed:23332755, ECO:0000305|PubMed:1394434}.
Note=About 50% of the protein is associated with translating
ribosomes, but sufficient Ssb exists in the cell for each ribosome
to be associated with at least one Ssb molecule.
{ECO:0000269|PubMed:1394434, ECO:0000269|PubMed:23332755,
ECO:0000269|PubMed:9670014}.
-!- INDUCTION: Expression decreases after heat shock or during growth
to stationary phase (PubMed:6761581, PubMed:2651414). Degraded
during heat shock treatment (at protein level) (PubMed:7646503).
Up-regulated upon carbon upshift and down-regulated upon amino
acid limitation in an HSF1-dependent manner (PubMed:10322015).
{ECO:0000269|PubMed:10322015, ECO:0000269|PubMed:2651414,
ECO:0000269|PubMed:6761581, ECO:0000269|PubMed:7646503}.
-!- MISCELLANEOUS: Present with 170000 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the heat shock protein 70 family. Ssb-type
Hsp70 subfamily. {ECO:0000305}.
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EMBL; X13713; CAA31995.1; -; Genomic_DNA.
EMBL; M25395; AAA35099.1; -; mRNA.
EMBL; Z74277; CAA98807.1; -; Genomic_DNA.
EMBL; M17585; AAA34692.1; -; Genomic_DNA.
EMBL; BK006938; DAA11637.1; -; Genomic_DNA.
PIR; S20149; S20149.
RefSeq; NP_010052.1; NM_001180289.1.
PDB; 3GL1; X-ray; 1.92 A; A/B=1-384.
PDBsum; 3GL1; -.
ProteinModelPortal; P11484; -.
SMR; P11484; -.
BioGrid; 31882; 772.
DIP; DIP-2254N; -.
IntAct; P11484; 776.
MINT; MINT-1325604; -.
STRING; 4932.YDL229W; -.
iPTMnet; P11484; -.
COMPLUYEAST-2DPAGE; P11484; -.
SWISS-2DPAGE; P11484; -.
UCD-2DPAGE; P11484; -.
MaxQB; P11484; -.
PRIDE; P11484; -.
TopDownProteomics; P11484; -.
EnsemblFungi; YDL229W; YDL229W; YDL229W.
GeneID; 851369; -.
KEGG; sce:YDL229W; -.
EuPathDB; FungiDB:YDL229W; -.
SGD; S000002388; SSB1.
GeneTree; ENSGT00900000141154; -.
HOGENOM; HOG000228135; -.
InParanoid; P11484; -.
OMA; FEEINST; -.
OrthoDB; EOG092C1VPN; -.
BioCyc; YEAST:G3O-29608-MONOMER; -.
EvolutionaryTrace; P11484; -.
PRO; PR:P11484; -.
Proteomes; UP000002311; Chromosome IV.
GO; GO:0005737; C:cytoplasm; IDA:SGD.
GO; GO:0005844; C:polysome; IDA:SGD.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016887; F:ATPase activity; IDA:SGD.
GO; GO:0005516; F:calmodulin binding; IDA:SGD.
GO; GO:0051082; F:unfolded protein binding; IDA:SGD.
GO; GO:0051083; P:'de novo' cotranslational protein folding; IDA:SGD.
GO; GO:0042149; P:cellular response to glucose starvation; IGI:SGD.
GO; GO:0002181; P:cytoplasmic translation; IMP:SGD.
GO; GO:0006450; P:regulation of translational fidelity; IMP:SGD.
GO; GO:0000054; P:ribosomal subunit export from nucleus; IGI:SGD.
GO; GO:0006364; P:rRNA processing; IGI:SGD.
GO; GO:0006452; P:translational frameshifting; IMP:SGD.
GO; GO:0006415; P:translational termination; IMP:SGD.
Gene3D; 1.20.1270.10; -; 1.
Gene3D; 2.60.34.10; -; 1.
InterPro; IPR018181; Heat_shock_70_CS.
InterPro; IPR029048; HSP70_C.
InterPro; IPR029047; HSP70_peptide-bd.
InterPro; IPR013126; Hsp_70_fam.
Pfam; PF00012; HSP70; 1.
PRINTS; PR00301; HEATSHOCK70.
SUPFAM; SSF100920; SSF100920; 1.
SUPFAM; SSF100934; SSF100934; 1.
PROSITE; PS00297; HSP70_1; 1.
PROSITE; PS00329; HSP70_2; 1.
PROSITE; PS01036; HSP70_3; 1.
1: Evidence at protein level;
3D-structure; Acetylation; ATP-binding; Chaperone; Complete proteome;
Cytoplasm; Direct protein sequencing; Hydrolase; Nucleotide-binding;
Phosphoprotein; Protein biosynthesis; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:9298649}.
CHAIN 2 613 Ribosome-associated molecular chaperone
SSB1.
/FTId=PRO_0000078389.
NP_BIND 16 18 ATP. {ECO:0000250|UniProtKB:G0SCU5}.
NP_BIND 205 207 ATP. {ECO:0000250|UniProtKB:G0SCU5}.
NP_BIND 271 278 ATP. {ECO:0000250|UniProtKB:G0SCU5}.
REGION 2 391 Nucleotide binding domain (NBD).
{ECO:0000250|UniProtKB:G0SCU5}.
REGION 392 402 Inter-domain linker.
{ECO:0000250|UniProtKB:G0SCU5}.
REGION 403 613 Substrate binding domain (SBD).
{ECO:0000250|UniProtKB:G0SCU5}.
REGION 516 612 Lid domain (SBDalpha).
{ECO:0000250|UniProtKB:G0SCU5}.
REGION 601 613 Required for interaction with ribosomes.
{ECO:0000269|PubMed:27917864}.
MOTIF 428 430 Contributes to ribosome binding.
{ECO:0000269|PubMed:27917864}.
MOTIF 574 582 Nuclear export signal.
{ECO:0000305|PubMed:10347213}.
BINDING 73 73 ATP. {ECO:0000250|UniProtKB:G0SCU5}.
BINDING 342 342 ATP; via amide nitrogen.
{ECO:0000250|UniProtKB:G0SCU5}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000269|PubMed:9298649}.
MOD_RES 47 47 Phosphothreonine.
{ECO:0000244|PubMed:18407956}.
MOD_RES 431 431 Phosphothreonine.
{ECO:0000244|PubMed:19779198}.
MUTAGEN 73 73 K->A: Unable to hydrolyze ATP and
moderately reduces ribosome binding.
{ECO:0000269|PubMed:27882919}.
MUTAGEN 567 568 KR->EE: In SSB1-L(BC): Reduces ribosome-
binding to less than 50%.
{ECO:0000269|PubMed:27882919}.
MUTAGEN 596 597 RK->DD: In SSB1-D1: Reduces ribosome-
binding to less than 50%.
{ECO:0000269|PubMed:27882919}.
MUTAGEN 603 604 KR->DD: In SSB1-D2: Reduces ribosome-
binding to less than 50%.
{ECO:0000269|PubMed:27882919}.
CONFLICT 180 184 AAAIA -> VVVIV (in Ref. 7; AAA34692).
{ECO:0000305}.
CONFLICT 189 189 A -> V (in Ref. 7; AAA34692).
{ECO:0000305}.
CONFLICT 192 192 S -> F (in Ref. 7; AAA34692).
{ECO:0000305}.
STRAND 10 13 {ECO:0000244|PDB:3GL1}.
STRAND 16 30 {ECO:0000244|PDB:3GL1}.
STRAND 38 41 {ECO:0000244|PDB:3GL1}.
STRAND 44 46 {ECO:0000244|PDB:3GL1}.
STRAND 51 54 {ECO:0000244|PDB:3GL1}.
HELIX 55 59 {ECO:0000244|PDB:3GL1}.
HELIX 61 63 {ECO:0000244|PDB:3GL1}.
HELIX 65 67 {ECO:0000244|PDB:3GL1}.
HELIX 72 74 {ECO:0000244|PDB:3GL1}.
TURN 75 77 {ECO:0000244|PDB:3GL1}.
HELIX 83 89 {ECO:0000244|PDB:3GL1}.
STRAND 93 99 {ECO:0000244|PDB:3GL1}.
STRAND 102 109 {ECO:0000244|PDB:3GL1}.
STRAND 112 116 {ECO:0000244|PDB:3GL1}.
HELIX 118 137 {ECO:0000244|PDB:3GL1}.
STRAND 143 148 {ECO:0000244|PDB:3GL1}.
HELIX 154 166 {ECO:0000244|PDB:3GL1}.
STRAND 170 176 {ECO:0000244|PDB:3GL1}.
HELIX 177 184 {ECO:0000244|PDB:3GL1}.
TURN 185 190 {ECO:0000244|PDB:3GL1}.
STRAND 196 203 {ECO:0000244|PDB:3GL1}.
STRAND 208 216 {ECO:0000244|PDB:3GL1}.
STRAND 219 228 {ECO:0000244|PDB:3GL1}.
HELIX 233 252 {ECO:0000244|PDB:3GL1}.
HELIX 260 276 {ECO:0000244|PDB:3GL1}.
TURN 277 279 {ECO:0000244|PDB:3GL1}.
STRAND 280 291 {ECO:0000244|PDB:3GL1}.
STRAND 294 301 {ECO:0000244|PDB:3GL1}.
HELIX 302 308 {ECO:0000244|PDB:3GL1}.
HELIX 310 315 {ECO:0000244|PDB:3GL1}.
HELIX 317 327 {ECO:0000244|PDB:3GL1}.
HELIX 331 333 {ECO:0000244|PDB:3GL1}.
STRAND 336 341 {ECO:0000244|PDB:3GL1}.
HELIX 342 345 {ECO:0000244|PDB:3GL1}.
HELIX 347 356 {ECO:0000244|PDB:3GL1}.
TURN 357 359 {ECO:0000244|PDB:3GL1}.
TURN 368 370 {ECO:0000244|PDB:3GL1}.
HELIX 371 383 {ECO:0000244|PDB:3GL1}.
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


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