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Ribosome-associated molecular chaperone SSB2 (EC 3.6.4.10) (Heat shock protein SSB2) (Hsp70 chaperone Ssb)

 SSB2_YEAST              Reviewed;         613 AA.
P40150; D6W0Y1;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
05-DEC-2018, entry version 171.
RecName: Full=Ribosome-associated molecular chaperone SSB2 {ECO:0000303|PubMed:11739779};
EC=3.6.4.10;
AltName: Full=Heat shock protein SSB2 {ECO:0000303|PubMed:3302682};
AltName: Full=Hsp70 chaperone Ssb;
Name=SSB2 {ECO:0000303|PubMed:3302682};
Synonyms=YG103 {ECO:0000303|PubMed:6761581};
OrderedLocusNames=YNL209W {ECO:0000312|SGD:S000005153};
ORFNames=N1333;
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 96604 / S288c / FY1679;
PubMed=7725799; DOI=10.1002/yea.320101213;
Jonniaux J.-L., Coster F., Purnelle B., Goffeau A.;
"A 21.7 kb DNA segment on the left arm of yeast chromosome XIV carries
WHI3, GCR2, SPX18, SPX19, an homologue to the heat shock gene SSB1 and
8 new open reading frames of unknown function.";
Yeast 10:1639-1645(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169873;
Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F.,
Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M.,
Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N.,
Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D.,
Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A.,
Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A.,
Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C.,
Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M.,
Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J.,
Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L.,
Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M.,
Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P.,
Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A.,
Wambutt R., Wedler H., Zollner A., Hani J.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV
and its evolutionary implications.";
Nature 387:93-98(1997).
[3]
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).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 444-535.
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).
[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]
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).
[7]
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).
[8]
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).
[9]
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).
[10]
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).
[11]
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).
[12]
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).
[13]
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).
[14]
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).
[15]
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).
[16]
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).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-47, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=YAL6B;
PubMed=15665377; DOI=10.1074/mcp.M400219-MCP200;
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,
Mann M., Jensen O.N.;
"Quantitative phosphoproteomics applied to the yeast pheromone
signaling pathway.";
Mol. Cell. Proteomics 4:310-327(2005).
[18]
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).
[19]
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).
[20]
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).
[21]
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).
-!- 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:9670014}.
-!- CATALYTIC ACTIVITY:
Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.10;
Evidence={ECO:0000250|UniProtKB:P11484};
-!- 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 (By similarity). Directly interacts with nascent
polypeptides. This interaction is dependent on the ribosome-
associated complex (RAC) (PubMed:11929994, PubMed:23332755).
Interacts with SSE1 (PubMed:23332755).
{ECO:0000250|UniProtKB:P11484, ECO:0000269|PubMed:11929994,
ECO:0000269|PubMed:1394434, ECO:0000269|PubMed:23332755,
ECO:0000269|PubMed:27917864, ECO:0000269|PubMed:9670014}.
-!- SUBCELLULAR LOCATION: Cytoplasm {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). Up-regulated
upon carbon upshift and down-regulated upon amino acid limitation
in an HSF1-dependent manner (PubMed:10322015). Interacts with SSE1
(PubMed:16219770, PubMed:16221677). Interacts with FES1 (By
similarity). {ECO:0000250|UniProtKB:P11484,
ECO:0000269|PubMed:10322015, ECO:0000269|PubMed:16219770,
ECO:0000269|PubMed:16221677, ECO:0000269|PubMed:2651414,
ECO:0000269|PubMed:6761581}.
-!- MISCELLANEOUS: Present with 104000 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; X78898; CAA55498.1; -; Genomic_DNA.
EMBL; Z71485; CAA96111.1; -; Genomic_DNA.
EMBL; M17586; AAA34693.1; -; Genomic_DNA.
EMBL; BK006947; DAA10347.1; -; Genomic_DNA.
PIR; S50721; S50721.
RefSeq; NP_014190.1; NM_001183047.1.
ProteinModelPortal; P40150; -.
SMR; P40150; -.
BioGrid; 35627; 2084.
DIP; DIP-7126N; -.
IntAct; P40150; 115.
MINT; P40150; -.
STRING; 4932.YNL209W; -.
iPTMnet; P40150; -.
COMPLUYEAST-2DPAGE; P40150; -.
MaxQB; P40150; -.
PaxDb; P40150; -.
PRIDE; P40150; -.
TopDownProteomics; P40150; -.
EnsemblFungi; YNL209W_mRNA; YNL209W_mRNA; YNL209W.
GeneID; 855512; -.
KEGG; sce:YNL209W; -.
SGD; S000005153; SSB2.
GeneTree; ENSGT00940000154813; -.
HOGENOM; HOG000228135; -.
InParanoid; P40150; -.
KO; K03283; -.
OMA; ATIERHC; -.
OrthoDB; EOG092C1VPN; -.
BioCyc; YEAST:G3O-33215-MONOMER; -.
Reactome; R-SCE-3371453; Regulation of HSF1-mediated heat shock response.
PRO; PR:P40150; -.
Proteomes; UP000002311; Chromosome XIV.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0010494; C:cytoplasmic stress granule; IDA:SGD.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0005844; C:polysome; IDA:SGD.
GO; GO:0005524; F:ATP binding; IBA:GO_Central.
GO; GO:0016887; F:ATPase activity; IDA:SGD.
GO; GO:0042623; F:ATPase activity, coupled; IBA:GO_Central.
GO; GO:0031072; F:heat shock protein binding; IBA:GO_Central.
GO; GO:0051787; F:misfolded protein binding; IBA:GO_Central.
GO; GO:0044183; F:protein binding involved in protein folding; IBA:GO_Central.
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:0034605; P:cellular response to heat; IBA:GO_Central.
GO; GO:0034620; P:cellular response to unfolded protein; IBA:GO_Central.
GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
GO; GO:0002181; P:cytoplasmic translation; IMP:SGD.
GO; GO:0042026; P:protein refolding; IBA:GO_Central.
GO; GO:0006450; P:regulation of translational fidelity; IMP:SGD.
GO; GO:0006986; P:response to unfolded protein; IBA:GO_Central.
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; IBA:GO_Central.
Gene3D; 1.20.1270.10; -; 1.
Gene3D; 2.60.34.10; -; 1.
InterPro; IPR018181; Heat_shock_70_CS.
InterPro; IPR029048; HSP70_C_sf.
InterPro; IPR029047; HSP70_peptide-bd_sf.
InterPro; IPR013126; Hsp_70_fam.
PANTHER; PTHR19375; PTHR19375; 1.
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;
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
SSB2.
/FTId=PRO_0000078390.
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:0000250|UniProtKB:P11484}.
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:15665377,
ECO:0000244|PubMed:18407956}.
MOD_RES 431 431 Phosphothreonine.
{ECO:0000250|UniProtKB:P11484}.
SEQUENCE 613 AA; 66595 MW; E1040A011346D953 CRC64;
MAEGVFQGAI GIDLGTTYSC VATYESSVEI IANEQGNRVT PSFVAFTPQE 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 GDIFGIVVPR
NTTVPTIKRR TFTTVSDNQT TVQFPVYQGE RVNCKENTLL GEFDLKNIPM MPAGEPVLEA
IFEVDANGIL KVTAVEKSTG KSSNITISNA VGRLSSEEIE KMVNQAEEFK AADEAFAKKH
EARQRLESYV ASIEQTVTDP VLSSKLKRGS KSKIEAALSD ALAALQIEDP SADELRKAEV
GLKRVVTKAM SSR


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U0873h CLIA Heat shock 70 kDa protein 1_2,Heat shock 70 kDa protein 1A_1B,Homo sapiens,HSP70.1_HSP70.2,HSP70-1_HSP70-2,HSPA1,HSPA1A,Human 96T
E0873h ELISA kit Heat shock 70 kDa protein 1_2,Heat shock 70 kDa protein 1A_1B,Homo sapiens,HSP70.1_HSP70.2,HSP70-1_HSP70-2,HSPA1,HSPA1A,Human 96T


 

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