UniProtKB - P11484 (SSB1_YEAST)
Ribosome-associated molecular chaperone SSB1
SSB1
Functioni
Miscellaneous
Catalytic activityi
- EC:3.6.4.101 Publication
Kineticsi
- KM=270 µM for ATP (at 2.5 mM potassium acetate)1 Publication
- KM=147 µM for ATP (at 100 mM potassium acetate)1 Publication
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 73 | ATPBy similarity | 1 | |
Binding sitei | 342 | ATP; via amide nitrogenBy similarity | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 16 – 18 | ATPBy similarity | 3 | |
Nucleotide bindingi | 205 – 207 | ATPBy similarity | 3 | |
Nucleotide bindingi | 271 – 278 | ATPBy similarity | 8 |
GO - Molecular functioni
- ATPase activity Source: SGD
- ATP binding Source: GO_Central
- calmodulin binding Source: SGD
- heat shock protein binding Source: GO_Central
- misfolded protein binding Source: GO_Central
- protein folding chaperone Source: GO_Central
- unfolded protein binding Source: SGD
GO - Biological processi
- 'de novo' cotranslational protein folding Source: SGD
- cellular response to glucose starvation Source: SGD
- cellular response to unfolded protein Source: GO_Central
- chaperone cofactor-dependent protein refolding Source: GO_Central
- cytoplasmic translation Source: SGD
- protein refolding Source: GO_Central
- regulation of translational fidelity Source: SGD
- ribosomal subunit export from nucleus Source: SGD
- rRNA processing Source: SGD
- translational frameshifting Source: SGD
- translational termination Source: SGD
Keywordsi
Molecular function | Chaperone, Hydrolase |
Biological process | Protein biosynthesis |
Ligand | ATP-binding, Nucleotide-binding |
Names & Taxonomyi
Protein namesi | Recommended name: Ribosome-associated molecular chaperone SSB11 Publication (EC:3.6.4.101 Publication)Alternative name(s): Cold-inducible protein YG1011 Publication Heat shock protein SSB11 Publication Hsp70 chaperone Ssb1 Publication |
Gene namesi | Ordered Locus Names:YDL229WImported |
Organismi | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
Taxonomic identifieri | 559292 [NCBI] |
Taxonomic lineagei | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › |
Proteomesi |
|
Organism-specific databases
SGDi | S000002388, SSB1 |
VEuPathDBi | FungiDB:YDL229W |
Subcellular locationi
Cytoplasm and Cytosol
- Cytoplasm 1 Publication2 Publications
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.3 Publications
Plasma Membrane
- plasma membrane Source: SGD
Other locations
Keywords - Cellular componenti
CytoplasmPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 73 | K → A: Unable to hydrolyze ATP and moderately reduces ribosome binding. 1 Publication | 1 | |
Mutagenesisi | 567 – 568 | KR → EE in SSB1-L(BC): Reduces ribosome-binding to less than 50%. 1 Publication | 2 | |
Mutagenesisi | 596 – 597 | RK → DD in SSB1-D1: Reduces ribosome-binding to less than 50%. 1 Publication | 2 | |
Mutagenesisi | 603 – 604 | KR → DD in SSB1-D2: Reduces ribosome-binding to less than 50%. 1 Publication | 2 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed1 Publication | |||
ChainiPRO_0000078389 | 2 – 613 | Ribosome-associated molecular chaperone SSB1Add BLAST | 612 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 2 | N-acetylalanine1 Publication | 1 | |
Modified residuei | 47 | PhosphothreonineCombined sources | 1 | |
Modified residuei | 431 | PhosphothreonineCombined sources | 1 |
Keywords - PTMi
Acetylation, PhosphoproteinProteomic databases
MaxQBi | P11484 |
PaxDbi | P11484 |
PRIDEi | P11484 |
TopDownProteomicsi | P11484 |
2D gel databases
COMPLUYEAST-2DPAGEi | P11484 |
SWISS-2DPAGEi | P11484 |
UCD-2DPAGEi | P11484 |
PTM databases
CarbonylDBi | P11484 |
iPTMneti | P11484 |
Expressioni
Inductioni
Interactioni
Subunit structurei
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).
10 PublicationsBinary interactionsi
Hide detailsP11484
With | #Exp. | IntAct |
---|---|---|
BUD27 [P43573] | 3 | EBI-8627,EBI-22787 |
PFK26 [P40433] | 2 | EBI-8627,EBI-1956 |
SSE1 [P32589] | 2 | EBI-8627,EBI-8648 |
TOM71 [P38825] | 2 | EBI-8627,EBI-24694 |
GO - Molecular functioni
- calmodulin binding Source: SGD
- heat shock protein binding Source: GO_Central
- misfolded protein binding Source: GO_Central
- unfolded protein binding Source: SGD
Protein-protein interaction databases
BioGRIDi | 31882, 815 interactors |
DIPi | DIP-2254N |
IntActi | P11484, 779 interactors |
MINTi | P11484 |
STRINGi | 4932.YDL229W |
Miscellaneous databases
RNActi | P11484, protein |
Structurei
Secondary structure
3D structure databases
SMRi | P11484 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P11484 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 2 – 391 | Nucleotide binding domain (NBD)By similarityAdd BLAST | 390 | |
Regioni | 392 – 402 | Inter-domain linkerBy similarityAdd BLAST | 11 | |
Regioni | 403 – 613 | Substrate binding domain (SBD)By similarityAdd BLAST | 211 | |
Regioni | 516 – 612 | Lid domain (SBDalpha)By similarityAdd BLAST | 97 | |
Regioni | 601 – 613 | Required for interaction with ribosomes1 PublicationAdd BLAST | 13 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 428 – 430 | Contributes to ribosome binding1 Publication | 3 | |
Motifi | 574 – 582 | Nuclear export signal1 Publication | 9 |
Sequence similaritiesi
Phylogenomic databases
eggNOGi | KOG0101, Eukaryota |
GeneTreei | ENSGT00940000154813 |
HOGENOMi | CLU_005965_2_1_1 |
InParanoidi | P11484 |
OMAi | HQTTVQF |
Family and domain databases
Gene3Di | 1.20.1270.10, 1 hit 2.60.34.10, 1 hit |
InterProi | View protein in InterPro IPR043129, ATPase_NBD IPR018181, Heat_shock_70_CS IPR029048, HSP70_C_sf IPR029047, HSP70_peptide-bd_sf IPR013126, Hsp_70_fam |
PANTHERi | PTHR19375, PTHR19375, 1 hit |
Pfami | View protein in Pfam PF00012, HSP70, 1 hit |
SUPFAMi | SSF100920, SSF100920, 1 hit SSF100934, SSF100934, 1 hit SSF53067, SSF53067, 2 hits |
PROSITEi | View protein in PROSITE PS00297, HSP70_1, 1 hit PS00329, HSP70_2, 1 hit PS01036, HSP70_3, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
10 20 30 40 50
MAEGVFQGAI GIDLGTTYSC VATYESSVEI IANEQGNRVT PSFVAFTPEE
60 70 80 90 100
RLIGDAAKNQ AALNPRNTVF DAKRLIGRRF DDESVQKDMK TWPFKVIDVD
110 120 130 140 150
GNPVIEVQYL EETKTFSPQE ISAMVLTKMK EIAEAKIGKK VEKAVITVPA
160 170 180 190 200
YFNDAQRQAT KDAGAISGLN VLRIINEPTA AAIAYGLGAG KSEKERHVLI
210 220 230 240 250
FDLGGGTFDV SLLHIAGGVY TVKSTSGNTH LGGQDFDTNL LEHFKAEFKK
260 270 280 290 300
KTGLDISDDA RALRRLRTAA ERAKRTLSSV TQTTVEVDSL FDGEDFESSL
310 320 330 340 350
TRARFEDLNA ALFKSTLEPV EQVLKDAKIS KSQIDEVVLV GGSTRIPKVQ
360 370 380 390 400
KLLSDFFDGK QLEKSINPDE AVAYGAAVQG AILTGQSTSD ETKDLLLLDV
410 420 430 440 450
APLSLGVGMQ GDMFGIVVPR NTTVPTIKRR TFTTCADNQT TVQFPVYQGE
460 470 480 490 500
RVNCKENTLL GEFDLKNIPM MPAGEPVLEA IFEVDANGIL KVTAVEKSTG
510 520 530 540 550
KSSNITISNA VGRLSSEEIE KMVNQAEEFK AADEAFAKKH EARQRLESYV
560 570 580 590 600
ASIEQTVTDP VLSSKLKRGS KSKIEAALSD ALAALQIEDP SADELRKAEV
610
GLKRVVTKAM SSR
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 180 – 184 | AAAIA → VVVIV in AAA34692 (PubMed:6761581).Curated | 5 | |
Sequence conflicti | 189 | A → V in AAA34692 (PubMed:6761581).Curated | 1 | |
Sequence conflicti | 192 | S → F in AAA34692 (PubMed:6761581).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X13713 Genomic DNA Translation: CAA31995.1 M25395 mRNA Translation: AAA35099.1 Z74277 Genomic DNA Translation: CAA98807.1 M17585 Genomic DNA Translation: AAA34692.1 BK006938 Genomic DNA Translation: DAA11637.1 |
PIRi | S20149 |
RefSeqi | NP_010052.1, NM_001180289.1 |
Genome annotation databases
EnsemblFungii | YDL229W_mRNA; YDL229W; YDL229W |
GeneIDi | 851369 |
KEGGi | sce:YDL229W |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X13713 Genomic DNA Translation: CAA31995.1 M25395 mRNA Translation: AAA35099.1 Z74277 Genomic DNA Translation: CAA98807.1 M17585 Genomic DNA Translation: AAA34692.1 BK006938 Genomic DNA Translation: DAA11637.1 |
PIRi | S20149 |
RefSeqi | NP_010052.1, NM_001180289.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
3GL1 | X-ray | 1.92 | A/B | 1-384 | [»] | |
SMRi | P11484 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 31882, 815 interactors |
DIPi | DIP-2254N |
IntActi | P11484, 779 interactors |
MINTi | P11484 |
STRINGi | 4932.YDL229W |
PTM databases
CarbonylDBi | P11484 |
iPTMneti | P11484 |
2D gel databases
COMPLUYEAST-2DPAGEi | P11484 |
SWISS-2DPAGEi | P11484 |
UCD-2DPAGEi | P11484 |
Proteomic databases
MaxQBi | P11484 |
PaxDbi | P11484 |
PRIDEi | P11484 |
TopDownProteomicsi | P11484 |
Genome annotation databases
EnsemblFungii | YDL229W_mRNA; YDL229W; YDL229W |
GeneIDi | 851369 |
KEGGi | sce:YDL229W |
Organism-specific databases
SGDi | S000002388, SSB1 |
VEuPathDBi | FungiDB:YDL229W |
Phylogenomic databases
eggNOGi | KOG0101, Eukaryota |
GeneTreei | ENSGT00940000154813 |
HOGENOMi | CLU_005965_2_1_1 |
InParanoidi | P11484 |
OMAi | HQTTVQF |
Miscellaneous databases
EvolutionaryTracei | P11484 |
PROi | PR:P11484 |
RNActi | P11484, protein |
Family and domain databases
Gene3Di | 1.20.1270.10, 1 hit 2.60.34.10, 1 hit |
InterProi | View protein in InterPro IPR043129, ATPase_NBD IPR018181, Heat_shock_70_CS IPR029048, HSP70_C_sf IPR029047, HSP70_peptide-bd_sf IPR013126, Hsp_70_fam |
PANTHERi | PTHR19375, PTHR19375, 1 hit |
Pfami | View protein in Pfam PF00012, HSP70, 1 hit |
SUPFAMi | SSF100920, SSF100920, 1 hit SSF100934, SSF100934, 1 hit SSF53067, SSF53067, 2 hits |
PROSITEi | View protein in PROSITE PS00297, HSP70_1, 1 hit PS00329, HSP70_2, 1 hit PS01036, HSP70_3, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | SSB1_YEAST | |
Accessioni | P11484Primary (citable) accession number: P11484 Secondary accession number(s): D6VRC7, Q05834 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | October 1, 1989 |
Last sequence update: | January 23, 2007 | |
Last modified: | April 7, 2021 | |
This is version 208 of the entry and version 3 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Fungal Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- Yeast
Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD - Yeast chromosome IV
Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families