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Protein

Ribosome-associated molecular chaperone SSB1

Gene

SSB1

Organism
Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) (Yeast) (Eremothecium gossypii)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

Functioni

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.By similarity

Catalytic activityi

ATP + H2O = ADP + phosphate.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei73ATPBy similarity1
Binding sitei342ATP; via amide nitrogenBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi16 – 18ATPBy similarity3
Nucleotide bindingi205 – 207ATPBy similarity3
Nucleotide bindingi271 – 278ATPBy similarity8

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionChaperone, Hydrolase
Biological processProtein biosynthesis
LigandATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Ribosome-associated molecular chaperone SSB1 (EC:3.6.4.10)
Alternative name(s):
Heat shock protein SSB1
Hsp70 chaperone Ssb
Gene namesi
Name:SSB1
Ordered Locus Names:ABL174C
OrganismiAshbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) (Yeast) (Eremothecium gossypii)
Taxonomic identifieri284811 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeEremothecium
Proteomesi
  • UP000000591 Componenti: Chromosome II

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000783611 – 613Ribosome-associated molecular chaperone SSB1Add BLAST613

Proteomic databases

PRIDEiQ75E44

Interactioni

Subunit structurei

Binds to ribosomes. Binds close to the ribosomal tunnel exit via contacts with both ribosomal proteins and rRNA. Directly interacts with nascent polypeptides. This interaction is dependent on the ribosome-associated complex (RAC). Interacts with SSE1. Interacts with FES1.By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi33169.AAS50597

Structurei

3D structure databases

ProteinModelPortaliQ75E44
SMRiQ75E44
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 391Nucleotide binding domain (NBD)By similarityAdd BLAST391
Regioni392 – 402Inter-domain linkerBy similarityAdd BLAST11
Regioni403 – 613Substrate binding domain (SBD)By similarityAdd BLAST211
Regioni516 – 612Lid domain (SBDalpha)By similarityAdd BLAST97

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi574 – 582Nuclear export signalBy similarity9

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000228135
InParanoidiQ75E44
KOiK03283
OMAiDFSARHE
OrthoDBiEOG092C1VPN

Family and domain databases

Gene3Di1.20.1270.10, 1 hit
2.60.34.10, 1 hit
InterProiView protein in InterPro
IPR018181 Heat_shock_70_CS
IPR029048 HSP70_C_sf
IPR029047 HSP70_peptide-bd_sf
IPR013126 Hsp_70_fam
PANTHERiPTHR19375 PTHR19375, 1 hit
PfamiView protein in Pfam
PF00012 HSP70, 1 hit
PRINTSiPR00301 HEATSHOCK70
SUPFAMiSSF100920 SSF100920, 1 hit
SSF100934 SSF100934, 1 hit
PROSITEiView protein in PROSITE
PS00297 HSP70_1, 1 hit
PS00329 HSP70_2, 1 hit
PS01036 HSP70_3, 1 hit

Sequencei

Sequence statusi: Complete.

Q75E44-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAEGVFSGAI GIDLGTTYSC VATYESSVEI IANEQGNRVT PSFVAFTPEE
60 70 80 90 100
RLIGDAAKNQ AALNPRNTVF DAKRLIGRRF DDESVQSDMK TWPFKVIDAN
110 120 130 140 150
GSPMIEVEYL GETKSFSPQE ISAMVLTKMK EIAEAKIGKK VEKAVITVPA
160 170 180 190 200
YFNDAQRQAT KDAGAIAGLN VLRIINEPTA AAIAYGLGAG KSEKERHVLI
210 220 230 240 250
FDLGGGTFDV SLLNIAGGVY TVKSTSGNTH LGGQDFDTNL LEHFKAEFKK
260 270 280 290 300
KTGLDISGDA RALRRLRTAA ERAKRTLSSV TQTTVEVDSL FEGEDFETSI
310 320 330 340 350
TRARFEDINA ALFKSTLEPV EQVLKDAQIS KSQIDEVVLV GGSTRIPKVQ
360 370 380 390 400
KLLSDFFEGK QLEKSINPDE AVAYGAAVQA AILTGSNLSD DTKDLLLLDV
410 420 430 440 450
APLSLGVAMQ GDVFACVIPR NTTVPTIKRR TFTTVHDGQT TVTFPVYQGE
460 470 480 490 500
RVNCKDNTLL GEFDLKGIPP LPAGEPVLEA IFEVDANGIL KVTAVEKSTG
510 520 530 540 550
KTANITISNA IGRLSSEDIE KMVSQAEEFK AADEAFAKRH EARQRLESYV
560 570 580 590 600
SSIEQTVSDP VLSAKMKKGA KSKVEAALAD AFSALQIEES SAEDYRKAEI
610
GLKRVVTKAM ATR
Length:613
Mass (Da):66,253
Last modified:January 23, 2007 - v3
Checksum:i22EA0480F0A6B106
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016815 Genomic DNA Translation: AAS50597.1
RefSeqiNP_982773.1, NM_208126.2

Genome annotation databases

EnsemblFungiiAAS50597; AAS50597; AGOS_ABL174C
GeneIDi4618853
KEGGiago:AGOS_ABL174C

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016815 Genomic DNA Translation: AAS50597.1
RefSeqiNP_982773.1, NM_208126.2

3D structure databases

ProteinModelPortaliQ75E44
SMRiQ75E44
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi33169.AAS50597

Proteomic databases

PRIDEiQ75E44

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiAAS50597; AAS50597; AGOS_ABL174C
GeneIDi4618853
KEGGiago:AGOS_ABL174C

Phylogenomic databases

HOGENOMiHOG000228135
InParanoidiQ75E44
KOiK03283
OMAiDFSARHE
OrthoDBiEOG092C1VPN

Family and domain databases

Gene3Di1.20.1270.10, 1 hit
2.60.34.10, 1 hit
InterProiView protein in InterPro
IPR018181 Heat_shock_70_CS
IPR029048 HSP70_C_sf
IPR029047 HSP70_peptide-bd_sf
IPR013126 Hsp_70_fam
PANTHERiPTHR19375 PTHR19375, 1 hit
PfamiView protein in Pfam
PF00012 HSP70, 1 hit
PRINTSiPR00301 HEATSHOCK70
SUPFAMiSSF100920 SSF100920, 1 hit
SSF100934 SSF100934, 1 hit
PROSITEiView protein in PROSITE
PS00297 HSP70_1, 1 hit
PS00329 HSP70_2, 1 hit
PS01036 HSP70_3, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiSSB1_ASHGO
AccessioniPrimary (citable) accession number: Q75E44
Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: January 23, 2007
Last modified: November 7, 2018
This is version 90 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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