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Protein

Ribosome-associated molecular chaperone SSB

Gene

SSB1

more
Organism
Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata)
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 SSB (EC:3.6.4.10)
Alternative name(s):
Heat shock protein SSB
Hsp70 chaperone Ssb
Gene namesi
Name:SSB1
Ordered Locus Names:CAGL0C05379g
AND
Name:SSB2
Ordered Locus Names:CAGL0K04741g
OrganismiCandida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata)
Taxonomic identifieri284593 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeNakaseomycesNakaseomyces/Candida clade
Proteomesi
  • UP000002428 Componentsi: Chromosome C, Chromosome K

Organism-specific databases

CGDiCAL0127488 SSB1
CAL0133897 SSB2

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_00000783671 – 613Ribosome-associated molecular chaperone SSBAdd BLAST613

Proteomic databases

PRIDEiQ876N3

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

STRINGi284593.XP_448432.1

Structurei

3D structure databases

ProteinModelPortaliQ876N3
SMRiQ876N3
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

eggNOGiKOG0101 Eukaryota
COG0443 LUCA
HOGENOMiHOG000228135
InParanoidiQ876N3
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.

Q876N3-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MADGVFQGAI GIDLGTTYSC VATYESSVEI IANEQGNRVT PSFVAFTPEE
60 70 80 90 100
RLIGDAAKNQ AALNPKNTVF DAKRLIGRRF DEESVQNDMK TWPFKVVDVD
110 120 130 140 150
GAPVIEVEYL GENKQFSPQE ISSMVLTKMK EIAEAKIGKK VEKAVITVPA
160 170 180 190 200
YFNDAQRQAT KDAGAISGLN VLRIINEPTA AAIAYGLGAG KSDKERHVLI
210 220 230 240 250
FDLGGGTFDV SLLHIAGGVY TVKSTSGNTH LGGQDFDTNL LEHFKGEFKK
260 270 280 290 300
KTGLDISNDA RALRRLRTAA ERAKRTLSSV TQTTVEVDSL FEGEDFEASL
310 320 330 340 350
TRARFEDLNA ALFKSTLEPV EQVLKDAKIS KSQIDEVVLV GGSTRIPKVQ
360 370 380 390 400
KLLSDYFDGK QLEKSINPDE AVAYGAAVQG AILTGQSTSD ETKDLLLLDV
410 420 430 440 450
APLSLGVGMQ GDIFGVVVPR NTTVPTIKRR TFTTVGDNQT TVQFPVYQGE
460 470 480 490 500
RVNCKENTLL GEFDLKNIPP MPAGEPVLEA IFEVDANGIL KVTAVEKSTG
510 520 530 540 550
KSANITISNA VGRLSSEDIE KMVNQAEEFK AADEAFAKRH EAKQRLESYV
560 570 580 590 600
ASIEQTVTDP VLSSKLKRGS KTKIEAALAD ALSALQIEDG SAEEYRKAEV
610
GLKRVVTKAM SSR
Length:613
Mass (Da):66,396
Last modified:January 23, 2007 - v3
Checksum:i16A361603AC31929
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY077689 Genomic DNA Translation: AAL86913.1
CR380949 Genomic DNA Translation: CAG58314.1
CR380957 Genomic DNA Translation: CAG61393.1
RefSeqiXP_445408.1, XM_445408.1
XP_448432.1, XM_448432.1

Genome annotation databases

EnsemblFungiiCAG58314; CAG58314; CAGL0C05379g
CAG61393; CAG61393; CAGL0K04741g
GeneIDi2886843
2890011
KEGGicgr:CAGL0C05379g
cgr:CAGL0K04741g

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY077689 Genomic DNA Translation: AAL86913.1
CR380949 Genomic DNA Translation: CAG58314.1
CR380957 Genomic DNA Translation: CAG61393.1
RefSeqiXP_445408.1, XM_445408.1
XP_448432.1, XM_448432.1

3D structure databases

ProteinModelPortaliQ876N3
SMRiQ876N3
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi284593.XP_448432.1

Proteomic databases

PRIDEiQ876N3

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCAG58314; CAG58314; CAGL0C05379g
CAG61393; CAG61393; CAGL0K04741g
GeneIDi2886843
2890011
KEGGicgr:CAGL0C05379g
cgr:CAGL0K04741g

Organism-specific databases

CGDiCAL0127488 SSB1
CAL0133897 SSB2

Phylogenomic databases

eggNOGiKOG0101 Eukaryota
COG0443 LUCA
HOGENOMiHOG000228135
InParanoidiQ876N3
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_CANGA
AccessioniPrimary (citable) accession number: Q876N3
Secondary accession number(s): Q6FWI6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: January 23, 2007
Last modified: November 7, 2018
This is version 93 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
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Main funding by: National Institutes of Health

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