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Protein

Ribosome-associated molecular chaperone SSB1

Gene

SSB1

Organism
Kluyveromyces marxianus (Yeast) (Candida kefyr)
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
OrganismiKluyveromyces marxianus (Yeast) (Candida kefyr)
Taxonomic identifieri4911 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeKluyveromyces

Subcellular locationi

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000783711 – 613Ribosome-associated molecular chaperone SSB1Add BLAST613

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

Structurei

3D structure databases

ProteinModelPortaliP41770
SMRiP41770
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

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.

P41770-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAEGVFPGAI GIDLGTTYSC VATYENSVEI IANEQGNRVT PSFVAFTPEE
60 70 80 90 100
RLIGDAAKNQ AALNPKNTVF DAKRLIGRRF DEESVQSDMK TWPFKVIDSN
110 120 130 140 150
GAPLIEVEYL GETKTFSPQE ISSMVLTKMK EIAEAKIGKK VEKAVVTVPA
160 170 180 190 200
YFNDAQRQAT KDAGAIAGLN VLRIINEPTA AAIAYGVGAG NSEKERHVLI
210 220 230 240 250
FDLGGGTFDV SLLHIAGGVY TVKSTSGNTH LGGQDFDTNL LEHFKTEFKK
260 270 280 290 300
KTGADISGDA RALRRLRTAA ERAKRTLSSV AQTTVEVDSL FDGEDFEATI
310 320 330 340 350
TRARFEDINA ALFKSTLEPV EQVLKDAKIS KSQIDEVVLV GGSTRIPKVQ
360 370 380 390 400
KLLSDFFDGK QLEKSINPDE AVAYGAAVQG AILTGQSTSD ETKDLLLLDV
410 420 430 440 450
APLSLGVGMA GDVFGVVVPR NTTVPTIKRR TFTTVADHQT TVTFPVYQGE
460 470 480 490 500
RVNCKENTLL GEFDLKGVPP MPAGEPVLEA IFEVDANGIL KVTAVEKSTG
510 520 530 540 550
KSANITISNA IGRLSSEEIE QMVNQAEEFK AADEAFAKKH EARQRLESYI
560 570 580 590 600
SSVQQTVTDP VLSAKIKRNA KAKVEAALAD AFSTLQIEDA SADDLRKAEV
610
GLKRAVTKAM STR
Length:613
Mass (Da):66,087
Last modified:January 23, 2007 - v2
Checksum:i7D3333E769F2CCB6
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti187V → L in CAE84429 (PubMed:14745027).Curated1
Sequence conflicti191N → K in CAE84429 (PubMed:14745027).Curated1
Sequence conflicti246T → A in CAE84429 (PubMed:14745027).Curated1
Sequence conflicti554Q → E in CAE84429 (PubMed:14745027).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59963 Genomic DNA Translation: CAA42589.1
AJ617308 Genomic DNA Translation: CAE84429.1
PIRiS30562

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59963 Genomic DNA Translation: CAA42589.1
AJ617308 Genomic DNA Translation: CAE84429.1
PIRiS30562

3D structure databases

ProteinModelPortaliP41770
SMRiP41770
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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_KLUMA
AccessioniPrimary (citable) accession number: P41770
Secondary accession number(s): Q707X6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: May 23, 2018
This is version 71 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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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