SSB1_CHATD
ID SSB1_CHATD Reviewed; 614 AA.
AC G0SCU5;
DT 15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2017, sequence version 2.
DT 03-AUG-2022, entry version 40.
DE RecName: Full=Ribosome-associated molecular chaperone SSB1 {ECO:0000305|PubMed:27882919};
DE EC=3.6.4.10;
DE AltName: Full=Heat shock protein SSB1;
DE AltName: Full=Hsp70 chaperone Ssb;
GN Name=SSB1 {ECO:0000303|PubMed:27882919}; ORFNames=CTHT_0058460;
OS Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX NCBI_TaxID=759272;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1495 / CBS 144.50 / IMI 039719;
RX PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R., Devos D.P.,
RA Arumugam M., Bork P., Hurt E.;
RT "Insight into structure and assembly of the nuclear pore complex by
RT utilizing the genome of a eukaryotic thermophile.";
RL Cell 146:277-289(2011).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 4-613 IN COMPLEX WITH ATP, AND
RP MUTAGENESIS OF THR-208.
RX PubMed=27882919; DOI=10.1038/ncomms13563;
RA Gumiero A., Conz C., Gese G.V., Zhang Y., Weyer F.A., Lapouge K.,
RA Kappes J., von Plehwe U., Schermann G., Fitzke E., Woelfle T., Fischer T.,
RA Rospert S., Sinning I.;
RT "Interaction of the cotranslational Hsp70 Ssb with ribosomal proteins and
RT rRNA depends on its lid domain.";
RL Nat. Commun. 7:13563-13563(2016).
CC -!- FUNCTION: Ribosome-bound, Hsp70-type chaperone that assists in the
CC cotranslational folding of newly synthesized proteins in the cytosol.
CC Stimulates folding by interacting with nascent chains, binding to
CC short, largely hydrophobic sequences exposed by unfolded proteins,
CC thereby stabilizing longer, more slowly translated, and aggregation-
CC prone nascent polypeptides and domains that cannot fold stably until
CC fully synthesized. The Hsp70-protein substrate interaction depends on
CC ATP-binding and on allosteric regulation between the NBD and the SBD.
CC The ATP-bound state is characterized by a fast exchange rate of
CC substrate (low affinity state), while in the ADP-bound state exchange
CC is much slower (high affinity state). During the Hsp70 cycle, the
CC chaperone switches between the ATP-bound state (open conformation) and
CC the ADP-bound state (closed conformation) by major conformational
CC rearrangements involving mainly the lid domain. Ssb cooperates with a
CC specific Hsp40/Hsp70 co-chaperone termed the ribosome-associated
CC complex (RAC), which stimulates the ATPase activity of the ribosome-
CC associated pool of Ssbs and switches it to the high affinity substrate
CC binding state. Hsp110 chaperone SSE1 and FES1 act as nucleotide
CC exchange factors that cause substrate release.
CC {ECO:0000250|UniProtKB:P11484}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.10;
CC Evidence={ECO:0000250|UniProtKB:P11484};
CC -!- SUBUNIT: Binds to ribosomes. Binds close to the ribosomal tunnel exit
CC via contacts with both ribosomal proteins and rRNA. Directly interacts
CC with nascent polypeptides. This interaction is dependent on the
CC ribosome-associated complex (RAC). Interacts with SSE1. Interacts with
CC FES1. {ECO:0000250|UniProtKB:P11484}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P11484}.
CC Note=Associated with translating ribosomes.
CC {ECO:0000250|UniProtKB:P11484}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. Ssb-type Hsp70
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EGS19221.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; GL988045; EGS19221.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_006696166.1; XM_006696103.1.
DR PDB; 5TKY; X-ray; 2.60 A; A/B=4-613.
DR PDB; 7OLC; EM; 2.90 A; C=1-614.
DR PDBsum; 5TKY; -.
DR PDBsum; 7OLC; -.
DR AlphaFoldDB; G0SCU5; -.
DR SMR; G0SCU5; -.
DR STRING; 759272.G0SCU5; -.
DR EnsemblFungi; EGS19221; EGS19221; CTHT_0058460.
DR GeneID; 18259884; -.
DR KEGG; cthr:CTHT_0058460; -.
DR eggNOG; KOG0101; Eukaryota.
DR HOGENOM; CLU_005965_0_1_1; -.
DR OrthoDB; 288077at2759; -.
DR Proteomes; UP000008066; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR GO; GO:0005844; C:polysome; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:EnsemblFungi.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0005516; F:calmodulin binding; IEA:EnsemblFungi.
DR GO; GO:0051082; F:unfolded protein binding; IEA:EnsemblFungi.
DR GO; GO:0051083; P:'de novo' cotranslational protein folding; IEA:EnsemblFungi.
DR GO; GO:0042149; P:cellular response to glucose starvation; IEA:EnsemblFungi.
DR GO; GO:0002181; P:cytoplasmic translation; IEA:EnsemblFungi.
DR GO; GO:0006450; P:regulation of translational fidelity; IEA:EnsemblFungi.
DR GO; GO:0000054; P:ribosomal subunit export from nucleus; IEA:EnsemblFungi.
DR GO; GO:0006364; P:rRNA processing; IEA:EnsemblFungi.
DR GO; GO:0006452; P:translational frameshifting; IEA:EnsemblFungi.
DR GO; GO:0006415; P:translational termination; IEA:EnsemblFungi.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 2.60.34.10; -; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR029048; HSP70_C_sf.
DR InterPro; IPR029047; HSP70_peptide-bd_sf.
DR InterPro; IPR013126; Hsp_70_fam.
DR PANTHER; PTHR19375; PTHR19375; 1.
DR Pfam; PF00012; HSP70; 1.
DR SUPFAM; SSF100920; SSF100920; 1.
DR SUPFAM; SSF100934; SSF100934; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Chaperone; Cytoplasm; Hydrolase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..614
FT /note="Ribosome-associated molecular chaperone SSB1"
FT /id="PRO_0000438973"
FT REGION 1..392
FT /note="Nucleotide binding domain (NBD)"
FT /evidence="ECO:0000305|PubMed:27882919"
FT REGION 393..403
FT /note="Inter-domain linker"
FT /evidence="ECO:0000305|PubMed:27882919"
FT REGION 404..614
FT /note="Substrate binding domain (SBD)"
FT /evidence="ECO:0000305|PubMed:27882919"
FT REGION 517..613
FT /note="Lid domain (SBDalpha)"
FT /evidence="ECO:0000305|PubMed:27882919"
FT MOTIF 575..583
FT /note="Nuclear export signal"
FT /evidence="ECO:0000305|PubMed:27882919"
FT BINDING 16..18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:27882919,
FT ECO:0007744|PDB:5TKY"
FT BINDING 74
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:27882919,
FT ECO:0007744|PDB:5TKY"
FT BINDING 206..208
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:27882919,
FT ECO:0007744|PDB:5TKY"
FT BINDING 272..279
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:27882919,
FT ECO:0007744|PDB:5TKY"
FT BINDING 343
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:27882919,
FT ECO:0007744|PDB:5TKY"
FT MUTAGEN 208
FT /note="T->A: Reduces ATPase activity."
FT /evidence="ECO:0000305|PubMed:27882919"
FT STRAND 10..14
FT /evidence="ECO:0007829|PDB:5TKY"
FT STRAND 16..24
FT /evidence="ECO:0007829|PDB:5TKY"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:5TKY"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:5TKY"
FT STRAND 44..47
FT /evidence="ECO:0007829|PDB:5TKY"
FT STRAND 52..55
FT /evidence="ECO:0007829|PDB:5TKY"
FT HELIX 56..60
FT /evidence="ECO:0007829|PDB:5TKY"
FT TURN 61..64
FT /evidence="ECO:0007829|PDB:5TKY"
FT TURN 66..68
FT /evidence="ECO:0007829|PDB:5TKY"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:5TKY"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:5TKY"
FT TURN 76..78
FT /evidence="ECO:0007829|PDB:5TKY"
FT HELIX 84..92
FT /evidence="ECO:0007829|PDB:5TKY"
FT STRAND 94..100
FT /evidence="ECO:0007829|PDB:5TKY"
FT STRAND 103..110
FT /evidence="ECO:0007829|PDB:5TKY"
FT STRAND 113..117
FT /evidence="ECO:0007829|PDB:5TKY"
FT HELIX 119..138
FT /evidence="ECO:0007829|PDB:5TKY"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:5TKY"
FT STRAND 144..149
FT /evidence="ECO:0007829|PDB:5TKY"
FT HELIX 155..167
FT /evidence="ECO:0007829|PDB:5TKY"
FT STRAND 171..177
FT /evidence="ECO:0007829|PDB:5TKY"
FT HELIX 178..188
FT /evidence="ECO:0007829|PDB:5TKY"
FT STRAND 197..204
FT /evidence="ECO:0007829|PDB:5TKY"
FT STRAND 209..217
FT /evidence="ECO:0007829|PDB:5TKY"
FT STRAND 220..229
FT /evidence="ECO:0007829|PDB:5TKY"
FT HELIX 234..253
FT /evidence="ECO:0007829|PDB:5TKY"
FT HELIX 261..278
FT /evidence="ECO:0007829|PDB:5TKY"
FT STRAND 281..292
FT /evidence="ECO:0007829|PDB:5TKY"
FT STRAND 295..302
FT /evidence="ECO:0007829|PDB:5TKY"
FT HELIX 303..309
FT /evidence="ECO:0007829|PDB:5TKY"
FT HELIX 311..316
FT /evidence="ECO:0007829|PDB:5TKY"
FT HELIX 318..328
FT /evidence="ECO:0007829|PDB:5TKY"
FT HELIX 332..334
FT /evidence="ECO:0007829|PDB:5TKY"
FT STRAND 337..342
FT /evidence="ECO:0007829|PDB:5TKY"
FT HELIX 343..346
FT /evidence="ECO:0007829|PDB:5TKY"
FT HELIX 348..357
FT /evidence="ECO:0007829|PDB:5TKY"
FT TURN 369..371
FT /evidence="ECO:0007829|PDB:5TKY"
FT HELIX 372..384
FT /evidence="ECO:0007829|PDB:5TKY"
FT STRAND 397..399
FT /evidence="ECO:0007829|PDB:5TKY"
FT STRAND 406..409
FT /evidence="ECO:0007829|PDB:5TKY"
FT STRAND 413..419
FT /evidence="ECO:0007829|PDB:5TKY"
FT STRAND 424..433
FT /evidence="ECO:0007829|PDB:5TKY"
FT STRAND 443..451
FT /evidence="ECO:0007829|PDB:5TKY"
FT HELIX 455..457
FT /evidence="ECO:0007829|PDB:5TKY"
FT STRAND 458..466
FT /evidence="ECO:0007829|PDB:5TKY"
FT STRAND 479..485
FT /evidence="ECO:0007829|PDB:5TKY"
FT STRAND 491..497
FT /evidence="ECO:0007829|PDB:5TKY"
FT TURN 498..500
FT /evidence="ECO:0007829|PDB:5TKY"
FT STRAND 501..503
FT /evidence="ECO:0007829|PDB:5TKY"
FT STRAND 506..510
FT /evidence="ECO:0007829|PDB:5TKY"
FT HELIX 517..558
FT /evidence="ECO:0007829|PDB:5TKY"
FT HELIX 573..587
FT /evidence="ECO:0007829|PDB:5TKY"
FT HELIX 593..611
FT /evidence="ECO:0007829|PDB:5TKY"
SQ SEQUENCE 614 AA; 67030 MW; B626C8FB94428542 CRC64;
MAEEVYDGAI GIDLGTTYSC VAVYEGTNVE IIANEQGNFT TPSFVSFTEN ERLIGEAAKN
QAAMNPANTI FDVKRLIGRR FDDPTVKKDM ESWPFKVVDD NGNPKVEVQY LGQTHTFSPQ
EISAMVLTKM KEIAETKLGK KVEKAVITVP AYFNDNQRQA TKDAGAIAGL NVLRIINEPT
AAAIAYGLGS GKSDKERNVL IYDLGGGTFD VSLLNIQGGV FTVKATAGDT HLGGQDFDTN
LLEYCKKEFT RKTKKDLSGD ARALRRLRTA CERAKRTLSS GAQTTIEIDS LFDGEDFNIQ
ITRARFEDLN AKAFAGTLEP VAQVLKDAGI EKHQVDEIVL VGGSTRIPRI QKLLSEFFDG
KKLEKSINPD EAVAYGAAVQ AGILSGKATS ADTSDLLLLD VVPLSLGVAM EGNIFAPVVP
RGQTVPTIKK RTFTTVADNQ QTVQFPVYQG ERVNCEDNTL LGEFTLAPIP PMKAGEPVLE
VVFEVDVNGI LKVTATEKTS GRSANITIAN SVGKLSTDEI EKMISDAEKF KSKDEAFSKR
FEAKQQLESY ISRVEEIISD PTLSLKLKRG QKDKIEQALS EAMAQLEIED STADELKKKE
LALKRLVTKA MASR
