SSB1_SCHPO
ID SSB1_SCHPO Reviewed; 613 AA.
AC Q10284; O74730; P87181;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 14-AUG-2001, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Ribosome-associated molecular chaperone sks2 {ECO:0000305};
DE EC=3.6.4.10;
DE AltName: Full=Heat shock cognate protein hsc1 {ECO:0000303|PubMed:8973306};
DE AltName: Full=Hsp70 chaperone Ssb;
DE AltName: Full=Suppressor of K-252a sensitivity protein 2 {ECO:0000303|PubMed:9161410};
GN Name=sks2 {ECO:0000303|PubMed:9161410};
GN Synonyms=hsc1 {ECO:0000303|PubMed:8973306}; ORFNames=SPBC1709.05;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8973306; DOI=10.1016/s0378-1119(96)00458-1;
RA Oishi K., Sugiura R., Shuntoh H., Kuno T.;
RT "Cloning and characterization of hsc1+, a heat shock cognate gene of the
RT fission yeast Schizosaccharomyces pombe.";
RL Gene 181:45-49(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9161410; DOI=10.1016/s0378-1119(96)00831-1;
RA Usui T., Yoshida M., Kasahara K., Honda A., Beppu T., Horinouchi S.;
RT "A novel HSP70 gene of Schizosaccharomyces pombe that confers K-252a
RT resistance.";
RL Gene 189:43-47(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-40; TYR-151; SER-153;
RP SER-155; SER-256; SER-353; SER-501; SER-514; SER-515 AND THR-516, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
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 pss1 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) (By similarity). Interacts with pss1
CC (By similarity). Interacts with fes1 (By similarity).
CC {ECO:0000250|UniProtKB:P11484}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
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}.
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DR EMBL; D84218; BAA12279.1; -; Genomic_DNA.
DR EMBL; D63798; BAA20093.1; -; Genomic_DNA.
DR EMBL; CU329671; CAA21244.1; -; Genomic_DNA.
DR PIR; JC5335; JC5335.
DR PIR; T39633; T39633.
DR PIR; T43239; T43239.
DR RefSeq; NP_595438.1; NM_001021346.2.
DR AlphaFoldDB; Q10284; -.
DR SMR; Q10284; -.
DR BioGRID; 276732; 15.
DR IntAct; Q10284; 2.
DR STRING; 4896.SPBC1709.05.1; -.
DR iPTMnet; Q10284; -.
DR MaxQB; Q10284; -.
DR PaxDb; Q10284; -.
DR PRIDE; Q10284; -.
DR EnsemblFungi; SPBC1709.05.1; SPBC1709.05.1:pep; SPBC1709.05.
DR GeneID; 2540199; -.
DR KEGG; spo:SPBC1709.05; -.
DR PomBase; SPBC1709.05; sks2.
DR VEuPathDB; FungiDB:SPBC1709.05; -.
DR eggNOG; KOG0101; Eukaryota.
DR HOGENOM; CLU_005965_0_1_1; -.
DR InParanoid; Q10284; -.
DR OMA; HQTTVQF; -.
DR PhylomeDB; Q10284; -.
DR PRO; PR:Q10284; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISO:PomBase.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0031072; F:heat shock protein binding; IBA:GO_Central.
DR GO; GO:0051787; F:misfolded protein binding; IBA:GO_Central.
DR GO; GO:0044183; F:protein folding chaperone; IBA:GO_Central.
DR GO; GO:0051082; F:unfolded protein binding; ISO:PomBase.
DR GO; GO:0051083; P:'de novo' cotranslational protein folding; ISO:PomBase.
DR GO; GO:0034620; P:cellular response to unfolded protein; IBA:GO_Central.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; ISO:PomBase.
DR GO; GO:0042254; P:ribosome biogenesis; ISO:PomBase.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
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; PS00297; HSP70_1; 1.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chaperone; Cytoplasm; Hydrolase; Nucleotide-binding;
KW Phosphoprotein; Protein biosynthesis; Reference proteome.
FT CHAIN 1..613
FT /note="Ribosome-associated molecular chaperone sks2"
FT /id="PRO_0000078381"
FT REGION 1..390
FT /note="Nucleotide binding domain (NBD)"
FT /evidence="ECO:0000250|UniProtKB:G0SCU5"
FT REGION 391..401
FT /note="Inter-domain linker"
FT /evidence="ECO:0000250|UniProtKB:G0SCU5"
FT REGION 402..612
FT /note="Substrate binding domain (SBD)"
FT /evidence="ECO:0000250|UniProtKB:G0SCU5"
FT REGION 515..611
FT /note="Lid domain (SBDalpha)"
FT /evidence="ECO:0000250|UniProtKB:G0SCU5"
FT MOTIF 573..581
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250|UniProtKB:P11484"
FT BINDING 15..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:G0SCU5"
FT BINDING 73
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:G0SCU5"
FT BINDING 204..206
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:G0SCU5"
FT BINDING 270..277
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:G0SCU5"
FT BINDING 341
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:G0SCU5"
FT MOD_RES 40
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 151
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 153
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 256
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 353
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 501
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 514
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 515
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 516
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CONFLICT 250..252
FT /note="KQK -> TKR (in Ref. 1; BAA12279)"
FT /evidence="ECO:0000305"
FT CONFLICT 456
FT /note="N -> T (in Ref. 2; BAA20093)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 613 AA; 67205 MW; EE86C49DB1F59348 CRC64;
MSEVYEGAIG IDLGTTYSCV AVWETANVEI IPNDQGARTT PSFVAFTETE RLVGDAAKNQ
AAMNPRNTVF DAKRLIGRRY EDPETQKDIK HWPFKVIDNN GIPTIEVNYL GEKKQFTAQE
ISAMVLTKMK EISEAKLNKR VEKAVITVPA YFSDSQRAAT KDAGAIAGLN VLRIINEPTA
AAIAYGLDAK SDKPKNVLIF DLGGGTFDVS LLKIQGGVFE VLATAGDTHL GGEDFDNALV
EHFIQEFKRK QKIDISDDPR ALRRLRSACE RAKRALSSVT QTTVEVDSLS NGIDFSSSIT
RARFEDINAT TFKATIDPVA KVLKDSKVPK ADVHDIVLVG GSTRIPKVQR LVSDFFDGRA
LNKSINPDEA VAYGAAVQAA VLTNKADSDK TQDLLLLDVV PLSLGVAMEG NVFGVVCPRN
TPIPTIKKRT FTTVADNQTT VTFPVYQGER VNCAENEPLG EFQLTGIPPM PRGQAELEAT
FELDANGILK VTAVEKTTGR SAHIEITNSV GHLSSTKIQE MIENADKFKQ QDKDFAKKLE
AKSQLESYIS NIETTISEPN VMMKLKRGDK SKIEAQLAEC MSQLELEDTN TDALRKAELR
LKRTVQKAFA SLR
