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SSB1_ZYGRC
ID   SSB1_ZYGRC              Reviewed;         613 AA.
AC   Q707X3; C5DTQ5;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Ribosome-associated molecular chaperone SSB1;
DE            EC=3.6.4.10;
DE   AltName: Full=Heat shock protein SSB1;
DE   AltName: Full=Hsp70 chaperone Ssb;
GN   Name=SSB1; OrderedLocusNames=ZYRO0C10450g;
OS   Zygosaccharomyces rouxii (strain ATCC 2623 / CBS 732 / NBRC 1130 / NCYC 568
OS   / NRRL Y-229) (Candida mogii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Zygosaccharomyces.
OX   NCBI_TaxID=559307;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=14745027; DOI=10.1073/pnas.0304170101;
RA   Butler G., Kenny C., Fagan A., Kurischko C., Gaillardin C., Wolfe K.H.;
RT   "Evolution of the MAT locus and its Ho endonuclease in yeast species.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:1632-1637(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2623 / CBS 732 / BCRC 21506 / NBRC 1130 / NCYC 568 / NRRL
RC   Y-229;
RX   PubMed=19525356; DOI=10.1101/gr.091546.109;
RG   The Genolevures Consortium;
RA   Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA   Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P., Jubin C.,
RA   Poulain J., Barbe V., Segurens B., Artiguenave F., Anthouard V.,
RA   Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R., Durrens P.,
RA   Jean G., Marck C., Martin T., Nikolski M., Rolland T., Seret M.-L.,
RA   Casaregola S., Despons L., Fairhead C., Fischer G., Lafontaine I., Leh V.,
RA   Lemaire M., de Montigny J., Neuveglise C., Thierry A., Blanc-Lenfle I.,
RA   Bleykasten C., Diffels J., Fritsch E., Frangeul L., Goeffon A.,
RA   Jauniaux N., Kachouri-Lafond R., Payen C., Potier S., Pribylova L.,
RA   Ozanne C., Richard G.-F., Sacerdot C., Straub M.-L., Talla E.;
RT   "Comparative genomics of protoploid Saccharomycetaceae.";
RL   Genome Res. 19:1696-1709(2009).
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}.
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DR   EMBL; AJ617309; CAE84432.1; -; Genomic_DNA.
DR   EMBL; CU928175; CAR27166.1; -; Genomic_DNA.
DR   RefSeq; XP_002496099.1; XM_002496054.1.
DR   AlphaFoldDB; Q707X3; -.
DR   SMR; Q707X3; -.
DR   STRING; 559307.Q707X3; -.
DR   PRIDE; Q707X3; -.
DR   EnsemblFungi; CAR27166; CAR27166; ZYRO0C10450g.
DR   GeneID; 8203314; -.
DR   KEGG; zro:ZYRO0C10450g; -.
DR   HOGENOM; CLU_005965_0_1_1; -.
DR   InParanoid; Q707X3; -.
DR   Proteomes; UP000008536; Chromosome C.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
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   3: Inferred from homology;
KW   ATP-binding; Chaperone; Cytoplasm; Hydrolase; Nucleotide-binding;
KW   Protein biosynthesis; Reference proteome.
FT   CHAIN           1..613
FT                   /note="Ribosome-associated molecular chaperone SSB1"
FT                   /id="PRO_0000078398"
FT   REGION          1..391
FT                   /note="Nucleotide binding domain (NBD)"
FT                   /evidence="ECO:0000250|UniProtKB:G0SCU5"
FT   REGION          392..402
FT                   /note="Inter-domain linker"
FT                   /evidence="ECO:0000250|UniProtKB:G0SCU5"
FT   REGION          403..613
FT                   /note="Substrate binding domain (SBD)"
FT                   /evidence="ECO:0000250|UniProtKB:G0SCU5"
FT   REGION          516..612
FT                   /note="Lid domain (SBDalpha)"
FT                   /evidence="ECO:0000250|UniProtKB:G0SCU5"
FT   MOTIF           574..582
FT                   /note="Nuclear export signal"
FT                   /evidence="ECO:0000250|UniProtKB:P11484"
FT   BINDING         16..18
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         205..207
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:G0SCU5"
FT   BINDING         271..278
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:G0SCU5"
FT   BINDING         342
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:G0SCU5"
SQ   SEQUENCE   613 AA;  66730 MW;  EDC4D0418B3F740E CRC64;
     MAEGVFQGAI GIDLGTTYSC VATYESSVEI IANEQGNRVT PSFVAFTPEE RLIGDAAKNQ
     AALNPENTVF DAKRLIGRRF DDESVQKDRK TWPFKLIDVE GNPVVEVQYL GETKTFSPQE
     ISSMVLTKMK EIAEAKIGQK VEKAVITVPA YFNDAQRQAT KDAGSISGLN VLRIINEPTA
     AAIAYGLGAG KSEKERHVLI FDLGGGTFDV SLLHIAGGVY TVKSTSGNTH LGGQDFDTNM
     LEHFKNEFKK KTGNDISGDA RALRRLRTAC ERAKRTLSSV TQTTIEVDSL YNGDDFETSI
     TRARFEDLNS SLFKSTLEPV EQVLKDAKVP KTEIDEVVLV GGSTRIPKVQ KMLSDFFEGK
     QLEKSINPDE AVAYGAAVQG AILTGQSTSE DTKDLLLLDV APLSLGVGMQ GDIFGIVVPR
     NTTVPTIKRR TFTTVADHQS TVQFPVYQGE RVNCKENTLL GEFDLKNIPP MQAGEPVLEA
     IFEVDANGIL KVTAVEKSTG KSANITISNA VGRLSSDEIE KMVNQAEEFK AADEAFAKKH
     EARQRLESYV ASIEQQVTDP VLSSKLKRGS KTKIESALSD ALASLEIQDA STDDLRKAEV
     GLKRVVTKAM SSR
 
 
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