SSB1_CANAW
ID SSB1_CANAW Reviewed; 613 AA.
AC P87222; C4YML8;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 2.
DT 03-AUG-2022, entry version 97.
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; Synonyms=HSP70B; ORFNames=CAWG_02101;
OS Candida albicans (strain WO-1) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=294748;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=WO-1;
RX PubMed=9200817;
RX DOI=10.1002/(sici)1097-0061(19970615)13:7<677::aid-yea131>3.0.co;2-6;
RA Maneu V., Cervera A.M., Martinez J.P., Gozalbo D.;
RT "Molecular cloning of a Candida albicans gene (SSB1) coding for a protein
RT related to the Hsp70 family.";
RL Yeast 13:677-681(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WO-1;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(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; X97723; CAA66308.1; -; Genomic_DNA.
DR EMBL; CM000309; EEQ43849.1; -; Genomic_DNA.
DR AlphaFoldDB; P87222; -.
DR SMR; P87222; -.
DR STRING; 5476.P87222; -.
DR COMPLUYEAST-2DPAGE; P87222; -.
DR PRIDE; P87222; -.
DR EnsemblFungi; EEQ43849; EEQ43849; CAWG_02101.
DR VEuPathDB; FungiDB:CAWG_02101; -.
DR HOGENOM; CLU_005965_2_1_1; -.
DR OMA; HQTTVQF; -.
DR Proteomes; UP000001429; Chromosome R.
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.
FT CHAIN 1..613
FT /note="Ribosome-associated molecular chaperone SSB1"
FT /id="PRO_0000078366"
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"
FT CONFLICT 325
FT /note="K -> E (in Ref. 1; CAA66308)"
FT /evidence="ECO:0000305"
FT CONFLICT 414
FT /note="F -> L (in Ref. 1; CAA66308)"
FT /evidence="ECO:0000305"
FT CONFLICT 455
FT /note="T -> S (in Ref. 1; CAA66308)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 613 AA; 66479 MW; 1014A4CAFFCF559A CRC64;
MADGVFQGAI GIDLGTTYSC VATYDSAVEI IANEQGNRVT PSFVAFTSEE RLIGDAAKNQ
AALNPKNTVF DAKRLIGRAF DDESVQKDIK SWPFKVVESN GQPLIEVEYL DETKTFSPQE
ISSMVLTKMK EIAEAKIGKK VEKAVVTVPA YFNDAQRQAT KDAGAIAGLN VLRIINEPTA
AAIAYGLGAG KSEKERHVLI FDLGGGTFDV SLLNITGGVF TVKATAGDTH LGGQDFDTNL
LEHFKKEFQK KTGNDISSDA RALRRLRTAC ERAKRSLSSG TQTTVEIDSL FDGEDFSANI
TRARFEDINS ALFKSTLEPV EQVLKDAKIS KSQVDEVVLV GGSTRIPKVQ KLLSDFFDGK
QLEKSINPDE AVAYGAAVQG AILTGQSTND DTKDLLLLDV IPLSLGVAMQ GNVFAPVVPR
NTTVPTIKRR TFTTVADHQT TVQFPVYQGE RVNCTENTLL GEFDLKNIPP MQAGEPVLEA
IFEVDANGIL KVTAVEKSTG RSANITISNS IGRLSTEEIE KMISDAEKFK SSDDAFAKRH
EQKQKLEAYV ASVESTVTDP VLSAKLKKSA KDKIEAALSD ALQTLEIEES SADDYRKAEL
ALKRAVTKGM ATR
