HSP71_YEAST
ID HSP71_YEAST Reviewed; 642 AA.
AC P10591; D6VPL2;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 230.
DE RecName: Full=Heat shock protein SSA1;
DE AltName: Full=Heat shock protein YG100;
GN Name=SSA1; OrderedLocusNames=YAL005C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=2644626; DOI=10.1093/nar/17.2.805;
RA Slater M.R., Craig E.A.;
RT "The SSA1 and SSA2 genes of the yeast Saccharomyces cerevisiae.";
RL Nucleic Acids Res. 17:805-806(1989).
RN [2]
RP SEQUENCE REVISION TO 208; 418 AND 422.
RA Slater M.R.;
RL Submitted (JUN-1993) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204511 / S288c / AB972;
RX PubMed=7941740; DOI=10.1002/yea.320100413;
RA Clark M.W., Keng T., Storms R.K., Zhong W.-W., Fortin N., Zeng B.,
RA Delaney S., Ouellette B.F.F., Barton A.B., Kaback D.B., Bussey H.;
RT "Sequencing of chromosome I of Saccharomyces cerevisiae: analysis of the 42
RT kbp SPO7-CENI-CDC15 region.";
RL Yeast 10:535-541(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7731988; DOI=10.1073/pnas.92.9.3809;
RA Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N.,
RA Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J.,
RA Storms R.K.;
RT "The nucleotide sequence of chromosome I from Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [6]
RP PROTEIN SEQUENCE OF 92-98 AND 326-342.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7895733; DOI=10.1002/elps.11501501210;
RA Garrels J.I., Futcher B., Kobayashi R., Latter G.I., Schwender B.,
RA Volpe T., Warner J.R., McLaughlin C.S.;
RT "Protein identifications for a Saccharomyces cerevisiae protein database.";
RL Electrophoresis 15:1466-1486(1994).
RN [7]
RP PROTEIN SEQUENCE OF 187-196.
RC STRAIN=ATCC 38531 / Y41;
RX PubMed=8935650; DOI=10.1111/j.1574-6968.1996.tb08073.x;
RA Norbeck J., Blomberg A.;
RT "Protein expression during exponential growth in 0.7 M NaCl medium of
RT Saccharomyces cerevisiae.";
RL FEMS Microbiol. Lett. 137:1-8(1996).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 591-642.
RX PubMed=6096826; DOI=10.1093/nar/12.24.9367;
RA Ogden R.C., Lee M.-C., Knapp G.;
RT "Transfer RNA splicing in Saccharomyces cerevisiae: defining the
RT substrates.";
RL Nucleic Acids Res. 12:9367-9382(1984).
RN [9]
RP ACETYLATION AT SER-2.
RX PubMed=9298649; DOI=10.1002/elps.1150180810;
RA Garrels J.I., McLaughlin C.S., Warner J.R., Futcher B., Latter G.I.,
RA Kobayashi R., Schwender B., Volpe T., Anderson D.S., Mesquita-Fuentes R.,
RA Payne W.E.;
RT "Proteome studies of Saccharomyces cerevisiae: identification and
RT characterization of abundant proteins.";
RL Electrophoresis 18:1347-1360(1997).
RN [10]
RP INTERACTION WITH PAB1 AND SIS1.
RX PubMed=11279042; DOI=10.1074/jbc.m100266200;
RA Horton L.E., James P., Craig E.A., Hensold J.O.;
RT "The yeast hsp70 homologue Ssa is required for translation and interacts
RT with Sis1 and Pab1 on translating ribosomes.";
RL J. Biol. Chem. 276:14426-14433(2001).
RN [11]
RP FUNCTION, AND INTERACTION WITH HUMAN HTN3.
RX PubMed=12761219; DOI=10.1074/jbc.m300680200;
RA Li X.S., Reddy M.S., Baev D., Edgerton M.;
RT "Candida albicans Ssa1/2p is the cell envelope binding protein for human
RT salivary histatin 5.";
RL J. Biol. Chem. 278:28553-28561(2003).
RN [12]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [13]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [15]
RP INTERACTION WITH NAP1, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18086883; DOI=10.1128/mcb.01035-07;
RA Calvert M.E.K., Keck K.M., Ptak C., Shabanowitz J., Hunt D.F.,
RA Pemberton L.F.;
RT "Phosphorylation by casein kinase 2 regulates Nap1 localization and
RT function.";
RL Mol. Cell. Biol. 28:1313-1325(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62 AND SER-603, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-551, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [18]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-556, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
CC -!- FUNCTION: May play a role in the transport of polypeptides both across
CC the mitochondrial membranes and into the endoplasmic reticulum. A
CC functional difference between SSA1 and SSA2 proteins is expected. SSA1
CC can participate in the ATP-dependent disassembly of clathrin-coated
CC vesicles. {ECO:0000269|PubMed:12761219}.
CC -!- SUBUNIT: Binds human HTN3/histatin-5, a peptide from saliva, and
CC mediates its fungicidal activity. Interacts with polyadenylate-binding
CC protein PAB1 and Hsp70 chaperone SSA1 on translating ribosomes.
CC Interacts with NAP1. {ECO:0000269|PubMed:11279042,
CC ECO:0000269|PubMed:12761219, ECO:0000269|PubMed:18086883}.
CC -!- INTERACTION:
CC P10591; P53940: APJ1; NbExp=2; IntAct=EBI-8591, EBI-2612341;
CC P10591; P35190: CLG1; NbExp=3; IntAct=EBI-8591, EBI-4762;
CC P10591; P38260: FES1; NbExp=3; IntAct=EBI-8591, EBI-21563;
CC P10591; P15108: HSC82; NbExp=2; IntAct=EBI-8591, EBI-8666;
CC P10591; P33416: HSP78; NbExp=2; IntAct=EBI-8591, EBI-8680;
CC P10591; P02829: HSP82; NbExp=3; IntAct=EBI-8591, EBI-8659;
CC P10591; P25693: PCL2; NbExp=3; IntAct=EBI-8591, EBI-4499;
CC P10591; P17157: PHO85; NbExp=2; IntAct=EBI-8591, EBI-13327;
CC P10591; Q01939: RPT6; NbExp=2; IntAct=EBI-8591, EBI-13914;
CC P10591; P25294: SIS1; NbExp=4; IntAct=EBI-8591, EBI-17244;
CC P10591; P32589: SSE1; NbExp=8; IntAct=EBI-8591, EBI-8648;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC Secreted, cell wall {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 269000 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR EMBL; X12926; CAA31393.1; -; Genomic_DNA.
DR EMBL; L22015; AAC04952.1; -; Genomic_DNA.
DR EMBL; BK006935; DAA06982.1; -; Genomic_DNA.
DR PIR; S43449; HHBYA1.
DR RefSeq; NP_009396.2; NM_001178151.1.
DR PDB; 3LCA; X-ray; 2.19 A; Q=631-642.
DR PDB; 5LYN; X-ray; 2.00 A; C/D=636-642.
DR PDB; 5Z8I; NMR; -; A=382-554.
DR PDB; 5Z8Q; NMR; -; A=523-622.
DR PDBsum; 3LCA; -.
DR PDBsum; 5LYN; -.
DR PDBsum; 5Z8I; -.
DR PDBsum; 5Z8Q; -.
DR AlphaFoldDB; P10591; -.
DR SMR; P10591; -.
DR BioGRID; 31786; 928.
DR ComplexPortal; CPX-1276; HMC complex.
DR ComplexPortal; CPX-1882; HAP1 transcriptional repressor complex, SSA1 variant.
DR DIP; DIP-2253N; -.
DR IntAct; P10591; 583.
DR MINT; P10591; -.
DR STRING; 4932.YAL005C; -.
DR ChEMBL; CHEMBL5186; -.
DR TCDB; 3.A.16.1.6; the endoplasmic reticular retrotranslocon (er-rt) family.
DR CarbonylDB; P10591; -.
DR iPTMnet; P10591; -.
DR COMPLUYEAST-2DPAGE; P10591; -.
DR SWISS-2DPAGE; P10591; -.
DR MaxQB; P10591; -.
DR PaxDb; P10591; -.
DR PRIDE; P10591; -.
DR EnsemblFungi; YAL005C_mRNA; YAL005C; YAL005C.
DR GeneID; 851259; -.
DR KEGG; sce:YAL005C; -.
DR SGD; S000000004; SSA1.
DR VEuPathDB; FungiDB:YAL005C; -.
DR eggNOG; KOG0101; Eukaryota.
DR GeneTree; ENSGT00940000176322; -.
DR HOGENOM; CLU_005965_7_0_1; -.
DR InParanoid; P10591; -.
DR OMA; KANPIMM; -.
DR BioCyc; YEAST:G3O-28819-MON; -.
DR Reactome; R-SCE-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-SCE-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-SCE-3371568; Attenuation phase.
DR EvolutionaryTrace; P10591; -.
DR PRO; PR:P10591; -.
DR Proteomes; UP000002311; Chromosome I.
DR RNAct; P10591; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0009277; C:fungal-type cell wall; IDA:SGD.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0005886; C:plasma membrane; HDA:SGD.
DR GO; GO:0005844; C:polysome; IDA:SGD.
DR GO; GO:0017053; C:transcription repressor complex; IC:ComplexPortal.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:SGD.
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:0000049; F:tRNA binding; IDA:SGD.
DR GO; GO:0051082; F:unfolded protein binding; IDA:SGD.
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:0072318; P:clathrin coat disassembly; IDA:SGD.
DR GO; GO:0002181; P:cytoplasmic translation; IMP:SGD.
DR GO; GO:0072671; P:mitochondria-associated ubiquitin-dependent protein catabolic process; IMP:SGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IMP:SGD.
DR GO; GO:0006457; P:protein folding; IDA:SGD.
DR GO; GO:0006606; P:protein import into nucleus; IDA:SGD.
DR GO; GO:0000209; P:protein polyubiquitination; IDA:SGD.
DR GO; GO:0042026; P:protein refolding; IDA:SGD.
DR GO; GO:0006626; P:protein targeting to mitochondrion; IMP:SGD.
DR GO; GO:0070482; P:response to oxygen levels; IC:ComplexPortal.
DR GO; GO:0006616; P:SRP-dependent cotranslational protein targeting to membrane, translocation; IDA:SGD.
DR GO; GO:0035617; P:stress granule disassembly; IDA:SGD.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
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 3D-structure; Acetylation; ATP-binding; Cell wall; Cytoplasm;
KW Direct protein sequencing; Isopeptide bond; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Secreted; Stress response;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9298649"
FT CHAIN 2..642
FT /note="Heat shock protein SSA1"
FT /id="PRO_0000078385"
FT REGION 606..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:9298649"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 551
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 603
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CROSSLNK 556
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CONFLICT 208
FT /note="S -> F (in Ref. 3; AAC04952)"
FT /evidence="ECO:0000305"
FT CONFLICT 418
FT /note="P -> S (in Ref. 3; AAC04952)"
FT /evidence="ECO:0000305"
FT CONFLICT 422
FT /note="S -> F (in Ref. 3; AAC04952)"
FT /evidence="ECO:0000305"
FT STRAND 384..386
FT /evidence="ECO:0007829|PDB:5Z8I"
FT STRAND 398..402
FT /evidence="ECO:0007829|PDB:5Z8I"
FT TURN 403..405
FT /evidence="ECO:0007829|PDB:5Z8I"
FT STRAND 406..411
FT /evidence="ECO:0007829|PDB:5Z8I"
FT STRAND 416..428
FT /evidence="ECO:0007829|PDB:5Z8I"
FT STRAND 433..443
FT /evidence="ECO:0007829|PDB:5Z8I"
FT HELIX 447..449
FT /evidence="ECO:0007829|PDB:5Z8I"
FT STRAND 450..459
FT /evidence="ECO:0007829|PDB:5Z8I"
FT STRAND 471..477
FT /evidence="ECO:0007829|PDB:5Z8I"
FT STRAND 482..489
FT /evidence="ECO:0007829|PDB:5Z8I"
FT TURN 490..492
FT /evidence="ECO:0007829|PDB:5Z8I"
FT STRAND 495..502
FT /evidence="ECO:0007829|PDB:5Z8I"
FT HELIX 509..521
FT /evidence="ECO:0007829|PDB:5Z8I"
FT HELIX 523..533
FT /evidence="ECO:0007829|PDB:5Z8I"
FT STRAND 537..542
FT /evidence="ECO:0007829|PDB:5Z8I"
FT TURN 554..556
FT /evidence="ECO:0007829|PDB:5Z8Q"
FT HELIX 559..578
FT /evidence="ECO:0007829|PDB:5Z8Q"
FT HELIX 584..609
FT /evidence="ECO:0007829|PDB:5Z8Q"
FT STRAND 614..616
FT /evidence="ECO:0007829|PDB:5Z8Q"
SQ SEQUENCE 642 AA; 69657 MW; 249D8A3BC42527CA CRC64;
MSKAVGIDLG TTYSCVAHFA NDRVDIIAND QGNRTTPSFV AFTDTERLIG DAAKNQAAMN
PSNTVFDAKR LIGRNFNDPE VQADMKHFPF KLIDVDGKPQ IQVEFKGETK NFTPEQISSM
VLGKMKETAE SYLGAKVNDA VVTVPAYFND SQRQATKDAG TIAGLNVLRI INEPTAAAIA
YGLDKKGKEE HVLIFDLGGG TFDVSLLSIE DGIFEVKATA GDTHLGGEDF DNRLVNHFIQ
EFKRKNKKDL STNQRALRRL RTACERAKRT LSSSAQTSVE IDSLFEGIDF YTSITRARFE
ELCADLFRST LDPVEKVLRD AKLDKSQVDE IVLVGGSTRI PKVQKLVTDY FNGKEPNRSI
NPDEAVAYGA AVQAAILTGD ESSKTQDLLL LDVAPLSLGI ETAGGVMTKL IPRNSTIPTK
KSEIFSTYAD NQPGVLIQVF EGERAKTKDN NLLGKFELSG IPPAPRGVPQ IEVTFDVDSN
GILNVSAVEK GTGKSNKITI TNDKGRLSKE DIEKMVAEAE KFKEEDEKES QRIASKNQLE
SIAYSLKNTI SEAGDKLEQA DKDTVTKKAE ETISWLDSNT TASKEEFDDK LKELQDIANP
IMSKLYQAGG APGGAAGGAP GGFPGGAPPA PEAEGPTVEE VD
