ID   HSP72_YEAST             Reviewed;         639 AA.
AC   P10592; D6VXY0;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   27-MAR-2024, entry version 237.
DE   RecName: Full=Heat shock protein SSA2;
GN   Name=SSA2; OrderedLocusNames=YLL024C; ORFNames=L0931;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9046100;
RX   DOI=10.1002/(sici)1097-0061(199702)13:2<183::aid-yea65>3.0.co;2-v;
RA   Purnelle B., Goffeau A.;
RT   "The sequence of 32kb on the left arm of yeast chromosome XII reveals six
RT   known genes, a new member of the seripauperins family and a new ABC
RT   transporter homologous to the human multidrug resistance protein.";
RL   Yeast 13:183-188(1997).
RN   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169871;
RA   Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA   Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA   Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA   Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA   Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA   Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA   Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA   Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA   Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA   Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA   Zollner A., Hani J., Hoheisel J.D.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL   Nature 387:87-90(1997).
RN   [5]
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   [6]
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   [7]
RP   ACETYLATION AT SER-2, AND PHOSPHORYLATION.
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   [8]
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   [9]
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   [10]
RP   UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-556, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RC   STRAIN=SUB592;
RX   PubMed=12872131; DOI=10.1038/nbt849;
RA   Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G.,
RA   Roelofs J., Finley D., Gygi S.P.;
RT   "A proteomics approach to understanding protein ubiquitination.";
RL   Nat. Biotechnol. 21:921-926(2003).
RN   [11]
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   [12]
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   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, AND IDENTIFICATION BY
RP   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   [14]
RP   IDENTIFICATION BY 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   [15]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [16]
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. SSA2
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 NAP1.
CC       {ECO:0000269|PubMed:12761219, ECO:0000269|PubMed:18086883}.
CC   -!- INTERACTION:
CC       P10592; P53940: APJ1; NbExp=2; IntAct=EBI-8603, EBI-2612341;
CC       P10592; P18900: COQ1; NbExp=2; IntAct=EBI-8603, EBI-4912;
CC       P10592; P22696: ESS1; NbExp=2; IntAct=EBI-8603, EBI-6679;
CC       P10592; P02829: HSP82; NbExp=2; IntAct=EBI-8603, EBI-8659;
CC       P10592; P17505: MDH1; NbExp=2; IntAct=EBI-8603, EBI-10594;
CC       P10592; P25294: SIS1; NbExp=2; IntAct=EBI-8603, EBI-17244;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Secreted, cell wall.
CC   -!- MISCELLANEOUS: Present with 364000 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; X12927; CAA31394.1; -; Genomic_DNA.
DR   EMBL; Z73129; CAA97472.1; -; Genomic_DNA.
DR   EMBL; X97560; CAA66167.1; -; Genomic_DNA.
DR   EMBL; BK006945; DAA09296.1; -; Genomic_DNA.
DR   PIR; S20139; S20139.
DR   RefSeq; NP_013076.1; NM_001181844.1.
DR   AlphaFoldDB; P10592; -.
DR   SMR; P10592; -.
DR   BioGRID; 31229; 569.
DR   ComplexPortal; CPX-1276; HMC complex.
DR   ComplexPortal; CPX-1883; HAP1 transcriptional repressor complex, SSA2 variant.
DR   DIP; DIP-2265N; -.
DR   IntAct; P10592; 972.
DR   MINT; P10592; -.
DR   STRING; 4932.YLL024C; -.
DR   CarbonylDB; P10592; -.
DR   iPTMnet; P10592; -.
DR   MaxQB; P10592; -.
DR   PaxDb; 4932-YLL024C; -.
DR   PeptideAtlas; P10592; -.
DR   EnsemblFungi; YLL024C_mRNA; YLL024C; YLL024C.
DR   GeneID; 850636; -.
DR   KEGG; sce:YLL024C; -.
DR   AGR; SGD:S000003947; -.
DR   SGD; S000003947; SSA2.
DR   VEuPathDB; FungiDB:YLL024C; -.
DR   eggNOG; KOG0101; Eukaryota.
DR   GeneTree; ENSGT00940000176322; -.
DR   HOGENOM; CLU_005965_7_0_1; -.
DR   InParanoid; P10592; -.
DR   OMA; VNEAESY; -.
DR   OrthoDB; 143at2759; -.
DR   BioCyc; YEAST:G3O-32128-MONOMER; -.
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   Reactome; R-SCE-3371571; HSF1-dependent transactivation.
DR   Reactome; R-SCE-6798695; Neutrophil degranulation.
DR   BioGRID-ORCS; 850636; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P10592; -.
DR   Proteomes; UP000002311; Chromosome XII.
DR   RNAct; P10592; Protein.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0005829; C:cytosol; IDA: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:0005739; C:mitochondrion; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; HDA:SGD.
DR   GO; GO:0017053; C:transcription repressor complex; NAS:ComplexPortal.
DR   GO; GO:0005524; F:ATP binding; IDA:SGD.
DR   GO; GO:0016887; F:ATP hydrolysis activity; ISS: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: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; IGI:SGD.
DR   GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; NAS:ComplexPortal.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IGI:SGD.
DR   GO; GO:0006457; P:protein folding; IDA:SGD.
DR   GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR   GO; GO:0070482; P:response to oxygen levels; NAS:ComplexPortal.
DR   GO; GO:0006616; P:SRP-dependent cotranslational protein targeting to membrane, translocation; IMP:SGD.
DR   GO; GO:0035719; P:tRNA import into nucleus; IMP:SGD.
DR   CDD; cd10233; HSPA1-2_6-8-like_NBD; 1.
DR   Gene3D; 1.20.1270.10; -; 1.
DR   Gene3D; 3.30.30.30; -; 1.
DR   Gene3D; 3.30.420.40; -; 2.
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:SF395; HEAT SHOCK 70 KDA PROTEIN COGNATE 1-RELATED; 1.
DR   PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   PRINTS; PR00301; HEATSHOCK70.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   SUPFAM; SSF100934; Heat shock protein 70kD (HSP70), C-terminal subdomain; 1.
DR   SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 1.
DR   PROSITE; PS00297; HSP70_1; 1.
DR   PROSITE; PS00329; HSP70_2; 1.
DR   PROSITE; PS01036; HSP70_3; 1.
DR   COMPLUYEAST-2DPAGE; P10592; -.
DR   SWISS-2DPAGE; P10592; -.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Cell wall; Cytoplasm; Direct protein sequencing;
KW   Isopeptide bond; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW   Secreted; Stress response; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:9298649,
FT                   ECO:0007744|PubMed:22814378"
FT   CHAIN           2..639
FT                   /note="Heat shock protein SSA2"
FT                   /id="PRO_0000078386"
FT   REGION          605..639
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                   ECO:0007744|PubMed:22814378"
FT   MOD_RES         20
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         551
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P10591"
FT   MOD_RES         603
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P10591"
FT   CROSSLNK        556
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0007744|PubMed:22106047"
SQ   SEQUENCE   639 AA;  69470 MW;  129049E21C9DD1F3 CRC64;
     MSKAVGIDLG TTYSCVAHFS NDRVDIIAND QGNRTTPSFV GFTDTERLIG DAAKNQAAMN
     PANTVFDAKR LIGRNFNDPE VQGDMKHFPF 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
     KSEVFSTYAD NQPGVLIQVF EGERAKTKDN NLLGKFELSG IPPAPRGVPQ IEVTFDVDSN
     GILNVSAVEK GTGKSNKITI TNDKGRLSKE DIEKMVAEAE KFKEEDEKES QRIASKNQLE
     SIAYSLKNTI SEAGDKLEQA DKDAVTKKAE ETIAWLDSNT TATKEEFDDQ LKELQEVANP
     IMSKLYQAGG APEGAAPGGF PGGAPPAPEA EGPTVEEVD
//