ID   HSP71_CRYNJ             Reviewed;         640 AA.
AC   Q5KKP4; Q55VJ4;
DT   10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Transcriptional coregulator SSA1 {ECO:0000303|PubMed:17040492};
GN   Name=SSA1 {ECO:0000303|PubMed:17040492};
GN   OrderedLocusNames=CNC02320 {ECO:0000312|EMBL:AAW42202.1};
OS   Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS   MYA-565) (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=214684 {ECO:0000312|Proteomes:UP000002149};
RN   [1] {ECO:0000312|Proteomes:UP000002149}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JEC21 / ATCC MYA-565 {ECO:0000312|Proteomes:UP000002149};
RX   PubMed=15653466; DOI=10.1126/science.1103773;
RA   Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA   Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA   Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA   Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA   Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA   Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA   Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA   Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA   Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA   Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT   "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT   neoformans.";
RL   Science 307:1321-1324(2005).
RN   [2] {ECO:0000305}
RP   FUNCTION, INTERACTION WITH HSF1, SUBCELLULAR LOCATION, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=17040492; DOI=10.1111/j.1365-2958.2006.05422.x;
RA   Zhang S., Hacham M., Panepinto J., Hu G., Shin S., Zhu X., Williamson P.R.;
RT   "The Hsp70 member, Ssa1, acts as a DNA-binding transcriptional co-activator
RT   of laccase in Cryptococcus neoformans.";
RL   Mol. Microbiol. 62:1090-1101(2006).
RN   [3] {ECO:0000305}
RP   DISRUPTION PHENOTYPE.
RX   PubMed=25972480; DOI=10.4049/jimmunol.1402719;
RA   Eastman A.J., He X., Qiu Y., Davis M.J., Vedula P., Lyons D.M., Park Y.D.,
RA   Hardison S.E., Malachowski A.N., Osterholzer J.J., Wormley F.L. Jr.,
RA   Williamson P.R., Olszewski M.A.;
RT   "Cryptococcal heat shock protein 70 homolog Ssa1 contributes to pulmonary
RT   expansion of Cryptococcus neoformans during the afferent phase of the
RT   immune response by promoting macrophage M2 polarization.";
RL   J. Immunol. 194:5999-6010(2015).
CC   -!- FUNCTION: Transcriptional coregulator that functions together with
CC       transcription factor HSF1 (PubMed:17040492). Positively regulates the
CC       expression of laccase LAC1 during glucose starvation (PubMed:17040492).
CC       {ECO:0000269|PubMed:17040492}.
CC   -!- SUBUNIT: Interacts with transcription factor HSF1 on chromatin.
CC       {ECO:0000269|PubMed:17040492}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17040492}.
CC   -!- DISRUPTION PHENOTYPE: Abolishes LAC1 expression and activity during
CC       glucose starvation (PubMed:17040492). Abolishes laccase activity during
CC       calcium stress and iron stress (PubMed:17040492). Severely decreases
CC       laccase activity during copper stress (PubMed:17040492). Melanin absent
CC       from cell (PubMed:25972480). Decreases virulence in a mouse intravenous
CC       inoculation model of infection (PubMed:17040492).
CC       {ECO:0000269|PubMed:17040492, ECO:0000269|PubMed:25972480}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC       {ECO:0000255|RuleBase:RU003322}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE017343; AAW42202.1; -; Genomic_DNA.
DR   RefSeq; XP_569509.1; XM_569509.1.
DR   AlphaFoldDB; Q5KKP4; -.
DR   SMR; Q5KKP4; -.
DR   STRING; 5207.AAW42202; -.
DR   PaxDb; Q5KKP4; -.
DR   EnsemblFungi; AAW42202; AAW42202; CNC02320.
DR   GeneID; 3256505; -.
DR   KEGG; cne:CNC02320; -.
DR   VEuPathDB; FungiDB:CNC02320; -.
DR   eggNOG; KOG0101; Eukaryota.
DR   HOGENOM; CLU_005965_3_2_1; -.
DR   InParanoid; Q5KKP4; -.
DR   OMA; KANPIMM; -.
DR   OrthoDB; 288077at2759; -.
DR   Proteomes; UP000002149; Chromosome 3.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
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:0003712; F:transcription coregulator activity; IDA:UniProtKB.
DR   GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
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: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   ATP-binding; Nucleotide-binding; Nucleus; Reference proteome;
KW   Stress response; Transcription; Transcription regulation.
FT   CHAIN           1..640
FT                   /note="Transcriptional coregulator SSA1"
FT                   /id="PRO_0000452019"
FT   REGION          606..640
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   640 AA;  69353 MW;  C3B5F2AA81F25A98 CRC64;
     MVKAVGIDLG TTYSCVAVWQ NDRVEIIAND QGNRTTPSYV AFNDSERLIG DAAKNQVAMN
     PYNTVFDAKR LIGRKFEDAE VQADMKHWPF KVIDRAGKPA IQVEYRGEEK VFTPEEISSM
     VLIKMKETAE AYLGGTVSKA VVTVPAYFND SQRQATKDAG AIAGLDVLRI INEPTAAAIA
     YGLDKKSEGE KNVLIFDLGG GTFDVSLLTI EEGIFEVKAT AGDTHLGGED FDNRLVNHFV
     QEFKRKNKKD LSSNARALRR LRTACERAKR TLSSAAQTSI EIDSLFDGID FYTSITRARF
     EELCQDLFRS TMDPVEKVLR DSKIDKSSVN EIVLVGGSTR IPKIQKLVSD MFSGREPNRS
     INPDEAVAYG AAVQAAILTG DTSEATQDLL LLDVAPLSMG IETAGGIMTP LIKRNTTVPT
     KKSEVFSTYS DNQPGVLIQV FEGERAKTKD CNLLGKFDLS GIPPAPRGVP QIEVSFDVDA
     NGILNVNAAD KSTGKSSKIT ITNDKGRLSK EEIERMLAEA EKFKAEDEAA AATVQAKNGL
     ESYSYSLKTT LSDNQDKFDA ADHETLSKKV DEVISSLDTM QSASKEEFES LQKELEAVAN
     PIMTKFYGAQ GGAPGGAPGG FPGAGGAPAQ EEGPSVEEVD