SSK1_CANAL
ID SSK1_CANAL Reviewed; 674 AA.
AC Q5AKU6; A0A1D8PFT0; G1UA00; Q9UVW6;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=Oxidative stress response two-component system protein SSK1;
GN Name=SSK1; OrderedLocusNames=CAALFM_C113930WA;
GN ORFNames=CaO19.12498, CaO19.5031;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=10487927;
RX DOI=10.1002/(sici)1097-0061(19990915)15:12<1243::aid-yea449>3.0.co;2-5;
RA Calera J.A., Calderone R.A.;
RT "Identification of a putative response regulator two-component phosphorelay
RT gene (CaSSK1) from Candida albicans.";
RL Yeast 15:1243-1254(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=10865904;
RA Calera J.A., Calderone R.;
RT "Histidine kinase, two-component signal transduction proteins of Candida
RT albicans and the pathogenesis of candidosis.";
RL Mycoses 42:49-53(1999).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=10639412; DOI=10.1128/iai.68.2.518-525.2000;
RA Calera J.A., Zhao X.J., Calderone R.;
RT "Defective hyphal development and avirulence caused by a deletion of the
RT SSK1 response regulator gene in Candida albicans.";
RL Infect. Immun. 68:518-525(2000).
RN [7]
RP DISRUPTION PHENOTYPE, AND INDUCTION.
RX PubMed=11854244; DOI=10.1128/iai.70.3.1558-1565.2002;
RA Li D., Bernhardt J., Calderone R.;
RT "Temporal expression of the Candida albicans genes CHK1 and CSSK1,
RT adherence, and morphogenesis in a model of reconstituted human esophageal
RT epithelial candidiasis.";
RL Infect. Immun. 70:1558-1565(2002).
RN [8]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=15470110; DOI=10.1099/mic.0.27237-0;
RA Li D., Gurkovska V., Sheridan M., Calderone R., Chauhan N.;
RT "Studies on the regulation of the two-component histidine kinase gene CHK1
RT in Candida albicans using the heterologous lacZ reporter gene.";
RL Microbiology 150:3305-3313(2004).
RN [9]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=15664927; DOI=10.1128/iai.73.2.865-871.2005;
RA Du C., Calderone R., Richert J., Li D.;
RT "Deletion of the SSK1 response regulator gene in Candida albicans
RT contributes to enhanced killing by human polymorphonuclear neutrophils.";
RL Infect. Immun. 73:865-871(2005).
RN [10]
RP FUNCTION, MUTAGENESIS OF ASP-513 AND ASP-556, AND PHOSPHORYLATION AT
RP ASP-556.
RX PubMed=17038117; DOI=10.1111/j.1365-2958.2006.05438.x;
RA Menon V., Li D., Chauhan N., Rajnarayanan R., Dubrovska A., West A.H.,
RA Calderone R.;
RT "Functional studies of the Ssk1p response regulator protein of Candida
RT albicans as determined by phenotypic analysis of receiver domain point
RT mutants.";
RL Mol. Microbiol. 62:997-1013(2006).
RN [11]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=17664325; DOI=10.1128/aac.00929-07;
RA Chauhan N., Kruppa M., Calderone R.;
RT "The Ssk1p response regulator and Chk1p histidine kinase mutants of Candida
RT albicans are hypersensitive to fluconazole and voriconazole.";
RL Antimicrob. Agents Chemother. 51:3747-3751(2007).
RN [12]
RP FUNCTION, AND MUTAGENESIS OF ASP-513 AND ASP-556.
RX PubMed=18616606; DOI=10.1111/j.1567-1364.2008.00404.x;
RA Menon V., De Bernardis F., Calderone R., Chauhan N.;
RT "Transcriptional profiling of the Candida albicans Ssk1p receiver domain
RT point mutants and their virulence.";
RL FEMS Yeast Res. 8:756-763(2008).
CC -!- FUNCTION: Final receptor of the SLN1-YPD1-SSK1 two-component regulatory
CC system, which controls activity of the HOG1 pathway in response to
CC oxidative stress and probably also to the osmolarity of the
CC extracellular environment. Involved in cell wall biosynthesis, hyphal
CC growth, and virulence. Regulates the expression of CHK1, as well as of
CC a subset of genes whose functions are associated with cell wall
CC biosynthesis and adaptation to oxidative stress. Provides at least
CC partial adaptive functions for the survival following encounter with
CC human neutrophils. {ECO:0000269|PubMed:10639412,
CC ECO:0000269|PubMed:10865904, ECO:0000269|PubMed:15470110,
CC ECO:0000269|PubMed:15664927, ECO:0000269|PubMed:17038117,
CC ECO:0000269|PubMed:17664325, ECO:0000269|PubMed:18616606}.
CC -!- INDUCTION: Expression is detected as early as 1 hour after infection of
CC reconstituted human esophageal tissue and increases thereafter up to 48
CC hours postinfection. {ECO:0000269|PubMed:11854244}.
CC -!- DISRUPTION PHENOTYPE: Leads to flocculation, attenuated virulence
CC towards reconstituted human esophageal tissue, and to hypersensitivity
CC to fluconazole and voriconazole. {ECO:0000269|PubMed:10639412,
CC ECO:0000269|PubMed:10865904, ECO:0000269|PubMed:11854244,
CC ECO:0000269|PubMed:15470110, ECO:0000269|PubMed:15664927,
CC ECO:0000269|PubMed:17664325}.
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; AF084608; AAD55813.1; -; Genomic_DNA.
DR EMBL; CP017623; AOW26994.1; -; Genomic_DNA.
DR RefSeq; XP_722233.1; XM_717140.1.
DR AlphaFoldDB; Q5AKU6; -.
DR SMR; Q5AKU6; -.
DR STRING; 237561.Q5AKU6; -.
DR PRIDE; Q5AKU6; -.
DR GeneID; 3636184; -.
DR KEGG; cal:CAALFM_C113930WA; -.
DR CGD; CAL0000190567; SSK1.
DR VEuPathDB; FungiDB:C1_13930W_A; -.
DR eggNOG; KOG0519; Eukaryota.
DR HOGENOM; CLU_008307_4_0_1; -.
DR InParanoid; Q5AKU6; -.
DR OMA; RAGCNDY; -.
DR OrthoDB; 1053761at2759; -.
DR PHI-base; PHI:189; -.
DR PHI-base; PHI:3020; -.
DR PRO; PR:Q5AKU6; -.
DR Proteomes; UP000000559; Chromosome 1.
DR GO; GO:0000156; F:phosphorelay response regulator activity; IMP:CGD.
DR GO; GO:0034605; P:cellular response to heat; IMP:CGD.
DR GO; GO:0036244; P:cellular response to neutral pH; IMP:CGD.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:CGD.
DR GO; GO:0009267; P:cellular response to starvation; IMP:CGD.
DR GO; GO:0042783; P:evasion of host immune response; IMP:CGD.
DR GO; GO:0030447; P:filamentous growth; IMP:CGD.
DR GO; GO:0044182; P:filamentous growth of a population of unicellular organisms; IMP:CGD.
DR GO; GO:0036180; P:filamentous growth of a population of unicellular organisms in response to biotic stimulus; IMP:CGD.
DR GO; GO:0036178; P:filamentous growth of a population of unicellular organisms in response to neutral pH; IMP:CGD.
DR GO; GO:0036170; P:filamentous growth of a population of unicellular organisms in response to starvation; IMP:CGD.
DR GO; GO:0031505; P:fungal-type cell wall organization; IMP:CGD.
DR GO; GO:0000160; P:phosphorelay signal transduction system; ISS:CGD.
DR GO; GO:1900445; P:positive regulation of filamentous growth of a population of unicellular organisms in response to biotic stimulus; IMP:CGD.
DR GO; GO:1900442; P:positive regulation of filamentous growth of a population of unicellular organisms in response to neutral pH; IMP:CGD.
DR GO; GO:1900436; P:positive regulation of filamentous growth of a population of unicellular organisms in response to starvation; IMP:CGD.
DR GO; GO:1900428; P:regulation of filamentous growth of a population of unicellular organisms; IMP:CGD.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR Pfam; PF00072; Response_reg; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 1: Evidence at protein level;
KW Phosphoprotein; Reference proteome; Stress response;
KW Two-component regulatory system; Virulence.
FT CHAIN 1..674
FT /note="Oxidative stress response two-component system
FT protein SSK1"
FT /id="PRO_0000425802"
FT DOMAIN 507..653
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT REGION 66..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 372..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..388
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..412
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..448
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..494
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 556
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169,
FT ECO:0000269|PubMed:17038117"
FT MUTAGEN 513
FT /note="D->K: Impairs filamentation and decreases
FT virulence."
FT /evidence="ECO:0000269|PubMed:17038117,
FT ECO:0000269|PubMed:18616606"
FT MUTAGEN 556
FT /note="D->N: Leads to sensitivity to H(2)O(2) and t-butyl
FT hydroperoxide and decreases virulence."
FT /evidence="ECO:0000269|PubMed:17038117,
FT ECO:0000269|PubMed:18616606"
SQ SEQUENCE 674 AA; 73560 MW; A9BBBE500DA64510 CRC64;
MNFLYNNSDY SSTSHTMKSP SAYNQFPKLQ ASNSTAGNNN TATTATAAAA AASASASASV
TPQLISPTTL TTPQNKYKRG GLDNTLPKIE TTRKNRPDDG NSITPSNSIN SGTTKLTLPP
RRVWVKKPQT NNPTTVLCYV NDIIDDLKVA VVNKYPNTIG RYEDAADLLV KIDLNNIRVP
VSPSVNRVSQ RTPFDNCIIL EPDQNVWQIL DNYFPNGMAM HDALIIETPT FKPDHQMLTP
ITANMNNNSN TFIPFQERQS SIGNNNNNNS NVNNNNKAQA VKHPQPMQPN NTRVGLHKSY
AMNRSSFSTN NNPVPSIIKD RSVSPSNLGV SRNSPVSHKR SYSNPVSSPN SVATQANNPS
AVLLLPRNFS LANNNSNQAS QSSGGTPAKK VLSEDGSKSV NDKTEEVVSS KLKPNDNNKS
YQAKQQEQQT AEQSENGFSE TSASPEAVHN SKAAPLPLTK SSTTATTTSS NSISNNNNTS
SKGKPSQSKL KAANDPTPTD IVLPSISVLV VEDNAINQAI LGAFLRKRKI HYQIAKNGQE
AIDKWKKGGF HLVLMDIQLP VKSGIEATKE IRHLEKLNRI GVFHENEIGK NVIINEEDRL
TSNTFRSPVI IVALTASSNS SVDKTNALTA GCNDYLTKPV NLVWLQNKIT EWGCMQALID
FDGWKDKNRR LNKA