NIK1_CANAL
ID NIK1_CANAL Reviewed; 1081 AA.
AC Q5A599; A0A1D8PR54; Q3MP73;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 3.
DT 25-MAY-2022, entry version 124.
DE RecName: Full=Histidine protein kinase NIK1;
DE EC=2.7.13.3;
GN Name=NIK1; Synonyms=COS1, HIK1; OrderedLocusNames=CAALFM_C702800WA;
GN ORFNames=CaO19.12648, CaO19.5181;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15937140; DOI=10.1534/genetics.104.034652;
RA Chibana H., Oka N., Nakayama H., Aoyama T., Magee B.B., Magee P.T.,
RA Mikami Y.;
RT "Sequence finishing and gene mapping for Candida albicans chromosome 7 and
RT syntenic analysis against the Saccharomyces cerevisiae genome.";
RL Genetics 170:1525-1537(2005).
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 INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=9802013; DOI=10.1099/00221287-144-10-2715;
RA Srikantha T., Tsai L., Daniels K., Enger L., Highley K., Soll D.R.;
RT "The two-component hybrid kinase regulator CaNIK1 of Candida albicans.";
RL Microbiology 144:2715-2729(1998).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=9618540; DOI=10.1073/pnas.95.12.7069;
RA Alex L.A., Korch C., Selitrennikoff C.P., Simon M.I.;
RT "COS1, a two-component histidine kinase that is involved in hyphal
RT development in the opportunistic pathogen Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:7069-7073(1998).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND AUTOPHOSPHORYLATION.
RX PubMed=10572127; DOI=10.1128/jb.181.23.7243-7247.1999;
RA Yamada-Okabe T., Mio T., Ono N., Kashima Y., Matsui M., Arisawa M.,
RA Yamada-Okabe H.;
RT "Roles of three histidine kinase genes in hyphal development and virulence
RT of the pathogenic fungus Candida albicans.";
RL J. Bacteriol. 181:7243-7247(1999).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11270409; DOI=10.1080/mmy.39.1.69.74;
RA Selitrennikoff C.P., Alex L., Miller T.K., Clemons K.V., Simon M.I.,
RA Stevens D.A.;
RT "COS-l, a putative two-component histidine kinase of Candida albicans, is
RT an in vivo virulence factor.";
RL Med. Mycol. 39:69-74(2001).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=14734021; DOI=10.1016/s1567-1356(03)00201-0;
RA Kruppa M., Jabra-Rizk M.A., Meiller T.F., Calderone R.;
RT "The histidine kinases of Candida albicans: regulation of cell wall mannan
RT biosynthesis.";
RL FEMS Yeast Res. 4:409-416(2004).
RN [10]
RP FUNCTION, AND DOMAIN.
RX PubMed=21963586; DOI=10.1016/j.jbiotec.2011.09.017;
RA Buschart A., Gremmer K., El-Mowafy M., van den Heuvel J., Mueller P.P.,
RA Bilitewski U.;
RT "A novel functional assay for fungal histidine kinases group III reveals
RT the role of HAMP domains for fungicide sensitivity.";
RL J. Biotechnol. 157:268-277(2012).
RN [11]
RP FUNCTION, AND DOMAIN.
RX PubMed=24044701; DOI=10.1186/1471-2180-13-209;
RA El-Mowafy M., Bahgat M.M., Bilitewski U.;
RT "Deletion of the HAMP domains from the histidine kinase CaNik1p of Candida
RT albicans or treatment with fungicides activates the MAP kinase Hog1p in S.
RT cerevisiae transformants.";
RL BMC Microbiol. 13:209-209(2013).
CC -!- FUNCTION: Histidine kinase involved in a two-component signaling
CC pathway that regulates cell wall mannan biosynthesis. Required for
CC hyphal formation and virulence. Plays a role in fungicides sensitivity,
CC probably through the positive regulation of the HOG1-signaling pathway.
CC Presumed to mediate phosphotransfer to the HOG1 MAP kinase pathway
CC during oxidative and perhaps osmotic stress.
CC {ECO:0000269|PubMed:10572127, ECO:0000269|PubMed:11270409,
CC ECO:0000269|PubMed:14734021, ECO:0000269|PubMed:21963586,
CC ECO:0000269|PubMed:24044701, ECO:0000269|PubMed:9618540}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: Expression is increased in opaque cells.
CC {ECO:0000269|PubMed:9802013}.
CC -!- DOMAIN: The HAMP domains are critical for the sensitivity to fungicides
CC such as fludioxonil, as well as for activation of HOG1.
CC {ECO:0000269|PubMed:21963586, ECO:0000269|PubMed:24044701}.
CC -!- PTM: The phosphorelay mechanism involves the sequential transfer of a
CC phosphate group from His-510 (H1) in the histidine kinase domain
CC (transmitter domain) to Asp-924 (D1) of the response regulatory domain
CC (receiver domain). This transfer probably occurs between two NIK1
CC molecules, rather than intramolecularly (By similarity). {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Impairs the hyphal formation and attenuates the
CC virulence in a mouse systemic candidiasis model.
CC {ECO:0000269|PubMed:10572127, ECO:0000269|PubMed:11270409,
CC ECO:0000269|PubMed:14734021, ECO:0000269|PubMed:9618540,
CC ECO:0000269|PubMed:9802013}.
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DR EMBL; AP006852; BAE44787.1; -; Genomic_DNA.
DR EMBL; CP017629; AOW30628.1; -; Genomic_DNA.
DR RefSeq; XP_717003.2; XM_711910.2.
DR AlphaFoldDB; Q5A599; -.
DR SMR; Q5A599; -.
DR STRING; 237561.Q5A599; -.
DR PRIDE; Q5A599; -.
DR GeneID; 3641358; -.
DR KEGG; cal:CAALFM_C702800WA; -.
DR CGD; CAL0000187540; NIK1.
DR VEuPathDB; FungiDB:C7_02800W_A; -.
DR eggNOG; KOG0519; Eukaryota.
DR HOGENOM; CLU_000445_3_1_1; -.
DR InParanoid; Q5A599; -.
DR OrthoDB; 27870at2759; -.
DR Proteomes; UP000000559; Chromosome 7.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000156; F:phosphorelay response regulator activity; ISS:CGD.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; ISS:CGD.
DR GO; GO:0004673; F:protein histidine kinase activity; IDA:CGD.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0071474; P:cellular hyperosmotic response; IBA:GO_Central.
DR GO; GO:0097308; P:cellular response to farnesol; IMP:CGD.
DR GO; GO:0030447; P:filamentous growth; 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:0036170; P:filamentous growth of a population of unicellular organisms in response to starvation; IMP:CGD.
DR GO; GO:0007234; P:osmosensory signaling via phosphorelay pathway; 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:1900436; P:positive regulation of filamentous growth of a population of unicellular organisms in response to starvation; IMP:CGD.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR Pfam; PF00672; HAMP; 2.
DR Pfam; PF18947; HAMP_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 5.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF52172; SSF52172; 2.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS50885; HAMP; 5.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell wall biogenesis/degradation; Cytoplasm; Kinase;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW Transferase; Two-component regulatory system; Virulence.
FT CHAIN 1..1081
FT /note="Histidine protein kinase NIK1"
FT /id="PRO_0000425799"
FT DOMAIN 63..118
FT /note="HAMP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 157..209
FT /note="HAMP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 249..301
FT /note="HAMP 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 341..393
FT /note="HAMP 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 433..485
FT /note="HAMP 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 507..730
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT DOMAIN 875..999
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT REGION 1010..1081
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1018..1036
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1051..1081
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 510
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 924
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT CONFLICT 1051
FT /note="S -> T (in Ref. 1; BAE44787)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1081 AA; 118932 MW; 260EE960E55CACF3 CRC64;
MNPTKKPRLS PMQPSVFEIL NDPELYSQHC HSLRETLLDH FNHQATLIDT YEHELEKSKN
ANKAFQQALS EIGTVVISVA MGDLSKKVEI HTVENDPEIL KVKITINTMM DQLQTFANEV
TKVATEVANG ELGGQAKNDG SVGIWRSLTD NVNIMALNLT NQVREIADVT RAVAKGDLSR
KINVHAQGEI LQLQRTINTM VDQLRTFAFE VSKVARDVGV LGILGGQALI ENVEGIWEEL
TDNVNAMALN LTTQVRNIAN VTTAVAKGDL SKKVTADCKG EILDLKLTIN QMVDRLQNFA
LAVTTLSREV GTLGILGGQA NVQDVEGAWK QVTENVNLMA TNLTNQVRSI ATVTTAVAHG
DLSQKIDVHA QGEILQLKNT INKMVDSLQL FASEVSKVAQ DVGINGKLGI QAQVSDVDGL
WKEITSNVNT MASNLTSQVR AFAQITAAAT DGDFTRFITV EASGEMDALK TKINQMVFNL
RESLQRNTAA REAAELANSA KSEFLANMSH EIRTPLNGII GMTQLSLDTE LTQYQREMLS
IVHNLANSLL TIIDDILDIS KIEANRMTVE QIDFSLRGTV FGALKTLAVK AIEKNLDLTY
QCDSSFPDNL IGDSFRLRQV ILNLAGNAIK FTKEGKVSVS VKKSDKMVLD SKLLLEVCVS
DTGIGIEKDK LGLIFDTFCQ ADGSTTRKFG GTGLGLSISK QLIHLMGGEI WVTSEYGSGS
NFYFTVCVSP SNIRYTRQTE QLLPFSSHYV LFVSTEHTQE ELDVLRDGII ELGLIPIIVR
NIEDATLTEP VKYDIIMIDS IEIAKKLRLL SEVKYIPLVL VHHSIPQLNM RVCIDLGISS
YANTPCSITD LASAIIPALE SRSISQNSDE SVRYKILLAE DNLVNQKLAV RILEKQGHSV
EVVENGLEAY EAIKRNKYDV VLMDVQMPVM GGFEATEKIR QWEKKSNPID SLTFRTPIIA
LTAHAMLGDR EKSLAKGMDD YVSKPLKPKL LMQTINKCIH NINQLKELSR NSRGSDFAKK
MTRNTPGSTT RQGSDEGSVE DMIGDTPRQG SVEGGGTSSR PVQRRSATEG SITTISEQID
R
