BCK1_ASPFU
ID BCK1_ASPFU Reviewed; 1617 AA.
AC Q4WXY0;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Mitogen-activated protein kinase kinae kinase bck1 {ECO:0000303|PubMed:19715768};
DE Short=MAPKKK bck1 {ECO:0000303|PubMed:19715768};
DE EC=2.7.11.24 {ECO:0000269|PubMed:19715768};
DE AltName: Full=MEKK bck1 {ECO:0000305};
GN Name=bck1 {ECO:0000303|PubMed:19715768}; ORFNames=AFUA_3G11080;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19715768; DOI=10.1016/j.fgb.2009.08.005;
RA Valiante V., Jain R., Heinekamp T., Brakhage A.A.;
RT "The MpkA MAP kinase module regulates cell wall integrity signaling and
RT pyomelanin formation in Aspergillus fumigatus.";
RL Fungal Genet. Biol. 46:909-918(2009).
RN [3]
RP FUNCTION.
RX PubMed=21883519; DOI=10.1111/j.1365-2958.2011.07778.x;
RA Jain R., Valiante V., Remme N., Docimo T., Heinekamp T., Hertweck C.,
RA Gershenzon J., Haas H., Brakhage A.A.;
RT "The MAP kinase MpkA controls cell wall integrity, oxidative stress
RT response, gliotoxin production and iron adaptation in Aspergillus
RT fumigatus.";
RL Mol. Microbiol. 82:39-53(2011).
RN [4]
RP FUNCTION.
RX PubMed=32005734; DOI=10.1128/aem.02347-19;
RA Rocha M.C., Fabri J.H.T.M., Simoes I.T., Silva-Rocha R., Hagiwara D.,
RA da Cunha A.F., Goldman G.H., Canovas D., Malavazi I.;
RT "The cell wall integrity pathway contributes to the early stages of
RT Aspergillus fumigatus asexual development.";
RL Appl. Environ. Microbiol. 86:0-0(2020).
RN [5]
RP FUNCTION.
RX PubMed=33010083; DOI=10.1111/cmi.13273;
RA Rocha M.C., Minari K., Fabri J.H.T.M., Kerkaert J.D., Gava L.M.,
RA da Cunha A.F., Cramer R.A., Borges J.C., Malavazi I.;
RT "Aspergillus fumigatus Hsp90 interacts with the main components of the cell
RT wall integrity pathway and cooperates in heat shock and cell wall stress
RT adaptation.";
RL Cell. Microbiol. 23:e13273-e13273(2021).
CC -!- FUNCTION: Mitogen-activated protein kinase kinase kinase; part of cell
CC wall integrity (CWI) signaling pathway composed of pkcA, the bck1-mkk2-
CC mpka MAPK cascade and the downstream rlmA transcription regulator
CC (PubMed:19715768). The CWI signaling pathway regulates cell wall
CC integrity and pyomelanin formation (PubMed:19715768). CWI controls also
CC oxidative stress response, gliotoxin production, iron adaptation and
CC asexual development (PubMed:21883519, PubMed:32005734). Finally, CWI is
CC constitutively required for A.fumigatus to cope with the temperature
CC increase found in the mammalian lung environment, during infection
CC (PubMed:33010083). {ECO:0000269|PubMed:19715768,
CC ECO:0000269|PubMed:21883519, ECO:0000269|PubMed:32005734,
CC ECO:0000269|PubMed:33010083}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.24;
CC Evidence={ECO:0000269|PubMed:19715768};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990;
CC Evidence={ECO:0000269|PubMed:19715768};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.24; Evidence={ECO:0000269|PubMed:19715768};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609;
CC Evidence={ECO:0000269|PubMed:19715768};
CC -!- DISRUPTION PHENOTYPE: Results in severe sensitivity against cell wall-
CC disturbing compounds congo red or calcofluor white, and drastic
CC alterations of the fungal morphology (PubMed:19715768). Impairs
CC phosphorylation of mpkA (PubMed:19715768).
CC {ECO:0000269|PubMed:19715768}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. MAP kinase kinase kinase subfamily.
CC {ECO:0000305}.
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DR EMBL; AAHF01000002; EAL92473.1; -; Genomic_DNA.
DR RefSeq; XP_754511.1; XM_749418.1.
DR SMR; Q4WXY0; -.
DR STRING; 746128.CADAFUBP00003728; -.
DR EnsemblFungi; EAL92473; EAL92473; AFUA_3G11080.
DR GeneID; 3512087; -.
DR KEGG; afm:AFUA_3G11080; -.
DR eggNOG; KOG0198; Eukaryota.
DR HOGENOM; CLU_000961_3_0_1; -.
DR InParanoid; Q4WXY0; -.
DR OMA; GNLGKMH; -.
DR OrthoDB; 55144at2759; -.
DR Proteomes; UP000002530; Chromosome 3.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004709; F:MAP kinase kinase kinase activity; IBA:GO_Central.
DR GO; GO:0000165; P:MAPK cascade; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Transferase;
KW Virulence.
FT CHAIN 1..1617
FT /note="Mitogen-activated protein kinase kinae kinase bck1"
FT /id="PRO_0000453184"
FT DOMAIN 1323..1596
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 167..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 211..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 345..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 455..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 568..633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 739..820
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 832..1144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1165..1277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..61
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..399
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 533..555
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..621
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 749..763
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 866..888
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 944..986
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 988..1002
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1017..1038
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1052..1107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1198..1222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1255..1271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1329..1337
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 1352
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 1617 AA; 175896 MW; 6D64EC12351F52B4 CRC64;
MDGQRQQTYI PAPPPPSATQ PSQSHMLSLP PPPPRHLPTQ PQGVMPPPPP GPPPGPPPGP
GYGASKLANS QLQQQNNLGW QHNWARQALS QGFLPPPPPP PMVPTNQAYG RQTSFSVPNA
DGPITSATYV PGSNTFGAGV GIPGFDAHTR PSYEAYGTMS GSDRIRGPVH HLYESSGGDG
SAYKRDGTVP PTPSARTMPS SLALHDNAQE SVASSLPGAT AQNHQSQTGQ TNEPTKSPSH
RQNNSNTLLG GMSPSEAAVQ WPLDRVLLWL AKNGFSRDWQ ETFKTLQIEG ADFLDIGHGA
NGRGNFNKMH NEVFPQLAKE CEASGTGWDK ERELGEGKRM RRLIRQIHDD DSFDVGIPAQ
KRRESQAPSE GAPDTSPKLS HEPQSAGPHS GTIENSPNLR APQLAQPHRH SVQMRSVTLP
IPTTHDIASS DFSQTDGISS RSDFSRSVLV GLGVDHRRQS PSMSSDNGNL VAPFRSYEDS
PKSGSPATQH ATLNQGLSSS STGDLSVKYE HSRGNSSDST MGRRYYESRK GQETIRPSPQ
EMCSRQWTGE TSSSYPKEHK GIFNFLKKRS KGGDSTHPSP EEPNLESPTS PVNLRQNGPH
LPYTKPSFNA SDMSLGERPS SASMSDHERL RGKPAQKGKK WSFVTLDGWN YRLVDITDMD
SVETLRAAIC HNLGIADWAS AQIFLTEPGQ SDHEEPLNDT MLALCRRTKS DSIGSLKLFV
RGTHLQPVPN HVPNFAGLGV PLPDKHTASP THHLPRKPLD DEALSRIPPQ PQTGPASPQL
GIRPQQPKTP AAKFPARDAP QHTEGMSPVE GDQQVGISPE PDKADLLARH EEHKREVERK
QKAYLSSKGP PQPRNDSYGE TGYRRAGVID FDERRVSPYE DKKADTLVPL RKPPSAPQES
YTLTRINSLR KKDGDRPRAQ PAVQTHGLGA VLASMGRMTS AIGTPAPSVP TPTSAGGKQT
NFGSFGSPTQ GNTKSAPQSS PEKESLDNPG NPAEHRHTKS TAPEIPKPTL QSRKSYGPEF
DFEETEVSFQ RSPRPQDDSD EDSDDGLFAI PLSNNKASTK ENDSGSGTSE AQKRTEKPAL
TVNTESRLRK GLSVSFRSPS ATRESFADAN GDSGGREGAS FLMAASPEDE RPTPRRDSFA
RGDIWASRPP VEGVIDNLDD FFPDIDLDAP YLDGQGVSPP SSPANRAPPE NDLHKKENQP
SSSYTGEMNA NAGDTLGSNE PTLKPQGGDV VARRNINRSG GGLTRGKSIR EVAKGANQAS
RSRSIHTGNQ KSGEILRRKS TKMFGAKIMQ IKPKPGSRLS QLDPIPQNNT PSGVPQRQPT
FRIIRGQLIG KGTYGRVYLG INADNGEVLA VKQVEINPRL AGQDTDRVKE MVAAMDQEID
TMQHLEHPNI VQYLGCERGE FSISIYLEYI SGGSIGSCLR KHGKFEESVV KSLTRQTLSG
LAYLHDQGIL HRDLKADNIL LDLDGTCKIS DFGISKKTDD IYGNDSSNSM QGSVFWMAPE
VIQSQGQGYS AKVDIWSLGC VVLEMFAGRR PWSKEEAIGA IFKLGSLSQA PPIPDDVSMT
ISPAALAFMY DCFTVPYRDS SERPTAQTLL TRHPFCEEDP NYNFLDTELY AKIRHVL
