LAEA_PENRW
ID LAEA_PENRW Reviewed; 427 AA.
AC B6H9U8; B2ZSZ4;
DT 16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Secondary metabolism regulator laeA {ECO:0000305};
DE AltName: Full=Methyltransferase laeA {ECO:0000305};
DE EC=2.1.1.- {ECO:0000250|UniProtKB:C8VQG9};
DE AltName: Full=Velvet complex subunit laeA {ECO:0000305};
GN Name=laeA {ECO:0000303|PubMed:18952140};
GN ORFNames=Pc16g14010, PCH_Pc16g14010;
OS Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS 54-1255) (Penicillium chrysogenum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC Penicillium chrysogenum species complex.
OX NCBI_TaxID=500485;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255;
RX PubMed=18952140; DOI=10.1016/j.biochi.2008.09.004;
RA Kosalkova K., Garcia-Estrada C., Ullan R.V., Godio R.P., Feltrer R.,
RA Teijeira F., Mauriz E., Martin J.F.;
RT "The global regulator LaeA controls penicillin biosynthesis, pigmentation
RT and sporulation, but not roquefortine C synthesis in Penicillium
RT chrysogenum.";
RL Biochimie 91:214-225(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255;
RX PubMed=18820685; DOI=10.1038/nbt.1498;
RA van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA Bovenberg R.A.L.;
RT "Genome sequencing and analysis of the filamentous fungus Penicillium
RT chrysogenum.";
RL Nat. Biotechnol. 26:1161-1168(2008).
RN [3]
RP FUNCTION, DISRUPTION PHENOTYPE, INDUCTION, INTERACTION WITH VELA, AND
RP SUBCELLULAR LOCATION.
RX PubMed=20543063; DOI=10.1128/ec.00077-10;
RA Hoff B., Kamerewerd J., Sigl C., Mitterbauer R., Zadra I., Kuernsteiner H.,
RA Kueck U.;
RT "Two components of a velvet-like complex control hyphal morphogenesis,
RT conidiophore development, and penicillin biosynthesis in Penicillium
RT chrysogenum.";
RL Eukaryot. Cell 9:1236-1250(2010).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21816879; DOI=10.1099/mic.0.051896-0;
RA Kamerewerd J., Zadra I., Kuernsteiner H., Kueck U.;
RT "PcchiB1, encoding a class V chitinase, is affected by PcVelA and PcLaeA,
RT and is responsible for cell wall integrity in Penicillium chrysogenum.";
RL Microbiology 157:3036-3048(2011).
RN [5]
RP FUNCTION.
RX PubMed=22439693; DOI=10.1089/omi.2011.0153;
RA Veiga T., Nijland J.G., Driessen A.J., Bovenberg R.A., Touw H.,
RA van den Berg M.A., Pronk J.T., Daran J.M.;
RT "Impact of velvet complex on transcriptome and penicillin G production in
RT glucose-limited chemostat cultures of a beta-lactam high-producing
RT Penicillium chrysogenum strain.";
RL OMICS 16:320-333(2012).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION.
RX PubMed=23089625; DOI=10.1016/j.fgb.2012.10.001;
RA Martin J., Garcia-Estrada C., Kosalkova K., Ullan R.V., Albillos S.M.,
RA Martin J.F.;
RT "The inducers 1,3-diaminopropane and spermidine produce a drastic increase
RT in the expression of the penicillin biosynthetic genes for prolonged time,
RT mediated by the laeA regulator.";
RL Fungal Genet. Biol. 49:1004-1013(2012).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23264641; DOI=10.1128/ec.00272-12;
RA Kopke K., Hoff B., Bloemendal S., Katschorowski A., Kamerewerd J.,
RA Kueck U.;
RT "Members of the Penicillium chrysogenum velvet complex play functionally
RT opposing roles in the regulation of penicillin biosynthesis and
RT conidiation.";
RL Eukaryot. Cell 12:299-310(2013).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25557366; DOI=10.1002/jobm.201400588;
RA Wolfers S., Kamerewerd J., Nowrousian M., Sigl C., Zadra I.,
RA Kuernsteiner H., Kueck U., Bloemendal S.;
RT "Microarray hybridization analysis of light-dependent gene expression in
RT Penicillium chrysogenum identifies bZIP transcription factor PcAtfA.";
RL J. Basic Microbiol. 55:480-489(2015).
CC -!- FUNCTION: Methyltransferase that performs automethylation (By
CC similarity). No other methyl-accepting substrate has been identified
CC yet (By similarity). Component of the velvet transcription factor
CC complex that acts as a global regulator for secondary metabolite gene
CC expression (PubMed:18952140, PubMed:22439693). Controls the expression
CC of the penicillin gene cluster (PubMed:18952140, PubMed:20543063,
CC PubMed:22439693, PubMed:23089625, PubMed:23264641). Controls
CC benzylpenicillin production, but is not involved in the biosynthesis of
CC the alkaloid roquefortine C (PubMed:18952140). Positively controls the
CC expression of the class V chitinase chiB1 (PubMed:21816879). Positively
CC controls the expression of the transcription factor atfA
CC (PubMed:25557366). Regulates also asexual differentiation
CC (PubMed:18952140, PubMed:23264641). {ECO:0000250|UniProtKB:C8VQG9,
CC ECO:0000269|PubMed:18952140, ECO:0000269|PubMed:20543063,
CC ECO:0000269|PubMed:21816879, ECO:0000269|PubMed:22439693,
CC ECO:0000269|PubMed:23089625, ECO:0000269|PubMed:23264641,
CC ECO:0000269|PubMed:25557366}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-methionyl-[protein] + S-adenosyl-L-methionine = S-adenosyl-
CC L-homocysteine + S-methyl-L-methionyl-[protein];
CC Xref=Rhea:RHEA:60560, Rhea:RHEA-COMP:12313, Rhea:RHEA-COMP:15592,
CC ChEBI:CHEBI:16044, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:142742; Evidence={ECO:0000250|UniProtKB:C8VQG9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60561;
CC Evidence={ECO:0000250|UniProtKB:C8VQG9};
CC -!- SUBUNIT: Component of the heterotrimeric velvet complex composed of
CC laeA, veA and velB; VeA acting as a bridging protein between laeA and
CC velB (By similarity). Interacts with velA (PubMed:20543063).
CC {ECO:0000250|UniProtKB:C8VQG9, ECO:0000269|PubMed:20543063}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20543063}.
CC -!- INDUCTION: Expression is negatively regulated by velA
CC (PubMed:20543063). Expression is stimulated by the polyamines 1,3-
CC diaminopropane (1,3-DAP) and spermidine (PubMed:23089625).
CC {ECO:0000269|PubMed:20543063, ECO:0000269|PubMed:23089625}.
CC -!- DISRUPTION PHENOTYPE: Leads to pigmentation and sporulation defects
CC (PubMed:18952140). Drastically reduces expression of the penicillin
CC biosynthetic genes pcbAB, pcbC and penDE (PubMed:20543063,
CC PubMed:23089625, PubMed:23264641). Leads to a severe impairment in
CC conidiophore formation under both light and dark conditions
CC (PubMed:20543063, PubMed:23264641). Decreases the expression of the
CC class V chitinase chiB1 (PubMed:21816879). Decreases the expression of
CC the transcription factor atfA (PubMed:25557366).
CC {ECO:0000269|PubMed:18952140, ECO:0000269|PubMed:20543063,
CC ECO:0000269|PubMed:21816879, ECO:0000269|PubMed:23089625,
CC ECO:0000269|PubMed:23264641, ECO:0000269|PubMed:25557366}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. LaeA
CC methyltransferase family. {ECO:0000305}.
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DR EMBL; EU685842; ACD50375.1; -; Genomic_DNA.
DR EMBL; AM920431; CAP94071.1; -; Genomic_DNA.
DR RefSeq; XP_002561699.1; XM_002561653.1.
DR AlphaFoldDB; B6H9U8; -.
DR STRING; 1108849.XP_002561699.1; -.
DR EnsemblFungi; CAP94071; CAP94071; PCH_Pc16g14010.
DR GeneID; 8311477; -.
DR KEGG; pcs:Pc16g14010; -.
DR VEuPathDB; FungiDB:PCH_Pc16g14010; -.
DR eggNOG; ENOG502QQMC; Eukaryota.
DR HOGENOM; CLU_010595_2_0_1; -.
DR OMA; KNCDFYA; -.
DR OrthoDB; 1047281at2759; -.
DR BioCyc; PCHR:PC16G14010-MON; -.
DR Proteomes; UP000000724; Contig Pc00c16.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW Methyltransferase; Nucleus; Reference proteome; S-adenosyl-L-methionine;
KW Sporulation; Transcription; Transcription regulation; Transferase.
FT CHAIN 1..427
FT /note="Secondary metabolism regulator laeA"
FT /id="PRO_0000435747"
FT REGION 1..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 427 AA; 48548 MW; 304C982E7AC5E356 CRC64;
MSYRESSGSF PAPDRTSLPK MFTNGDSRLR HLPPISSPPP PKRYKSESTP GSDAGHSRYY
SHSVASDRTR SRQPSSAMDL YTLIDRDPVD KDPRRNARFT SNGSVATQAS HASNASQISR
SSPIIISDRK IPEKYPNHKE NGRMYHGYRK GIYPLPCDEE EQDRLDIFHK LFTVARAEDG
LIYAPHPPGS RILDLGCGTG IWSIEVANKF PGSFVVGVDL APIQPTNTPK NCDFYAPFDF
EAPWTMGEDS WDIIHMQMGC GSVASWPSLY RRVFQHLKPG GWFEQVEIDF RPRVEDKDGE
PGRAMANWYS TLKHATEATM RPLAHSSNET IRNLQEAGFT EIDHQIVGLP MNPWHPDSHE
QKVARWYNLA ISESVQPMCL APFSRVLSWT REQIDRIAFD VKQEAFDKRI KTYNLLHIYQ
ARKPVEE
