STUA_ACRC1
ID STUA_ACRC1 Reviewed; 623 AA.
AC A0A0K0QSV4; A0A086T8Z7;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 11-NOV-2015, sequence version 1.
DT 25-MAY-2022, entry version 19.
DE RecName: Full=Cell pattern formation-associated protein stuA {ECO:0000305};
DE AltName: Full=Stunted protein A {ECO:0000250|UniProtKB:P36011};
GN Name=stuA {ECO:0000303|PubMed:26283234}; ORFNames=ACRE_033420;
OS Acremonium chrysogenum (strain ATCC 11550 / CBS 779.69 / DSM 880 / IAM
OS 14645 / JCM 23072 / IMI 49137).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreales incertae sedis; Acremonium.
OX NCBI_TaxID=857340;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Sabtcheva S.D., Ivanov I.N.;
RT "Emergence of plasmid-mediated VIM-4 carbapenemase in Citrobacter freundii,
RT co-harbouring armA, CTX-M-3, TEM-1 and QnrB at a cancer centre in
RT Bulgaria.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11550 / CBS 779.69 / DSM 880 / IAM 14645 / JCM 23072 / IMI
RC 49137;
RX PubMed=25291769; DOI=10.1128/genomea.00948-14;
RA Terfehr D., Dahlmann T.A., Specht T., Zadra I., Kuernsteiner H., Kueck U.;
RT "Genome sequence and annotation of Acremonium chrysogenum, producer of the
RT beta-lactam antibiotic cephalosporin C.";
RL Genome Announc. 2:E0094814-E0094814(2014).
RN [3]
RP DISRUPTION PHENOTYPE, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=26283234; DOI=10.1016/j.fgb.2015.08.003;
RA Hu P., Wang Y., Zhou J., Pan Y., Liu G.;
RT "AcstuA, which encodes an APSES transcription regulator, is involved in
RT conidiation, cephalosporin biosynthesis and cell wall integrity of
RT Acremonium chrysogenum.";
RL Fungal Genet. Biol. 83:26-40(2015).
CC -!- FUNCTION: Transcription factor that regulates asexual reproduction
CC (PubMed:26283234). Binds the StuA-response elements (StRE) with the
CC consensus sequence 5'-(A/T)CGCG(T/A)N(A/C)-3' at the promoters of
CC target genes (By similarity). Controls conidiation by positively
CC regulating the expression of brlA and abaA (PubMed:26283234).
CC Positively regulates the cephalosporin biosynthesis gene cluster
CC (PubMed:26283234). Also involved hyphal fragmentation and cell wall
CC integrity (PubMed:26283234). {ECO:0000250|UniProtKB:P36011,
CC ECO:0000269|PubMed:26283234}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26283234}.
CC -!- DISRUPTION PHENOTYPE: Blocks the conidiation through severely down-
CC regulating the expression of brlA and abaA (PubMed:26283234).
CC Drastically reduces cephalosporin production by decreasing expression
CC of pcbAB, pbcC, cefD1, cefD2, cefEF and cefG (PubMed:26283234). Reduces
CC also the expression of the mannoprotein encoding genes Acmp2 and Acmp3
CC and impairs cell wall integrity (PubMed:26283234).
CC {ECO:0000269|PubMed:26283234}.
CC -!- SIMILARITY: Belongs to the EFG1/PHD1/stuA family. {ECO:0000305}.
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; KP881734; AKR16194.1; -; mRNA.
DR EMBL; JPKY01000026; KFH45829.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K0QSV4; -.
DR SMR; A0A0K0QSV4; -.
DR STRING; 857340.A0A0K0QSV4; -.
DR EnsemblFungi; KFH45829; KFH45829; ACRE_033420.
DR OrthoDB; 311987at2759; -.
DR Proteomes; UP000029964; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0048315; P:conidium formation; IEA:UniProtKB-KW.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR Gene3D; 3.10.260.10; -; 1.
DR InterPro; IPR029790; EFG1/Phd1/StuA.
DR InterPro; IPR036887; HTH_APSES_sf.
DR InterPro; IPR018004; KilA_N/APSES_HTH.
DR InterPro; IPR003163; Tscrpt_reg_HTH_APSES-type.
DR PANTHER; PTHR47792; PTHR47792; 1.
DR SMART; SM01252; KilA-N; 1.
DR SUPFAM; SSF54616; SSF54616; 1.
DR PROSITE; PS51299; HTH_APSES; 1.
PE 2: Evidence at transcript level;
KW Conidiation; DNA-binding; Nucleus; Reference proteome; Sporulation;
KW Transcription; Transcription regulation.
FT CHAIN 1..623
FT /note="Cell pattern formation-associated protein stuA"
FT /id="PRO_0000435969"
FT DOMAIN 115..221
FT /note="HTH APSES-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00630"
FT DNA_BIND 149..170
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00630"
FT REGION 13..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 232..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 332..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 569..594
FT /note="Nuclear localization domain"
FT /evidence="ECO:0000250|UniProtKB:P36011"
FT COMPBIAS 13..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..376
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..406
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..448
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..513
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 569..596
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 623 AA; 66223 MW; D097C626134C3B68 CRC64;
MNNGGPTEMY YQQHMQSAGQ PQQPQTVTSG PMSHYPPAQP PLLQPGQPYS HGAPSPYQYG
YANGMASPSG GPVPSNLPSN QPVLPLPGVG GQGAMPAHYS FDTTGQHPPP GMKPRVTATL
WEDEGSLCFQ VEARGICVAR REDNHMINGT KLLNVAGMTR GRRDGILKSE KVRHVVKIGP
MHLKGVWIPY ERALDFANKE KITELLYPLF VHNIGALLYH PTNQTRTSQV MAAAERRKQD
QGQMRTPPAG LPSIQHQPHN SMALPGPQSS LPSNNMARPP LDRAATFPTP PTTASSVMPN
MGSTDNFNWQ GQSMNGNQGT NAIAIDANLG HARSMPTTPA TTPPGSMQPY GSAQSFDGSR
QQMYNAPSQQ SPYPASNGAH DRMYGQGNSY AKNDMGPPSS RPSGSAPSGE HEHKGSNGIL
PSEHGHQSHA GEEDGEHEQH DAEYTHDSGA YDSNRPSYNY TAPGVGSLAG DANNVDPSMT
GSPNHPPASG RATPRTAAQP QPYYHNSGYG ASPRVQQAPG FYNGVGGDRP AVNGGSGSDV
YAPPADMANP MPNGYAPAPQ VPNGVSGVKR GREGDDDLSR PVGDVPGMDM KRRKTLESSM
PAPPFDSMSG RTAPTIGGDP RQR
