ACTC_BPMU
ID ACTC_BPMU Reviewed; 140 AA.
AC P06022;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Late transcription activator C;
DE Short=C;
DE AltName: Full=Gene product 21;
DE Short=gp21;
DE AltName: Full=Protein C;
GN Name=C; OrderedLocusNames=Mup21;
OS Escherichia phage Mu (Bacteriophage Mu).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Myoviridae; Muvirus.
OX NCBI_TaxID=10677;
OH NCBI_TaxID=543; Enterobacteriaceae.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3014438; DOI=10.1093/nar/14.12.4881;
RA Margolin W., Howe M.M.;
RT "Localization and DNA sequence analysis of the C gene of bacteriophage Mu,
RT the positive regulator of Mu late transcription.";
RL Nucleic Acids Res. 14:4881-4897(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Priess H., Brauer B., Schmidt C., Kamp D.;
RT "Sequence of the left end of Mu.";
RL (In) Symonds N., Toussaint A., van de Putte P., Howe M.M. (eds.);
RL Phage Mu, pp.277-296, Cold Spring Harbor Laboratory Press, New York (1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3019838; DOI=10.1016/0378-1119(86)90008-9;
RA Heisig P., Kahmann R.;
RT "The sequence and mom-transactivation function of the C gene of
RT bacteriophage Mu.";
RL Gene 43:59-67(1986).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11922669; DOI=10.1006/jmbi.2002.5437;
RA Morgan G.J., Hatfull G.F., Casjens S., Hendrix R.W.;
RT "Bacteriophage Mu genome sequence: analysis and comparison with Mu-like
RT prophages in Haemophilus, Neisseria and Deinococcus.";
RL J. Mol. Biol. 317:337-359(2002).
RN [5]
RP DNA-BINDING.
RX PubMed=2967705; DOI=10.1016/0006-2952(88)90457-1;
RA Nagaraja V., Hecht G., Hattman S.;
RT "The phage Mu 'late' gene transcription activator, C, is a site-specific
RT DNA binding protein.";
RL Biochem. Pharmacol. 37:1809-1810(1988).
RN [6]
RP INDUCTION.
RX PubMed=2524470; DOI=10.1128/jb.171.6.3440-3448.1989;
RA Stoddard S.F., Howe M.M.;
RT "Localization and regulation of bacteriophage Mu promoters.";
RL J. Bacteriol. 171:3440-3448(1989).
RN [7]
RP FUNCTION.
RX PubMed=9367769; DOI=10.1006/jmbi.1997.1349;
RA Sun W., Hattman S., Kool E.;
RT "Interaction of the bacteriophage Mu transcriptional activator protein, C,
RT with its target site in the mom promoter.";
RL J. Mol. Biol. 273:765-774(1997).
RN [8]
RP DNA-BINDING.
RX PubMed=12833550; DOI=10.1002/prot.10413;
RA Paul B.D., Kanhere A., Chakraborty A., Bansal M., Nagaraja V.;
RT "Identification of the domains for DNA binding and transactivation function
RT of C protein from bacteriophage Mu.";
RL Proteins 52:272-282(2003).
RN [9]
RP DNA-BINDING, AND MUTAGENESIS OF LEU-83 AND LEU-90.
RX PubMed=17218337; DOI=10.1093/protein/gzl047;
RA Chakraborty A., Paul B.D., Nagaraja V.;
RT "Bacteriophage Mu C protein is a new member of unusual leucine zipper-HTH
RT class of proteins.";
RL Protein Eng. Des. Sel. 20:1-5(2007).
RN [10]
RP MUTAGENESIS OF SER-110; GLN-113; ILE-114 AND TYR-115.
RX PubMed=18838393; DOI=10.1093/nar/gkn639;
RA Jiang Y., Howe M.M.;
RT "Regional mutagenesis of the gene encoding the phage Mu late gene activator
RT C identifies two separate regions important for DNA binding.";
RL Nucleic Acids Res. 36:6396-6405(2008).
RN [11]
RP COFACTOR, AND MUTAGENESIS OF GLU-26; ASP-37 AND ASP-40.
RX PubMed=19170593; DOI=10.1021/bi8022448;
RA Swapna G., Saravanan M., Nagaraja V.;
RT "Conformational changes triggered by Mg2+ mediate transactivator
RT function.";
RL Biochemistry 48:2347-2354(2009).
CC -!- FUNCTION: Positive regulator of viral late genes transcription.
CC Responsible for the transition from middle to late gene expression.
CC Activates the Plys, PI, PP and Pmom late promoters thereby allowing the
CC expression of viral endolysin and structural genes. Activates Pmom
CC promoter by unwinding the DNA, thus realigning the promoter elements
CC and recruiting the RNAP. {ECO:0000269|PubMed:9367769}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000305|PubMed:19170593};
CC Note=Binding magnesium induces a conformational change that allows DNA-
CC binding. {ECO:0000305|PubMed:19170593};
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000305}.
CC -!- INDUCTION: Expressed in the intermediate phase of the viral replicative
CC cycle. {ECO:0000269|PubMed:2524470}.
CC -!- DOMAIN: The helix-turn-helix (HTH) motif is involved in DNA-binding.
CC The leucine zipper (bZIP) domain is involved in dimerization.
CC -!- SIMILARITY: Belongs to the c/mor transcriptional regulatory family.
CC {ECO:0000305}.
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DR EMBL; X03992; CAA27628.1; -; Genomic_DNA.
DR EMBL; M64097; AAA32414.1; -; Genomic_DNA.
DR EMBL; M13657; AAA32372.1; -; Genomic_DNA.
DR EMBL; AF083977; AAF01098.1; -; Genomic_DNA.
DR PIR; A91549; ZCBPU2.
DR RefSeq; NP_050625.1; NC_000929.1.
DR SMR; P06022; -.
DR GeneID; 2636301; -.
DR KEGG; vg:2636301; -.
DR Proteomes; UP000002611; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR014875; Mor_transcription_activator.
DR Pfam; PF08765; Mor; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
PE 1: Evidence at protein level;
KW Activator; DNA-binding; Host cytoplasm; Magnesium; Metal-binding;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..140
FT /note="Late transcription activator C"
FT /id="PRO_0000062804"
FT DOMAIN 69..90
FT /note="bZIP"
FT DNA_BIND 99..119
FT /note="H-T-H motif"
FT /evidence="ECO:0000250"
FT BINDING 26
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 37
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 40
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT MUTAGEN 26
FT /note="E->D: Loss of DNA-binding activity and
FT transactivation. No effect on dimerization."
FT /evidence="ECO:0000269|PubMed:19170593"
FT MUTAGEN 26
FT /note="E->Q: Almost no effect on DNA-binding. No effect on
FT transactivation and dimerization."
FT /evidence="ECO:0000269|PubMed:19170593"
FT MUTAGEN 37
FT /note="D->N: Almost no effect on DNA-binding. No effect on
FT transactivation and dimerization."
FT /evidence="ECO:0000269|PubMed:19170593"
FT MUTAGEN 40
FT /note="D->N: Loss of DNA-binding activity and
FT transactivation. No effect on dimerization."
FT /evidence="ECO:0000269|PubMed:19170593"
FT MUTAGEN 83
FT /note="L->R: No effect on dimerization and DNA binding.
FT Complete loss of dimerization and DNA-binding when
FT associated with Ser-90."
FT /evidence="ECO:0000269|PubMed:17218337"
FT MUTAGEN 90
FT /note="L->S: No effect on dimerization and DNA binding.
FT Complete loss of dimerization and DNA-binding when
FT associated with Arg-83."
FT /evidence="ECO:0000269|PubMed:17218337"
FT MUTAGEN 110
FT /note="S->T: Loss of DNA-binding activity."
FT /evidence="ECO:0000269|PubMed:18838393"
FT MUTAGEN 113
FT /note="Q->P: Loss of DNA-binding activity."
FT /evidence="ECO:0000269|PubMed:18838393"
FT MUTAGEN 114
FT /note="I->N: Loss of DNA-binding activity."
FT /evidence="ECO:0000269|PubMed:18838393"
FT MUTAGEN 115
FT /note="Y->D: Loss of DNA-binding activity."
FT /evidence="ECO:0000269|PubMed:18838393"
SQ SEQUENCE 140 AA; 16514 MW; 18771FB38C606917 CRC64;
MQHDLFEHDP AIRQLIGHID NIPAPELESR WPRSVVDLID VLENELKRQN VSNPRELARK
QAVALSCFLG GRQFYIPCGD TILTALRDDL LYCQFNGRNM EELRRQYRLS QPQIYQIIAR
QRKLHTRRHQ PDLFSPETPK
