MOR_BPMU
ID MOR_BPMU Reviewed; 129 AA.
AC P23848;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 02-JUN-2021, entry version 99.
DE RecName: Full=Middle operon regulator;
DE Short=Mor;
DE AltName: Full=GemB;
DE AltName: Full=Gene product 17;
DE Short=gp17;
GN Name=mor; OrderedLocusNames=Mup17;
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=2147678; DOI=10.1128/jb.172.12.6641-6650.1990;
RA Mathee K., Howe M.M.;
RT "Identification of a positive regulator of the Mu middle operon.";
RL J. Bacteriol. 172:6641-6650(1990).
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 [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 [4]
RP FUNCTION.
RX PubMed=2173258; DOI=10.1016/0042-6822(90)90136-f;
RA Giusti M., Di Lallo G., Ghelardini P., Paolozzi L.;
RT "The bacteriophage Mu gem gene: a positive regulator of the C operon
RT required for normal levels of late transcription.";
RL Virology 179:694-700(1990).
RN [5]
RP REVIEW.
RX PubMed=7896136; DOI=10.1007/bf01443429;
RA Ghelardini P., La Valle R., Paolozzi L.;
RT "The Mu gem operon: its role in gene expression, recombination and cell
RT cycle.";
RL Genetica 94:151-156(1994).
RN [6]
RP FUNCTION.
RX PubMed=8790343; DOI=10.1073/pnas.93.18.9408;
RA Artsimovitch I., Kahmeyer-Gabbe M., Howe M.M.;
RT "Distortion in the spacer region of Pm during activation of middle
RT transcription of phage Mu.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:9408-9413(1996).
RN [7]
RP INDUCTION.
RX PubMed=9454718; DOI=10.1006/viro.1997.8948;
RA Fabozzi G., Paolozzi L., Ghelardini P.;
RT "Regulation of the bacteriophage Mu gem operon.";
RL Virology 241:73-79(1998).
RN [8]
RP DNA-BINDING, SUBUNIT, DIMERIZATION DOMAIN, AND MUTAGENESIS OF GLY-65;
RP GLY-66; GLN-68; TYR-70 AND GLY-74.
RX PubMed=21859715; DOI=10.1074/jbc.m111.269860;
RA Kumaraswami M., Avanigadda L., Rai R., Park H.W., Howe M.M.;
RT "Genetic analysis of phage Mu Mor protein amino acids involved in DNA minor
RT groove binding and conformational changes.";
RL J. Biol. Chem. 286:35852-35862(2011).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), DNA-BINDING, AND SUBUNIT.
RX PubMed=14729670; DOI=10.1074/jbc.m313555200;
RA Kumaraswami M., Howe M.M., Park H.W.;
RT "Crystal structure of the Mor protein of bacteriophage Mu, a member of the
RT Mor/C family of transcription activators.";
RL J. Biol. Chem. 279:16581-16590(2004).
CC -!- FUNCTION: Activator of the Pm promoter, which controls middle genes
CC expression. Activation of Pm allows expression of protein C necessary
CC for late gene expression. In addition to Mor binding, activation of Pm
CC might require the interaction of Mor with the C-terminus of host RNAP
CC subunits RpoA and RpoH. {ECO:0000269|PubMed:2173258,
CC ECO:0000269|PubMed:8790343}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:14729670,
CC ECO:0000269|PubMed:21859715}.
CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000305}.
CC -!- INDUCTION: This protein is constitively expressed from the Pgem
CC promoter unlike most other early proteins which are expressed under the
CC control of the Pe promoter. Its expression seems to escape repression
CC by repressor protein c and thus could occur throughout latency
CC (Probable). {ECO:0000305|PubMed:9454718}.
CC -!- DOMAIN: The dimerization domain in the N-terminus and the DNA-binding
CC domain in the C-terminus are connected by a linker containing a beta-
CC strand.
CC -!- SIMILARITY: Belongs to the c/mor transcriptional regulatory family.
CC {ECO:0000305}.
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DR EMBL; M64097; AAA32408.1; -; Genomic_DNA.
DR EMBL; AF083977; AAF01094.1; -; Genomic_DNA.
DR RefSeq; NP_050621.1; NC_000929.1.
DR PDB; 1RR7; X-ray; 2.20 A; A=1-129.
DR PDBsum; 1RR7; -.
DR SMR; P23848; -.
DR GeneID; 2636272; -.
DR KEGG; vg:2636272; -.
DR EvolutionaryTrace; P23848; -.
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 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 3D-structure; Activator; DNA-binding; Early protein; Host cytoplasm;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..129
FT /note="Middle operon regulator"
FT /id="PRO_0000062803"
FT DNA_BIND 94..114
FT /note="H-T-H motif"
FT /evidence="ECO:0000255"
FT REGION 28..64
FT /note="Dimerization"
FT REGION 77..129
FT /note="DNA-binding"
FT MUTAGEN 65
FT /note="G->M,N,R,T,V: Complete loss of DNA-binding and
FT transcription activation ability."
FT /evidence="ECO:0000269|PubMed:21859715"
FT MUTAGEN 66
FT /note="G->A,H,L,P,R: Complete loss of DNA-binding and
FT transcription activation ability."
FT /evidence="ECO:0000269|PubMed:21859715"
FT MUTAGEN 68
FT /note="Q->G,F,I,L,K,P,R: Complete loss of DNA-binding and
FT transcription activation ability."
FT /evidence="ECO:0000269|PubMed:21859715"
FT MUTAGEN 70
FT /note="Y->G,I,R,S,V: Complete loss of DNA-binding and
FT transcription activation ability."
FT /evidence="ECO:0000269|PubMed:21859715"
FT MUTAGEN 74
FT /note="G->F,W: Partial loss of DNA-binding and
FT transcription activation ability."
FT /evidence="ECO:0000269|PubMed:21859715"
FT MUTAGEN 74
FT /note="G->I,S,T,Y: Partial loss of DNA-binding and
FT transcription activation ability."
FT /evidence="ECO:0000269|PubMed:21859715"
FT MUTAGEN 74
FT /note="G->R: Complete loss of DNA-binding and transcription
FT activation ability."
FT /evidence="ECO:0000269|PubMed:21859715"
FT HELIX 28..45
FT /evidence="ECO:0007829|PDB:1RR7"
FT HELIX 53..64
FT /evidence="ECO:0007829|PDB:1RR7"
FT HELIX 75..89
FT /evidence="ECO:0007829|PDB:1RR7"
FT HELIX 95..102
FT /evidence="ECO:0007829|PDB:1RR7"
FT HELIX 106..118
FT /evidence="ECO:0007829|PDB:1RR7"
SQ SEQUENCE 129 AA; 14714 MW; C796C950F1686FBA CRC64;
MTEDLFGDLQ DDTILAHLDN PAEDTSRFPA LLAELNDLLR GELSRLGVDP AHSLEIVVAI
CKHLGGGQVY IPRGQALDSL IRDLRIWNDF NGRNVSELTT RYGVTFNTVY KAIRRMRRLK
YRQYQPSLL
