SIGML_BPT4
ID SIGML_BPT4 Reviewed; 185 AA.
AC P04524;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=RNA polymerase sigma-like factor {ECO:0000255|HAMAP-Rule:MF_04164, ECO:0000305};
DE AltName: Full=Gene product 55;
DE Short=gp55;
DE AltName: Full=Promoter specificity factor {ECO:0000255|HAMAP-Rule:MF_04164};
GN Name=55;
OS Enterobacteria phage T4 (Bacteriophage T4).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Myoviridae; Tevenvirinae; Tequatrovirus.
OX NCBI_TaxID=10665;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=4018026; DOI=10.1002/j.1460-2075.1985.tb02344.x;
RA Gram H., Rueger W.;
RT "Genes 55, alpha gt, 47 and 46 of bacteriophage T4: the genomic
RT organization as deduced by sequence analysis.";
RL EMBO J. 4:257-264(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=C;
RX PubMed=3575111; DOI=10.1093/nar/15.8.3632;
RA Tomaschewski J., Rueger W.;
RT "Nucleotide sequence and primary structures of gene products coded for by
RT the T4 genome between map positions 48.266 kb and 39.166 kb.";
RL Nucleic Acids Res. 15:3632-3633(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12626685; DOI=10.1128/mmbr.67.1.86-156.2003;
RA Miller E.S., Kutter E., Mosig G., Arisaka F., Kunisawa T., Ruger W.;
RT "Bacteriophage T4 genome.";
RL Microbiol. Mol. Biol. Rev. 67:86-156(2003).
RN [4]
RP INTERACTION WITH HOST RNA POLYMERASE.
RX PubMed=3305506; DOI=10.1016/s0021-9258(18)45362-8;
RA Williams K.P., Kassavetis G.A., Geiduschek E.P.;
RT "Interactions of the bacteriophage T4 gene 55 product with Escherichia coli
RT RNA polymerase. Competition with Escherichia coli sigma 70 and release from
RT late T4 transcription complexes following initiation.";
RL J. Biol. Chem. 262:12365-12371(1987).
RN [5]
RP FUNCTION, AND INTERACTION WITH THE TERMINASE LARGE SUBUNIT.
RX PubMed=12051907; DOI=10.1016/s0022-2836(02)00298-x;
RA Malys N., Chang D.Y., Baumann R.G., Xie D., Black L.W.;
RT "A bipartite bacteriophage T4 SOC and HOC randomized peptide display
RT library: detection and analysis of phage T4 terminase (gp17) and late sigma
RT factor (gp55) interaction.";
RL J. Mol. Biol. 319:289-304(2002).
RN [6]
RP MUTAGENESIS OF GLU-70; ASP-74; GLU-77; ALA-78; GLY-82 AND LEU-83, AND
RP INTERACTION WITH HOST RNAP.
RX PubMed=12496274; DOI=10.1074/jbc.m211447200;
RA Wong K., Kassavetis G.A., Leonetti J.P., Geiduschek E.P.;
RT "Mutational and functional analysis of a segment of the sigma family
RT bacteriophage T4 late promoter recognition protein gp55.";
RL J. Biol. Chem. 278:7073-7080(2003).
RN [7]
RP REVIEW ON FUNCTION.
RX PubMed=21029432; DOI=10.1186/1743-422x-7-288;
RA Geiduschek E.P., Kassavetis G.A.;
RT "Transcription of the T4 late genes.";
RL Virol. J. 7:288-288(2010).
RN [8]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS) IN COMPLEX WITH DNA AND
RP HOST RNAP, IDENTIFICATION IN THE TRANSCRIPTION ACTIVATION COMPLEX,
RP INTERACTION WITH HOST RNAP, FUNCTION, DNA-BINDING, AND MUTAGENESIS OF
RP ASN-13; LEU-54; ARG-57; PHE-86; HIS-95; TYR-97 AND THR-99.
RX PubMed=33602900; DOI=10.1038/s41467-021-21392-0;
RA Shi J., Wen A., Jin S., Gao B., Huang Y., Feng Y.;
RT "Transcription activation by a sliding clamp.";
RL Nat. Commun. 12:1131-1131(2021).
CC -!- FUNCTION: Plays a role in the transcription of the viral late genes by
CC acting as a late promoter recognition subunit (PubMed:33602900).
CC Associates with host RNA polymerase (RNAP) core and thus replaces the
CC host sigma-70/rpoD subunit in the complex (PubMed:33602900). May also
CC play a role in DNA packaging by interacting with the terminase subunit
CC gp17 (PubMed:12051907). {ECO:0000255|HAMAP-Rule:MF_04164,
CC ECO:0000269|PubMed:12051907, ECO:0000269|PubMed:33602900}.
CC -!- SUBUNIT: Interacts with the host RNA polymerase catalytic core formed
CC by RpoA, RpoB, RpoC and RpoZ to form the RNAP-gp55 holoenzyme
CC (PubMed:3305506, PubMed:12496274, PubMed:33602900). Part of the
CC transcription activation complex containing host RNAP, the viral RNA
CC polymerase sigma-like factor, the late transcription coactivator, and
CC the sliding clamp (PubMed:33602900). Interacts with the terminase large
CC subunit; this interaction may load the terminase onto DNA for packaging
CC (PubMed:12051907). {ECO:0000255|HAMAP-Rule:MF_04164,
CC ECO:0000269|PubMed:12051907, ECO:0000269|PubMed:12496274,
CC ECO:0000269|PubMed:3305506, ECO:0000269|PubMed:33602900}.
CC -!- SIMILARITY: Belongs to the Tevenvirinae RNA polymerase sigma-like
CC factor family. {ECO:0000255|HAMAP-Rule:MF_04164}.
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DR EMBL; X01804; CAA25934.1; -; Genomic_DNA.
DR EMBL; Y00122; CAA68321.1; -; Genomic_DNA.
DR EMBL; M10160; AAC05389.1; -; Genomic_DNA.
DR EMBL; AF158101; AAD42491.1; -; Genomic_DNA.
DR PIR; B30291; Z5BPT4.
DR PIR; T10151; T10151.
DR RefSeq; NP_049679.1; NC_000866.4.
DR PDB; 7D7C; EM; 3.60 A; F=1-185.
DR PDBsum; 7D7C; -.
DR SMR; P04524; -.
DR PRIDE; P04524; -.
DR GeneID; 1258806; -.
DR KEGG; vg:1258806; -.
DR Proteomes; UP000009087; Genome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016987; F:sigma factor activity; IMP:UniProtKB.
DR GO; GO:0019083; P:viral transcription; IEA:UniProtKB-KW.
DR HAMAP; MF_04164; T4_Sigma_like_factor; 1.
DR InterPro; IPR046386; T4_Sigma_like_factor.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Host-virus interaction; Nucleotidyltransferase;
KW Reference proteome; Sigma factor; Transcription; Transcription regulation;
KW Transferase; Viral transcription.
FT CHAIN 1..185
FT /note="RNA polymerase sigma-like factor"
FT /id="PRO_0000164978"
FT DNA_BIND 114
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04164,
FT ECO:0000269|PubMed:33602900"
FT REGION 13..113
FT /note="Interaction with host RNAP core and recognition of
FT the promoter specific element"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04164,
FT ECO:0000269|PubMed:12496274, ECO:0000269|PubMed:33602900"
FT REGION 114..153
FT /note="Chaperons the template-strand ssDNA of the
FT transcription bubble"
FT /evidence="ECO:0000269|PubMed:33602900"
FT SITE 70
FT /note="Interaction with host RNAP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04164,
FT ECO:0000269|PubMed:33602900"
FT SITE 74
FT /note="Interaction with host RNAP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04164,
FT ECO:0000269|PubMed:33602900"
FT SITE 77
FT /note="Interaction with host RNAP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04164,
FT ECO:0000269|PubMed:33602900"
FT MUTAGEN 13
FT /note="N->A: 40% loss of transcription capacity."
FT /evidence="ECO:0000269|PubMed:33602900"
FT MUTAGEN 54
FT /note="L->A: 50% loss of transcription capacity."
FT /evidence="ECO:0000269|PubMed:33602900"
FT MUTAGEN 57
FT /note="R->A: 45% loss of transcription capacity."
FT /evidence="ECO:0000269|PubMed:33602900"
FT MUTAGEN 70
FT /note="E->A: Loss of interaction with host RNAP core."
FT /evidence="ECO:0000269|PubMed:12496274"
FT MUTAGEN 74
FT /note="D->A: Loss of interaction with host RNAP core."
FT /evidence="ECO:0000269|PubMed:12496274"
FT MUTAGEN 77
FT /note="E->A: Loss of interaction with host RNAP core."
FT /evidence="ECO:0000269|PubMed:12496274"
FT MUTAGEN 78
FT /note="A->G: Loss of interaction with host RNAP core."
FT /evidence="ECO:0000269|PubMed:12496274"
FT MUTAGEN 82
FT /note="G->A: Loss of interaction with host RNAP core."
FT /evidence="ECO:0000269|PubMed:12496274"
FT MUTAGEN 83
FT /note="L->A: Loss of interaction with host RNAP core."
FT /evidence="ECO:0000269|PubMed:12496274"
FT MUTAGEN 86
FT /note="F->A: 60% loss of transcription capacity."
FT /evidence="ECO:0000269|PubMed:33602900"
FT MUTAGEN 95
FT /note="H->A: 65% loss of transcription capacity."
FT /evidence="ECO:0000269|PubMed:33602900"
FT MUTAGEN 97
FT /note="Y->A: 65% loss of transcription capacity."
FT /evidence="ECO:0000269|PubMed:33602900"
FT MUTAGEN 99
FT /note="T->A: 40% loss of transcription capacity."
FT /evidence="ECO:0000269|PubMed:33602900"
FT CONFLICT 175
FT /note="P -> S (in Ref. 3; CAA68321)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 185 AA; 21536 MW; C516CD13A63963D4 CRC64;
MSETKPKYNY VNNKELLQAI IDWKTELANN KDPNKVVRQN DTIGLAIMLI AEGLSKRFNF
SGYTQSWKQE MIADGIEASI KGLHNFDETK YKNPHAYITQ ACFNAFVQRI KKERKEVAKK
YSYFVHNVYD SRDDDMVALV DETFIQDIYD KMTHYEESTY RTPGAEKKSV VDDSPSLDFL
YEAND
