ID   LTACT_BPT4              Reviewed;         112 AA.
AC   P13338;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Late transcription coactivator {ECO:0000255|HAMAP-Rule:MF_04165, ECO:0000303|PubMed:22135460};
DE   AltName: Full=Gene product 33;
DE            Short=gp33;
DE   AltName: Full=RNA polymerase-associated protein Gp33 {ECO:0000255|HAMAP-Rule:MF_04165};
GN   Name=33;
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].
RC   STRAIN=BK536;
RX   PubMed=2674900; DOI=10.1093/nar/17.16.6729;
RA   Hahn S., Rueger W.;
RT   "Organization of the bacteriophage T4 genome between map positions 150.745
RT   and 145.824.";
RL   Nucleic Acids Res. 17:6729-6729(1989).
RN   [2]
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   [3]
RP   DOMAIN, INTERACTION WITH HOST RNAP, AND FUNCTION.
RX   PubMed=8106327; DOI=10.1128/jb.176.4.1164-1171.1994;
RA   Winkelman J.W., Kassavetis G.A., Geiduschek E.P.;
RT   "Molecular genetic analysis of a prokaryotic transcriptional coactivator:
RT   functional domains of the bacteriophage T4 gene 33 protein.";
RL   J. Bacteriol. 176:1164-1171(1994).
RN   [4] {ECO:0007744|PDB:3TBI}
RP   X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS), AND INTERACTION WITH HOST RPOB.
RX   PubMed=22135460; DOI=10.1073/pnas.1113328108;
RA   Twist K.A., Campbell E.A., Deighan P., Nechaev S., Jain V.,
RA   Geiduschek E.P., Hochschild A., Darst S.A.;
RT   "Crystal structure of the bacteriophage T4 late-transcription coactivator
RT   gp33 with the beta-subunit flap domain of Escherichia coli RNA
RT   polymerase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:19961-19966(2011).
RN   [5] {ECO:0007744|PDB:7D7D}
RP   STRUCTURE BY ELECTRON MICROSCOPY (4.50 ANGSTROMS), IDENTIFICATION IN THE
RP   TRANSCRIPTION ACTIVATION COMPLEX, INTERACTION WITH HOST RNAP, AND FUNCTION.
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: Activates transcription at late promoters when the sliding
CC       clamp is present (PubMed:33602900). Binds to both the host RNA
CC       polymerase (RNAP) and the upstream dsDNA (PubMed:33602900,
CC       PubMed:8106327). {ECO:0000255|HAMAP-Rule:MF_04165,
CC       ECO:0000269|PubMed:33602900, ECO:0000269|PubMed:8106327}.
CC   -!- SUBUNIT: Interacts with the beta subunit of host RNAP RpoB (via flap
CC       domain) (PubMed:33602900, PubMed:22135460). Part of the transcription
CC       activation complex containing host RNAP, the viral RNA polymerase
CC       sigma-like factor, the coactivator gp33, and the sliding clamp
CC       (PubMed:33602900). {ECO:0000255|HAMAP-Rule:MF_04165,
CC       ECO:0000269|PubMed:22135460, ECO:0000269|PubMed:33602900}.
CC   -!- INTERACTION:
CC       P13338; P0A8V2: rpoB; Xeno; NbExp=5; IntAct=EBI-15955782, EBI-544996;
CC   -!- DOMAIN: The C-terminus is involved in transcriptional enhancement.
CC       {ECO:0000255|HAMAP-Rule:MF_04165, ECO:0000269|PubMed:8106327}.
CC   -!- SIMILARITY: Belongs to the Tevenvirinae late transcription coactivator
CC       family. {ECO:0000255|HAMAP-Rule:MF_04165}.
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DR   EMBL; X15818; CAA33814.1; -; Genomic_DNA.
DR   EMBL; AF158101; AAD42456.1; -; Genomic_DNA.
DR   PIR; S05558; GWBPT4.
DR   RefSeq; NP_049857.1; NC_000866.4.
DR   PDB; 3TBI; X-ray; 3.00 A; A=1-112.
DR   PDB; 7D7D; EM; 4.50 A; K=1-112.
DR   PDBsum; 3TBI; -.
DR   PDBsum; 7D7D; -.
DR   SMR; P13338; -.
DR   DIP; DIP-60377N; -.
DR   IntAct; P13338; 1.
DR   PRIDE; P13338; -.
DR   GeneID; 1258793; -.
DR   KEGG; vg:1258793; -.
DR   Proteomes; UP000009087; Genome.
DR   DisProt; DP00898; -.
DR   Gene3D; 1.10.10.2850; -; 1.
DR   HAMAP; MF_04165; T4_TRANSCR_COACT; 1.
DR   InterPro; IPR046384; LTACT_myovirus.
DR   InterPro; IPR031836; Trans_coact.
DR   InterPro; IPR042071; Trans_coact_sf.
DR   Pfam; PF16805; Trans_coact; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Reference proteome.
FT   CHAIN           1..112
FT                   /note="Late transcription coactivator"
FT                   /id="PRO_0000165019"
FT   REGION          62..92
FT                   /note="Interaction with host RNAP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04165,
FT                   ECO:0000269|PubMed:8106327"
FT   REGION          106..112
FT                   /note="Involved in transcriptional enhancement"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04165,
FT                   ECO:0000269|PubMed:8106327"
FT   HELIX           37..50
FT                   /evidence="ECO:0007829|PDB:3TBI"
FT   HELIX           55..65
FT                   /evidence="ECO:0007829|PDB:3TBI"
FT   HELIX           70..72
FT                   /evidence="ECO:0007829|PDB:3TBI"
FT   HELIX           73..76
FT                   /evidence="ECO:0007829|PDB:3TBI"
FT   HELIX           79..92
FT                   /evidence="ECO:0007829|PDB:3TBI"
FT   HELIX           97..101
FT                   /evidence="ECO:0007829|PDB:3TBI"
SQ   SEQUENCE   112 AA;  12831 MW;  665443899373E04A CRC64;
     MTQFSLNDIR PVDETGLSEK ELSIKKEKDE IAKLLDRQEN GFIIEKMVEE FGMSYLEATT
     AFLEENSIPE TQFAKFIPSG IIEKIQSEAI DENLLRPSVV RCEKTNTLDF LL