REGQ_BPP22
ID REGQ_BPP22 Reviewed; 207 AA.
AC P57020; A0A2H4A365; A8CGF2; Q8LTF1;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2018, sequence version 2.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Antitermination protein Q {ECO:0000255|HAMAP-Rule:MF_04158};
GN Name=23;
OS Salmonella phage P22 (Bacteriophage P22).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Podoviridae; Lederbergvirus.
OX NCBI_TaxID=10754;
OH NCBI_TaxID=90371; Salmonella typhimurium.
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11053393; DOI=10.1128/jb.182.22.6472-6481.2000;
RA Vander Byl C.S., Kropinski A.M.B.;
RT "Sequence of the genome of Salmonella bacteriophage P22.";
RL J. Bacteriol. 182:6472-6481(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12562822; DOI=10.1128/jb.185.4.1475-1477.2003;
RA Pedulla M.L., Ford M.E., Karthikeyan T., Houtz J.M., Hendrix R.W.,
RA Hatfull G.F., Poteete A.R., Gilcrease E.B., Winn-Stapley D.A.,
RA Casjens S.R.;
RT "Corrected sequence of the bacteriophage P22 genome.";
RL J. Bacteriol. 185:1475-1477(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSU;
RX PubMed=18621868; DOI=10.1128/aem.00352-08;
RA Masago Y., Shibata T., Rose J.B.;
RT "Bacteriophage P22 and Staphylococcus aureus attenuation on nonporous
RT fomites as determined by plate assay and quantitative PCR.";
RL Appl. Environ. Microbiol. 74:5838-5840(2008).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19585-B1;
RA Masago Y., Fong T.T., Rose J.B.;
RT "The Molecular Identity of Contaminant Hydrology (20 years later).";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Mediates the switch from middle to viral late gene expression
CC by associating with host RNA polymerase (RNAP) so that the latter can
CC read without pausing and through transcription terminators preceding
CC late genes. Competes with host factor sigma 70 for binding to RPOB, the
CC beta-subunit of host RNAP. To join the elongation complex, binds a
CC specific DNA Q-binding element (QBE) and interacts with RNAP that is
CC paused during early elongation. Participates in the lysis-lysogeny
CC decision by activating the expression of the late lytic genes.
CC {ECO:0000255|HAMAP-Rule:MF_04158}.
CC -!- SUBUNIT: Interacts with host RPOB (via flap domain); this interaction
CC renders host RNAP resistant to transcription pausing and allows it to
CC read through termination signals. Interacts with host RNA polymerase
CC sigma factor RPOD (via domain-4). Interacts with host NUSA (via N-
CC terminus and AR2 domain); this interaction releases the autoinhibition
CC of NUSA. {ECO:0000255|HAMAP-Rule:MF_04158}.
CC -!- SIMILARITY: Belongs to the phage antitermination Q type 2 family.
CC {ECO:0000255|HAMAP-Rule:MF_04158}.
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DR EMBL; AF217253; AAF75038.1; -; Genomic_DNA.
DR EMBL; AB362338; BAF80778.1; -; Genomic_DNA.
DR EMBL; AB426868; BAG12661.1; -; Genomic_DNA.
DR EMBL; AF527608; AAM81439.1; -; Genomic_DNA.
DR EMBL; BK000583; DAA01037.1; -; Genomic_DNA.
DR RefSeq; YP_063730.1; NC_002371.2.
DR SMR; P57020; -.
DR GeneID; 2944235; -.
DR KEGG; vg:2944235; -.
DR Proteomes; UP000001315; Genome.
DR Proteomes; UP000001795; Genome.
DR Proteomes; UP000001796; Genome.
DR Proteomes; UP000002165; Genome.
DR Proteomes; UP000007960; Genome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006353; P:DNA-templated transcription, termination; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR Gene3D; 1.10.274.110; -; 1.
DR HAMAP; MF_04158; Antitermination_lambda; 1.
DR InterPro; IPR038500; Antitermination_sf.
DR InterPro; IPR003222; Antitermntn.
DR InterPro; IPR036410; HSP_DnaJ_Cys-rich_dom_sf.
DR Pfam; PF03589; Antiterm; 2.
DR SUPFAM; SSF57938; SSF57938; 1.
PE 3: Inferred from homology;
KW DNA-binding; Host-virus interaction; Metal-binding; Reference proteome;
KW Transcription; Transcription regulation; Transcription termination; Zinc;
KW Zinc-finger.
FT CHAIN 1..207
FT /note="Antitermination protein Q"
FT /id="PRO_0000073893"
FT ZN_FING 118..147
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04158"
FT DNA_BIND 171..192
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04158"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 118
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04158"
FT BINDING 121
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04158"
FT BINDING 144
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04158"
FT BINDING 147
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04158"
FT SITE 101
FT /note="Interaction with host rpoB"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04158"
FT SITE 134
FT /note="Interaction with host RNA polymerase sigma factor
FT RPOD"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04158"
FT SITE 160
FT /note="Interaction with host rpoB"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04158"
FT SITE 165
FT /note="Interaction with host rpoB"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04158"
FT CONFLICT 150..155
FT /note="VGYSKV -> FGCSKA (in Ref. 1; AAF75038)"
FT /evidence="ECO:0000305"
FT CONFLICT 162..164
FT /note="RAI -> LSV (in Ref. 1; AAF75038)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 207 AA; 22353 MW; B3372AB63182C27F CRC64;
MRLESVAKFH SPKSPMMSDS PRATASDSLS GTDVMAAMGM AQSQAGFGMA AFCGKHELSQ
NDKQKAINYL MQFAHKVSGK YPGVAKLEGN TKAKVLQVLA TFAYADYCRS AATPGARCRD
CHGTGRAVDI AKTEQWGRVV EKVCGRCKGV GYSKVPASAA YRAITMLIPN LTQPTWSRTV
KPLYDALVVQ CHKEESIADN ILNAVTR
