ID   REGQ_BPHK0              Reviewed;         207 AA.
AC   Q02582;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Antitermination protein Q {ECO:0000255|HAMAP-Rule:MF_04158};
GN   Name=Q;
OS   Escherichia phage HK022 (Bacteriophage HK022).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Siphoviridae; Hendrixvirinae; Shamshuipovirus.
OX   NCBI_TaxID=10742;
OH   NCBI_TaxID=562; Escherichia coli.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1522593; DOI=10.1016/0022-2836(92)90679-e;
RA   Atkinson B.L., Gottesman M.E.;
RT   "The Escherichia coli rpoB60 mutation blocks antitermination by coliphage
RT   HK022 Q-function.";
RL   J. Mol. Biol. 227:29-37(1992).
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; X60309; CAA42854.1; -; Genomic_DNA.
DR   PIR; S28977; S28977.
DR   RefSeq; NP_037694.1; NC_002166.1.
DR   SMR; Q02582; -.
DR   GeneID; 1262474; -.
DR   KEGG; vg:1262474; -.
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; Transcription;
KW   Transcription regulation; Transcription termination; Zinc; Zinc-finger.
FT   CHAIN           1..207
FT                   /note="Antitermination protein Q"
FT                   /id="PRO_0000073892"
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..29
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"
SQ   SEQUENCE   207 AA;  22488 MW;  019E83D9D997ACCE CRC64;
     MRLESVAKFH SPKSPMMSDS PRTTASDSLS GTDVMAAMGM AQSQAGFGMA AFCGKHELSQ
     NDKQKAINYL MQFAHKVSGK YRGVAKLEGN TKAKVLQVLA TFAYADYCRS AATPGARCRD
     CHGTGRAVDI AKTEQWGRVV EKECGRCKGV GYSRMPASAA YRAVTMLIPN LTQPTWSRTV
     KPLYDALVVQ CHKEESIADN ILNAVAR