REGQ_LAMBD
ID REGQ_LAMBD Reviewed; 207 AA.
AC P03047; Q38271;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Antitermination protein Q {ECO:0000255|HAMAP-Rule:MF_04158};
GN Name=Q {ECO:0000255|HAMAP-Rule:MF_04158};
OS Escherichia phage lambda (Bacteriophage lambda).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Siphoviridae; Lambdavirus.
OX NCBI_TaxID=10710;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=6221115; DOI=10.1016/0022-2836(82)90546-0;
RA Sanger F., Coulson A.R., Hong G.F., Hill D.F., Petersen G.B.;
RT "Nucleotide sequence of bacteriophage lambda DNA.";
RL J. Mol. Biol. 162:729-773(1982).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6458514; DOI=10.1016/0014-5793(81)80532-7;
RA Petrov N.A., Karginov V.A., Mikriukov N.N., Serpinski O.I.,
RA Kravchenko V.V.;
RT "Complete nucleotide sequence of the bacteriophage lambda DNA region
RT containing gene Q and promoter pR'.";
RL FEBS Lett. 133:316-320(1981).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Petrov N.A., Serpinski O.I., Mikryukov N.N., Karginov V.A.,
RA Kravchenko V.V.;
RT "Nucleotide sequence of the bacteriophage lambda DNA region containing gene
RT Q.";
RL Bioorg. Khim. 8:561-563(1982).
RN [4]
RP REVIEW.
RX PubMed=10384296; DOI=10.1101/sqb.1998.63.319;
RA Roberts J.W., Yarnell W., Bartlett E., Guo J., Marr M., Ko D.C., Sun H.,
RA Roberts C.W.;
RT "Antitermination by bacteriophage lambda Q protein.";
RL Cold Spring Harb. Symp. Quant. Biol. 63:319-325(1998).
RN [5]
RP MUTAGENESIS OF GLU-134; VAL-189 AND HIS-192, AND DNA-BINDING.
RX PubMed=15150248; DOI=10.1128/jb.186.11.3599-3608.2004;
RA Guo J., Roberts J.W.;
RT "DNA binding regions of Q proteins of phages lambda and phi80.";
RL J. Bacteriol. 186:3599-3608(2004).
RN [6]
RP FUNCTION, AND INTERACTION WITH HOST RPOB.
RX PubMed=18832144; DOI=10.1073/pnas.0805757105;
RA Deighan P., Diez C.M., Leibman M., Hochschild A., Nickels B.E.;
RT "The bacteriophage lambda Q antiterminator protein contacts the beta-flap
RT domain of RNA polymerase.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:15305-15310(2008).
RN [7]
RP FUNCTION.
RX PubMed=25092034; DOI=10.1128/jb.01705-14;
RA Svenningsen S.L., Semsey S.;
RT "Commitment to lysogeny is preceded by a prolonged period of sensitivity to
RT the late lytic regulator Q in bacteriophage lambda.";
RL J. Bacteriol. 196:3582-3588(2014).
RN [8]
RP FUNCTION.
RX PubMed=31455742; DOI=10.1073/pnas.1909801116;
RA Yin Z., Kaelber J.T., Ebright R.H.;
RT "Structural basis of Q-dependent antitermination.";
RL Proc. Natl. Acad. Sci. U.S.A. 116:18384-18390(2019).
RN [9]
RP INTERACTION WITH HOST NUSA.
RX PubMed=32313022; DOI=10.1038/s41598-020-63523-5;
RA Dudenhoeffer B.R., Borggraefe J., Schweimer K., Knauer S.H.;
RT "NusA directly interacts with antitermination factor Q from phage lambda.";
RL Sci. Rep. 10:6607-6607(2020).
RN [10] {ECO:0007744|PDB:4MO1}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 38-207 IN COMPLEX WITH ZINC,
RP INTERACTION WITH HOST RPOB, INTERACTION WITH HOST RNA POLYMERASE SIGMA
RP FACTOR RPOD, DNA-BINDING, AND MUTAGENESIS OF GLU-134.
RX PubMed=24440517; DOI=10.1016/j.str.2013.12.010;
RA Vorobiev S.M., Gensler Y., Vahedian-Movahed H., Seetharaman J., Su M.,
RA Huang J.Y., Xiao R., Kornhaber G., Montelione G.T., Tong L., Ebright R.H.,
RA Nickels B.E.;
RT "Structure of the DNA-binding and RNA-polymerase-binding region of
RT transcription antitermination factor lambdaQ.";
RL Structure 22:488-495(2014).
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 (PubMed:18832144, PubMed:10384296, PubMed:31455742).
CC Competes with host factor sigma 70 for binding to RPOB, the beta-
CC subunit of host RNAP (PubMed:18832144). To join the elongation complex,
CC binds a specific DNA Q-binding element (QBE) and interacts with RNAP
CC that is paused during early elongation (PubMed:10384296). Participates
CC in the lysis-lysogeny decision by activating the expression of the late
CC lytic genes (PubMed:25092034). {ECO:0000255|HAMAP-Rule:MF_04158,
CC ECO:0000269|PubMed:18832144, ECO:0000269|PubMed:25092034,
CC ECO:0000269|PubMed:31455742, ECO:0000303|PubMed:10384296}.
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 (PubMed:18832144). Interacts with host
CC RNA polymerase sigma factor RPOD (via domain-4) (PubMed:24440517).
CC Interacts with host NUSA (via N-terminus and AR2 domain); this
CC interaction releases the autoinhibition of NUSA (PubMed:32313022).
CC {ECO:0000255|HAMAP-Rule:MF_04158, ECO:0000269|PubMed:18832144,
CC ECO:0000269|PubMed:24440517, ECO:0000269|PubMed:32313022}.
CC -!- SIMILARITY: Belongs to the phage antitermination Q type 2 family.
CC {ECO:0000255|HAMAP-Rule:MF_04158}.
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DR EMBL; J02459; AAA96595.1; -; Genomic_DNA.
DR EMBL; M38285; AAA32253.1; -; Genomic_DNA.
DR PIR; E94614; ZQBPL.
DR RefSeq; NP_040642.1; NC_001416.1.
DR PDB; 4MO1; X-ray; 2.10 A; A/B=38-207.
DR PDBsum; 4MO1; -.
DR SMR; P03047; -.
DR IntAct; P03047; 9.
DR DNASU; 2703477; -.
DR GeneID; 2703477; -.
DR KEGG; vg:2703477; -.
DR Proteomes; UP000001711; 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 GO; GO:0031564; P:transcription antitermination; IDA:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Host-virus interaction; Metal-binding;
KW Reference proteome; Transcription; Transcription regulation;
KW Transcription termination; Zinc; Zinc-finger.
FT CHAIN 1..207
FT /note="Antitermination protein Q"
FT /id="PRO_0000073895"
FT ZN_FING 118..147
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04158,
FT ECO:0000305|PubMed:24440517"
FT DNA_BIND 171..192
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04158,
FT ECO:0000269|PubMed:15150248, ECO:0000269|PubMed:24440517"
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 ECO:0000269|PubMed:24440517"
FT BINDING 121
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04158,
FT ECO:0000269|PubMed:24440517"
FT BINDING 144
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04158,
FT ECO:0000269|PubMed:24440517"
FT BINDING 147
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04158,
FT ECO:0000269|PubMed:24440517"
FT SITE 101
FT /note="Interaction with host rpoB"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04158,
FT ECO:0000269|PubMed:24440517"
FT SITE 134
FT /note="Interaction with host RNA polymerase sigma factor
FT RPOD"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04158,
FT ECO:0000269|PubMed:24440517"
FT SITE 160
FT /note="Interaction with host rpoB"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04158,
FT ECO:0000269|PubMed:24440517"
FT SITE 165
FT /note="Interaction with host rpoB"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04158,
FT ECO:0000269|PubMed:24440517"
FT MUTAGEN 134
FT /note="E->K: Increased binding to QBE and increased
FT suppressor activity."
FT /evidence="ECO:0000269|PubMed:15150248,
FT ECO:0000269|PubMed:24440517"
FT MUTAGEN 189
FT /note="V->E: Increased suppressor activity."
FT /evidence="ECO:0000269|PubMed:15150248"
FT MUTAGEN 192
FT /note="H->Y: Increased suppressor activity."
FT /evidence="ECO:0000269|PubMed:15150248"
FT CONFLICT 102..103
FT /note="FA -> LP (in Ref. 2; AAA32253)"
FT /evidence="ECO:0000305"
FT CONFLICT 111
FT /note="A -> G (in Ref. 2; AAA32253)"
FT /evidence="ECO:0000305"
FT CONFLICT 205
FT /note="V -> I (in Ref. 2 and 3)"
FT /evidence="ECO:0000305"
FT HELIX 63..77
FT /evidence="ECO:0007829|PDB:4MO1"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:4MO1"
FT HELIX 82..85
FT /evidence="ECO:0007829|PDB:4MO1"
FT HELIX 89..112
FT /evidence="ECO:0007829|PDB:4MO1"
FT TURN 119..123
FT /evidence="ECO:0007829|PDB:4MO1"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:4MO1"
FT HELIX 130..136
FT /evidence="ECO:0007829|PDB:4MO1"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:4MO1"
FT TURN 145..149
FT /evidence="ECO:0007829|PDB:4MO1"
FT HELIX 157..167
FT /evidence="ECO:0007829|PDB:4MO1"
FT HELIX 173..179
FT /evidence="ECO:0007829|PDB:4MO1"
FT HELIX 181..202
FT /evidence="ECO:0007829|PDB:4MO1"
SQ SEQUENCE 207 AA; 22473 MW; 12D4D3AF93DBACDB CRC64;
MRLESVAKFH SPKSPMMSDS PRATASDSLS GTDVMAAMGM AQSQAGFGMA AFCGKHELSQ
NDKQKAINYL MQFAHKVSGK YRGVAKLEGN TKAKVLQVLA TFAYADYCRS AATPGARCRD
CHGTGRAVDI AKTELWGRVV EKECGRCKGV GYSRMPASAA YRAVTMLIPN LTQPTWSRTV
KPLYDALVVQ CHKEESIADN ILNAVTR
