ID   RPC2_LAMBD              Reviewed;          97 AA.
AC   P03042;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   02-JUN-2021, entry version 112.
DE   RecName: Full=Transcriptional activator II;
GN   Name=cII; OrderedLocusNames=lambdap59;
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].
RC   STRAIN=DVH93;
RX   PubMed=264238; DOI=10.1038/272410a0;
RA   Schwarz E., Scherer G., Hobom G., Koessel H.;
RT   "Nucleotide sequence of cro, cII and part of the O gene in phage lambda
RT   DNA.";
RL   Nature 272:410-414(1978).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=IMM434;
RX   PubMed=478301; DOI=10.1016/0378-1119(79)90060-x;
RA   Ovchinnikov Y.A., Guryev S.O., Krayev A.S., Monastyrskaya G.S.,
RA   Skryabin K.G., Sverdlov E.D., Zakharyev V.M., Bayev A.A.;
RT   "Primary structure of an EcoRI fragment of lambda imm434 DNA containing
RT   regions cI-cro of phage 434 and cII-o of phage lambda.";
RL   Gene 6:235-249(1979).
RN   [4]
RP   FUNCTION.
RX   PubMed=6295882; DOI=10.1016/0378-1119(82)90020-8;
RA   Benedik M., Mascarenhas D., Campbell A.;
RT   "Probing cII and himA action at the integrase promoter pi of bacteriophage
RT   lambda.";
RL   Gene 19:303-311(1982).
RN   [5]
RP   FUNCTION.
RX   PubMed=3159014; DOI=10.1073/pnas.82.10.3134;
RA   Hoopes B.C., McClure W.R.;
RT   "A cII-dependent promoter is located within the Q gene of bacteriophage
RT   lambda.";
RL   Proc. Natl. Acad. Sci. U.S.A. 82:3134-3138(1985).
RN   [6]
RP   FUNCTION.
RX   PubMed=9218777; DOI=10.1046/j.1365-2958.1997.4231796.x;
RA   Shotland Y., Koby S., Teff D., Mansur N., Oren D.A., Tatematsu K.,
RA   Tomoyasu T., Kessel M., Bukau B., Ogura T., Oppenheim A.B.;
RT   "Proteolysis of the phage lambda CII regulatory protein by FtsH (HflB) of
RT   Escherichia coli.";
RL   Mol. Microbiol. 24:1303-1310(1997).
RN   [7]
RP   FUNCTION.
RX   PubMed=19853572; DOI=10.1016/j.abb.2009.10.010;
RA   Parua P.K., Mondal A., Parrack P.;
RT   "HflD, an Escherichia coli protein involved in the lambda lysis-lysogeny
RT   switch, impairs transcription activation by lambdaCII.";
RL   Arch. Biochem. Biophys. 493:175-183(2010).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.56 ANGSTROMS).
RX   PubMed=16061804; DOI=10.1073/pnas.0504535102;
RA   Datta A.B., Panjikar S., Weiss M.S., Chakrabarti P., Parrack P.;
RT   "Structure of lambda CII: implications for recognition of direct-repeat DNA
RT   by an unusual tetrameric organization.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:11242-11247(2005).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RX   PubMed=16039594; DOI=10.1016/j.molcel.2005.06.006;
RA   Jain D., Kim Y., Maxwell K.L., Beasley S., Zhang R., Gussin G.N.,
RA   Edwards A.M., Darst S.A.;
RT   "Crystal structure of bacteriophage lambda cII and its DNA complex.";
RL   Mol. Cell 19:259-269(2005).
CC   -!- FUNCTION: Acts as a transcriptional activator that allows virus to
CC       initiate a latent state. Following infection, participates, together
CC       with cIII, in activation of the Pe and Pi promoters, which are
CC       responsible for the transcription of the cI (repressor) and int
CC       (integrase) genes, respectively. Both of these gene products are
CC       required for the establishment of latency.
CC       {ECO:0000269|PubMed:19853572, ECO:0000269|PubMed:3159014,
CC       ECO:0000269|PubMed:6295882, ECO:0000269|PubMed:9218777}.
CC   -!- SUBUNIT: Homotetramer. Interacts with cIII; this interaction is
CC       essential to stabilize cII that would otherwise be quickly degraded by
CC       host protease FtsH.
CC   -!- INTERACTION:
CC       P03042; P0AAI3: ftsH; Xeno; NbExp=5; IntAct=EBI-4478343, EBI-548381;
CC   -!- MISCELLANEOUS: Lambda-imm434 is a hybrid of bacteriophages 434 and
CC       lambda. The cII protein coding region is in the lambda portion of the
CC       imm434 genome.
CC   -!- SIMILARITY: Belongs to the lambda phage cII protein family.
CC       {ECO:0000305}.
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DR   EMBL; J02460; AAA32246.1; -; Genomic_DNA.
DR   EMBL; J02459; AAA96583.1; -; Genomic_DNA.
DR   PIR; A03579; QCBP2L.
DR   RefSeq; NP_040630.1; NC_001416.1.
DR   PDB; 1XWR; X-ray; 2.56 A; A/B/C/D=1-97.
DR   PDB; 1ZPQ; X-ray; 2.80 A; A/B/C/D=1-97.
DR   PDB; 1ZS4; X-ray; 1.70 A; A/B/C/D=4-82.
DR   PDBsum; 1XWR; -.
DR   PDBsum; 1ZPQ; -.
DR   PDBsum; 1ZS4; -.
DR   SMR; P03042; -.
DR   IntAct; P03042; 3.
DR   GeneID; 2703494; -.
DR   KEGG; vg:2703494; -.
DR   EvolutionaryTrace; P03042; -.
DR   Proteomes; UP000001711; Genome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   GO; GO:0019042; P:viral latency; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.260.40; -; 1.
DR   InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR   InterPro; IPR007933; Transcrpt_activ_CII.
DR   Pfam; PF05269; Phage_CII; 1.
DR   SUPFAM; SSF47413; SSF47413; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; DNA-binding; Early protein; Reference proteome;
KW   Transcription; Transcription regulation; Viral latency;
KW   Viral latency initiation and maintenance.
FT   CHAIN           1..97
FT                   /note="Transcriptional activator II"
FT                   /id="PRO_0000077592"
FT   DNA_BIND        26..45
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255"
FT   HELIX           6..24
FT                   /evidence="ECO:0007829|PDB:1ZS4"
FT   HELIX           26..33
FT                   /evidence="ECO:0007829|PDB:1ZS4"
FT   HELIX           37..46
FT                   /evidence="ECO:0007829|PDB:1ZS4"
FT   HELIX           48..58
FT                   /evidence="ECO:0007829|PDB:1ZS4"
FT   HELIX           64..77
FT                   /evidence="ECO:0007829|PDB:1ZS4"
SQ   SEQUENCE   97 AA;  11056 MW;  AF4E0428E68DB9E8 CRC64;
     MVRANKRNEA LRIESALLNK IAMLGTEKTA EAVGVDKSQI SRWKRDWIPK FSMLLAVLEW
     GVVDDDMARL ARQVAAILTN KKRPAATERS EQIQMEF