RCRO_LAMBD
ID RCRO_LAMBD Reviewed; 66 AA.
AC P03040;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 02-JUN-2021, entry version 143.
DE RecName: Full=Regulatory protein cro;
GN Name=cro; OrderedLocusNames=lambdap57;
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].
RX PubMed=593347; DOI=10.1038/270274a0;
RA Roberts T.M., Shimatake H., Brady C., Rosenberg M.;
RT "Sequence of Cro gene of bacteriophage lambda.";
RL Nature 270:274-275(1977).
RN [4]
RP PROTEIN SEQUENCE.
RX PubMed=593348; DOI=10.1038/270275a0;
RA Hsiang M.W., Cole R.D., Takeda Y., Echols H.;
RT "Amino acid sequence of Cro regulatory protein of bacteriophage lambda.";
RL Nature 270:275-277(1977).
RN [5]
RP FUNCTION.
RX PubMed=1065873; DOI=10.1073/pnas.73.7.2249;
RA Folkmanis A., Takeda Y., Simuth J., Gussin G., Echols H.;
RT "Purification and properties of a DNA-binding protein with characteristics
RT expected for the Cro protein of bacteriophage lambda, a repressor essential
RT for lytic growth.";
RL Proc. Natl. Acad. Sci. U.S.A. 73:2249-2253(1976).
RN [6]
RP FUNCTION.
RX PubMed=6457992; DOI=10.1038/294217a0;
RA Johnson A.D., Poteete A.R., Lauer G., Sauer R.T., Ackers G.K., Ptashne M.;
RT "lambda Repressor and cro--components of an efficient molecular switch.";
RL Nature 294:217-223(1981).
RN [7]
RP FUNCTION.
RX PubMed=17908932; DOI=10.1101/gad.1584907;
RA Schubert R.A., Dodd I.B., Egan J.B., Shearwin K.E.;
RT "Cro's role in the CI Cro bistable switch is critical for lambda's
RT transition from lysogeny to lytic development.";
RL Genes Dev. 21:2461-2472(2007).
RN [8]
RP FUNCTION.
RX PubMed=29158090; DOI=10.1016/j.jmb.2017.11.005;
RA Lee S., Lewis D.E.A., Adhya S.;
RT "The Developmental Switch in Bacteriophage lambda: A Critical Role of the
RT Cro Protein.";
RL J. Mol. Biol. 430:58-68(2018).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RX PubMed=6452580; DOI=10.1038/290754a0;
RA Anderson W.F., Ohlendorf D.H., Takeda Y., Matthews B.W.;
RT "Structure of the cro repressor from bacteriophage lambda and its
RT interaction with DNA.";
RL Nature 290:754-758(1981).
RN [10]
RP COMPARISON OF X-RAY STRUCTURES.
RX PubMed=6226802; DOI=10.1016/s0022-2836(83)80169-7;
RA Ohlendorf D.H., Anderson W.F., Lewis M., Pabo C.O., Matthews B.W.;
RT "Comparison of the structures of cro and lambda repressor proteins from
RT bacteriophage lambda.";
RL J. Mol. Biol. 169:757-769(1983).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (3.9 ANGSTROMS).
RX PubMed=2146682; DOI=10.1073/pnas.87.20.8165;
RA Brennan R.G., Roderick S.L., Takeda Y., Matthews B.W.;
RT "Protein-DNA conformational changes in the crystal structure of a lambda
RT Cro-operator complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:8165-8169(1990).
RN [12] {ECO:0007744|PDB:1COP}
RP STRUCTURE BY NMR.
RX PubMed=7500341; DOI=10.1006/jmbi.1995.0646;
RA Matsuo H., Shirakawa M., Kyogoku Y.;
RT "Three-dimensional dimer structure of the lambda-Cro repressor in solution
RT as determined by heteronuclear multidimensional NMR.";
RL J. Mol. Biol. 254:668-680(1995).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX PubMed=9653036; DOI=10.1006/jmbi.1998.1849;
RA Ohlendorf D.H., Tronrud D.E., Matthews B.W.;
RT "Refined structure of Cro repressor protein from bacteriophage lambda
RT suggests both flexibility and plasticity.";
RL J. Mol. Biol. 280:129-136(1998).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RX PubMed=9653037; DOI=10.1006/jmbi.1998.1848;
RA Albright R.A., Matthews B.W.;
RT "Crystal structure of lambda-Cro bound to a consensus operator at 3.0 A
RT resolution.";
RL J. Mol. Biol. 280:137-151(1998).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RX PubMed=9684880; DOI=10.1002/pro.5560070701;
RA Albright R.A., Mossing M.C., Matthews B.W.;
RT "Crystal structure of an engineered Cro monomer bound nonspecifically to
RT DNA: possible implications for nonspecific binding by the wild-type
RT protein.";
RL Protein Sci. 7:1485-1494(1998).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS).
RX PubMed=10686105; DOI=10.1006/jmbi.1999.3498;
RA Rupert P.B., Mollah A.K., Mossing M.C., Matthews B.W.;
RT "The structural basis for enhanced stability and reduced DNA binding seen
RT in engineered second-generation Cro monomers and dimers.";
RL J. Mol. Biol. 296:1079-1090(2000).
RN [17] {ECO:0007744|PDB:2A63}
RP STRUCTURE BY NMR, AND MUTAGENESIS OF ALA-33 AND PHE-58.
RX PubMed=16700549; DOI=10.1021/bi052541c;
RA Newlove T., Atkinson K.R., Van Dorn L.O., Cordes M.H.;
RT "A trade between similar but nonequivalent intrasubunit and intersubunit
RT contacts in Cro dimer evolution.";
RL Biochemistry 45:6379-6391(2006).
RN [18] {ECO:0007744|PDB:2ECS, ECO:0007744|PDB:2OVG}
RP X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS), AND SUBUNIT.
RX PubMed=18054042; DOI=10.1016/j.jmb.2007.10.082;
RA Hall B.M., Roberts S.A., Heroux A., Cordes M.H.;
RT "Two structures of a lambda Cro variant highlight dimer flexibility but
RT disfavor major dimer distortions upon specific binding of cognate DNA.";
RL J. Mol. Biol. 375:802-811(2008).
CC -!- FUNCTION: Plays an essential role in the switch from lysogenic to lytic
CC state and in fine-tuning the lytic phase activation. Mediates the de-
CC repression of the lytic promoters from repression by cI at an early
CC stage of prophage induction. Turns down the expression of the
CC transcriptional activator cII, a factor that initiates the expression
CC of repressor cI, the major component promoting latency. Additionally,
CC cro is able to directly bind to the promoter region of cI thereby
CC preventing the transcription of cI repressor. These two mechanisms
CC ultimately lead to a strong decrease in the amount of cI that will
CC become unable to maintain the latent phase, allowing the transition to
CC lytic growth. Low level of Cro also stimulates the lytic promoters
CC while cI repressor is still present (PubMed:29158090). Cro-mediated up-
CC regulation of pR and pL ultimately leads to its own increased
CC expression and to a successful switch to lytic growth
CC (PubMed:29158090). The second function assigned to Cro is the fine-
CC tuning of the lytic phase activation. Indeed, cro initially diminishes
CC the strength of activation by turning down the expression of lytic
CC genes as well as its own expression. {ECO:0000269|PubMed:1065873,
CC ECO:0000269|PubMed:17908932, ECO:0000269|PubMed:29158090,
CC ECO:0000269|PubMed:6457992}.
CC -!- SUBUNIT: Binds DNA as a homodimer. {ECO:0000269|PubMed:18054042}.
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DR EMBL; J02459; AAA96582.1; -; Genomic_DNA.
DR PIR; B94614; RCBPL.
DR RefSeq; NP_040629.1; NC_001416.1.
DR PDB; 1COP; NMR; -; D/E=1-66.
DR PDB; 1D1L; X-ray; 2.10 A; A=1-61.
DR PDB; 1D1M; X-ray; 2.05 A; A/B=1-60.
DR PDB; 1ORC; X-ray; 1.54 A; A=1-66.
DR PDB; 2A63; NMR; -; A=1-66.
DR PDB; 2ECS; X-ray; 1.40 A; A/B=1-66.
DR PDB; 2ORC; NMR; -; A=1-66.
DR PDB; 2OVG; X-ray; 1.35 A; A=1-66.
DR PDB; 3ORC; X-ray; 3.00 A; A=2-61.
DR PDB; 4CRO; X-ray; 3.90 A; A/B/C/D/E/F=1-66.
DR PDB; 5CRO; X-ray; 2.30 A; A/B/C/O=1-66.
DR PDB; 6CRO; X-ray; 3.00 A; A=2-61.
DR PDBsum; 1COP; -.
DR PDBsum; 1D1L; -.
DR PDBsum; 1D1M; -.
DR PDBsum; 1ORC; -.
DR PDBsum; 2A63; -.
DR PDBsum; 2ECS; -.
DR PDBsum; 2ORC; -.
DR PDBsum; 2OVG; -.
DR PDBsum; 3ORC; -.
DR PDBsum; 4CRO; -.
DR PDBsum; 5CRO; -.
DR PDBsum; 6CRO; -.
DR BMRB; P03040; -.
DR SMR; P03040; -.
DR IntAct; P03040; 1.
DR GeneID; 2703466; -.
DR GeneID; 2703467; -.
DR KEGG; vg:2703467; -.
DR EvolutionaryTrace; P03040; -.
DR Proteomes; UP000001711; Genome.
DR GO; GO:0001046; F:core promoter sequence-specific DNA binding; IDA:CAFA.
DR GO; GO:0003677; F:DNA binding; IDA:CAFA.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:CAFA.
DR GO; GO:0098689; P:latency-replication decision; IDA:UniProtKB.
DR GO; GO:0010944; P:negative regulation of transcription by competitive promoter binding; IMP:CAFA.
DR GO; GO:0032897; P:negative regulation of viral transcription; IDA:UniProtKB.
DR GO; GO:0019046; P:release from viral latency; IMP:CAFA.
DR GO; GO:0009411; P:response to UV; IMP:CAFA.
DR DisProt; DP00741; -.
DR Gene3D; 3.30.240.10; -; 1.
DR InterPro; IPR000655; Cro.
DR InterPro; IPR038202; Cro_sf.
DR InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR Pfam; PF09048; Cro; 1.
DR PIRSF; PIRSF003217; Cro_protein; 1.
DR PRINTS; PR00030; HTHCRO.
DR SUPFAM; SSF47413; SSF47413; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; DNA-binding; Early protein;
KW Latency-replication decision; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Viral latency;
KW Viral latency initiation and maintenance.
FT CHAIN 1..66
FT /note="Regulatory protein cro"
FT /id="PRO_0000077579"
FT DNA_BIND 16..35
FT /note="H-T-H motif"
FT MUTAGEN 33
FT /note="A->W: Loss of dimerization; when associated with D-
FT 58."
FT /evidence="ECO:0000269|PubMed:18054042"
FT MUTAGEN 58
FT /note="F->D: Loss of dimerization; when associated with W-
FT 33."
FT /evidence="ECO:0000269|PubMed:18054042"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:2ECS"
FT HELIX 7..14
FT /evidence="ECO:0007829|PDB:2OVG"
FT HELIX 16..23
FT /evidence="ECO:0007829|PDB:2OVG"
FT HELIX 27..36
FT /evidence="ECO:0007829|PDB:2OVG"
FT STRAND 39..44
FT /evidence="ECO:0007829|PDB:2OVG"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:3ORC"
FT STRAND 50..55
FT /evidence="ECO:0007829|PDB:2OVG"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:3ORC"
SQ SEQUENCE 66 AA; 7363 MW; 233A02DA0873E4D4 CRC64;
MEQRITLKDY AMRFGQTKTA KDLGVYQSAI NKAIHAGRKI FLTINADGSV YAEEVKPFPS
NKKTTA
