ID   RCRO_BP434              Reviewed;          71 AA.
AC   P03036;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   02-JUN-2021, entry version 106.
DE   RecName: Full=Regulatory protein cro;
DE   AltName: Full=Antirepressor;
GN   Name=CRO;
OS   Enterobacteria phage 434 (Bacteriophage 434).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Siphoviridae; Lambdavirus.
OX   NCBI_TaxID=10712;
OH   NCBI_TaxID=562; Escherichia coli.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=375198; DOI=10.1093/nar/6.3.867;
RA   Grosschedl R., Schwarz E.;
RT   "Nucleotide sequence of the cro-cII-oop region of bacteriophage 434 DNA.";
RL   Nucleic Acids Res. 6:867-881(1979).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS).
RX   PubMed=2647998; DOI=10.1016/0022-2836(89)90374-4;
RA   Mondragon A., Wolberger C., Harrison S.C.;
RT   "Structure of phage 434 Cro protein at 2.35-A resolution.";
RL   J. Mol. Biol. 205:179-188(1989).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX   PubMed=2038059; DOI=10.1016/0022-2836(91)90568-q;
RA   Mondragon A., Harrison S.C.;
RT   "The phage 434 Cro/OR1 complex at 2.5-A resolution.";
RL   J. Mol. Biol. 219:321-334(1991).
RN   [4]
RP   STRUCTURE BY NMR.
RX   PubMed=9174359; DOI=10.1021/bi970085p;
RA   Padmanabhan S., Jimenez M.A., Gonzalez C., Sanz J.M., Gimenez-Gallego G.,
RA   Rico M.;
RT   "Three-dimensional solution structure and stability of phage 434 Cro
RT   protein.";
RL   Biochemistry 36:6424-6436(1997).
CC   -!- FUNCTION: Cro represses genes normally expressed in early phage
CC       development and is necessary for the late stage of lytic growth. It
CC       does this by binding to the OL and OR operators regions normally used
CC       by the repressor protein for lysogenic maintenance.
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DR   EMBL; V00635; CAA23908.1; -; Genomic_DNA.
DR   EMBL; J02460; AAA32245.1; -; Genomic_DNA.
DR   PIR; A03572; RCBP4.
DR   PDB; 1ZUG; NMR; -; A=1-71.
DR   PDB; 2CRO; X-ray; 2.35 A; A=1-71.
DR   PDB; 3CRO; X-ray; 2.50 A; L/R=1-71.
DR   PDBsum; 1ZUG; -.
DR   PDBsum; 2CRO; -.
DR   PDBsum; 3CRO; -.
DR   SMR; P03036; -.
DR   EvolutionaryTrace; P03036; -.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   CDD; cd00093; HTH_XRE; 1.
DR   Gene3D; 1.10.260.40; -; 1.
DR   InterPro; IPR000655; Cro.
DR   InterPro; IPR001387; Cro/C1-type_HTH.
DR   InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR   Pfam; PF01381; HTH_3; 1.
DR   PRINTS; PR00030; HTHCRO.
DR   SMART; SM00530; HTH_XRE; 1.
DR   SUPFAM; SSF47413; SSF47413; 1.
DR   PROSITE; PS50943; HTH_CROC1; 1.
PE   1: Evidence at protein level;
KW   3D-structure; DNA-binding; Early protein; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..71
FT                   /note="Regulatory protein cro"
FT                   /id="PRO_0000149707"
FT   DOMAIN          8..61
FT                   /note="HTH cro/C1-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00257"
FT   DNA_BIND        19..38
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00257"
FT   HELIX           4..14
FT                   /evidence="ECO:0007829|PDB:2CRO"
FT   HELIX           19..26
FT                   /evidence="ECO:0007829|PDB:2CRO"
FT   HELIX           30..37
FT                   /evidence="ECO:0007829|PDB:2CRO"
FT   HELIX           47..53
FT                   /evidence="ECO:0007829|PDB:2CRO"
FT   HELIX           58..63
FT                   /evidence="ECO:0007829|PDB:2CRO"
SQ   SEQUENCE   71 AA;  8063 MW;  8783051BDF6D0606 CRC64;
     MQTLSERLKK RRIALKMTQT ELATKAGVKQ QSIQLIEAGV TKRPRFLFEI AMALNCDPVW
     LQYGTKRGKA A