ID   CNU_ECOLI               Reviewed;          71 AA.
AC   P64467; P76179; Q2MB72; Q5VJ24;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=OriC-binding nucleoid-associated protein;
DE   AltName: Full=H-NS/StpA-binding protein 2;
DE   AltName: Full=Transcription modulator YdgT;
GN   Name=cnu {ECO:0000303|PubMed:16199570}; Synonyms=ydgT;
GN   OrderedLocusNames=b1625, JW1617;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN BINDING TO ORIC, AND
RP   SUBUNIT.
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=16199570; DOI=10.1128/jb.187.20.6998-7008.2005;
RA   Kim M.S., Bae S.-H., Yun S.H., Lee H.J., Ji S.C., Lee J.H., Srivastava P.,
RA   Lee S.-H., Chae H., Lee Y., Choi B.-S., Chattoraj D.K., Lim H.M.;
RT   "Cnu, a novel oriC-binding protein of Escherichia coli.";
RL   J. Bacteriol. 187:6998-7008(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [4]
RP   PRELIMINARY FUNCTION, AND SUBUNIT.
RX   PubMed=15458420; DOI=10.1111/j.1365-2958.2004.04268.x;
RA   Paytubi S., Madrid C., Forns N., Nieto J.M., Balsalobre C., Uhlin B.E.,
RA   Juarez A.;
RT   "YdgT, the Hha paralogue in Escherichia coli, forms heteromeric complexes
RT   with H-NS and StpA.";
RL   Mol. Microbiol. 54:251-263(2004).
RN   [5]
RP   INTERACTION WITH H-NS, AND MUTAGENESIS OF ASP-44.
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=21600204; DOI=10.1016/j.febslet.2011.05.024;
RA   de Alba C.F., Solorzano C., Paytubi S., Madrid C., Juarez A., Garcia J.,
RA   Pons M.;
RT   "Essential residues in the H-NS binding site of Hha, a co-regulator of
RT   horizontally acquired genes in Enterobacteria.";
RL   FEBS Lett. 585:1765-1770(2011).
RN   [6]
RP   FUNCTION, REGULON, AND DISRUPTION PHENOTYPE.
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=23543115; DOI=10.1093/dnares/dst008;
RA   Ueda T., Takahashi H., Uyar E., Ishikawa S., Ogasawara N., Oshima T.;
RT   "Functions of the Hha and YdgT proteins in transcriptional silencing by the
RT   nucleoid proteins, H-NS and StpA, in Escherichia coli.";
RL   DNA Res. 20:263-271(2013).
CC   -!- FUNCTION: Modifies the set of genes regulated by H-NS; Hha and Cnu
CC       (YdgT) increase the number of genes bound by H-NS/StpA and may also
CC       modulate the oligomerization of the H-NS/StpA-complex on DNA
CC       (PubMed:23543115). The complex formed with H-NS binds to the specific
CC       26-bp cnb site in the origin of replication oriC (PubMed:16199570). Can
CC       complement, at least partially, the absence of the Hha protein in hha
CC       mutants. {ECO:0000269|PubMed:16199570, ECO:0000269|PubMed:23543115}.
CC   -!- SUBUNIT: Forms complexes with both H-NS and StpA.
CC       {ECO:0000269|PubMed:15458420, ECO:0000269|PubMed:16199570,
CC       ECO:0000269|PubMed:21600204}.
CC   -!- INTERACTION:
CC       P64467; P0ACF8: hns; NbExp=3; IntAct=EBI-551907, EBI-544934;
CC   -!- DISRUPTION PHENOTYPE: At 0.3 M NaCl up-regulation of 1 gene and down-
CC       regulation of 6 genes was observed; a double cnu-hha deletion up-
CC       regulated 134 and down-regulated 5 genes, most of which are thought to
CC       have been acquired horizontally and are also up-regulated in double
CC       hns-stpA deletions (PubMed:23543115). {ECO:0000269|PubMed:23543115}.
CC   -!- MISCELLANEOUS: Expression becomes maximal as cells enter the stationary
CC       phase but decreases later in the stationary phase.
CC   -!- SIMILARITY: Belongs to the Hha/YmoA/Cnu family. {ECO:0000305}.
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DR   EMBL; AY442175; AAS07631.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC74697.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76484.1; -; Genomic_DNA.
DR   PIR; C64919; C64919.
DR   RefSeq; NP_416142.1; NC_000913.3.
DR   RefSeq; WP_000217950.1; NZ_STEB01000003.1.
DR   PDB; 2JQT; NMR; -; A=1-71.
DR   PDBsum; 2JQT; -.
DR   AlphaFoldDB; P64467; -.
DR   SMR; P64467; -.
DR   BioGRID; 4259630; 18.
DR   ComplexPortal; CPX-1980; H-NS-Cnu transcription factor complex.
DR   DIP; DIP-48011N; -.
DR   IntAct; P64467; 3.
DR   MINT; P64467; -.
DR   STRING; 511145.b1625; -.
DR   jPOST; P64467; -.
DR   PaxDb; P64467; -.
DR   PRIDE; P64467; -.
DR   EnsemblBacteria; AAC74697; AAC74697; b1625.
DR   EnsemblBacteria; BAE76484; BAE76484; BAE76484.
DR   GeneID; 66674483; -.
DR   GeneID; 946152; -.
DR   KEGG; ecj:JW1617; -.
DR   KEGG; eco:b1625; -.
DR   PATRIC; fig|1411691.4.peg.636; -.
DR   EchoBASE; EB4050; -.
DR   eggNOG; ENOG5032S5U; Bacteria.
DR   HOGENOM; CLU_190629_0_0_6; -.
DR   OMA; PKSVWHF; -.
DR   PhylomeDB; P64467; -.
DR   BioCyc; EcoCyc:G6869-MON; -.
DR   EvolutionaryTrace; P64467; -.
DR   PRO; PR:P64467; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0036411; C:H-NS-Cnu complex; IPI:ComplexPortal.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:1900232; P:negative regulation of single-species biofilm formation on inanimate substrate; IMP:EcoCyc.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IC:ComplexPortal.
DR   GO; GO:0060566; P:positive regulation of DNA-templated transcription, termination; IMP:EcoCyc.
DR   Gene3D; 1.20.1280.40; -; 1.
DR   InterPro; IPR007985; Hemolysn_expr_modulating_HHA.
DR   InterPro; IPR036666; HHA_sf.
DR   Pfam; PF05321; HHA; 1.
DR   SUPFAM; SSF68989; SSF68989; 1.
PE   1: Evidence at protein level;
KW   3D-structure; DNA-binding; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..71
FT                   /note="OriC-binding nucleoid-associated protein"
FT                   /id="PRO_0000201733"
FT   SITE            44
FT                   /note="Interacts with H-NS"
FT   MUTAGEN         44
FT                   /note="D->N: Abolishes heterocomplex formation with H-NS."
FT                   /evidence="ECO:0000269|PubMed:21600204"
FT   HELIX           7..12
FT                   /evidence="ECO:0007829|PDB:2JQT"
FT   HELIX           17..29
FT                   /evidence="ECO:0007829|PDB:2JQT"
FT   HELIX           33..51
FT                   /evidence="ECO:0007829|PDB:2JQT"
SQ   SEQUENCE   71 AA;  8417 MW;  CE9FF2E890E78219 CRC64;
     MTVQDYLLKF RKISSLESLE KLYDHLNYTL TDDQELINMY RAADHRRAEL VSGGRLFDLG
     QVPKSVWHYV Q