ID   DBHB_ECOLI              Reviewed;          90 AA.
AC   P0ACF4; P02341; Q2MBY6;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   02-SEP-2026, entry version 150.
DE   RecName: Full=DNA-binding protein HU-beta;
DE   AltName: Full=HU-1;
DE   AltName: Full=NS1;
GN   Name=hupB; Synonyms=hopD; OrderedLocusNames=b0440, JW0430;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RX   PubMed=3003540; DOI=10.1007/bf00425687;
RA   Kano Y., Yoshimno S., Wada M., Yokoyama K., Nobuhara M., Imamoto F.;
RT   "Molecular cloning and nucleotide sequence of the HU-1 gene of Escherichia
RT   coli.";
RL   Mol. Gen. Genet. 201:360-362(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RA   Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA   Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA   Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT   "Sequence of minutes 4-25 of Escherichia coli.";
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
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   [4]
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   [5]
RP   PROTEIN SEQUENCE.
RX   PubMed=215461; DOI=10.1016/0014-5793(78)80446-3;
RA   Mende L., Timm B., Subramanian A.R.;
RT   "Primary structures of two homologous ribosome-associated DNA-binding
RT   proteins of Escherichia coli.";
RL   FEBS Lett. 96:395-398(1978).
RN   [6]
RP   PROTEIN SEQUENCE.
RX   PubMed=6987059; DOI=10.1111/j.1432-1033.1980.tb05968.x;
RA   Laine B., Kmiecik D., Sautiere P., Biserte G., Cohen-Solal M.;
RT   "Complete amino-acid sequences of DNA-binding proteins HU-1 and HU-2 from
RT   Escherichia coli.";
RL   Eur. J. Biochem. 103:447-461(1980).
RN   [7]
RP   PROTEIN SEQUENCE OF 1-37 AND 80-90.
RX   PubMed=350619; DOI=10.1016/0014-5793(78)80535-3;
RA   Laine B., Sautiere P., Biserte G., Cohen-Solal M., Gros F.,
RA   Rouviere-Yaniv J.;
RT   "The amino- and carboxy-terminal amino acid sequences of protein HU from
RT   Escherichia coli.";
RL   FEBS Lett. 89:116-120(1978).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-23.
RX   PubMed=2187099; DOI=10.1016/s0022-2836(05)80119-6;
RA   Kohno K., Wada M., Kano Y., Imamoto F.;
RT   "Promoters and autogenous control of the Escherichia coli hupA and hupB
RT   genes.";
RL   J. Mol. Biol. 213:27-36(1990).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 37-90.
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA   Hatada E., Ohmori H., Qiao Y., Tsuji M., Fukuda R.;
RL   Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
RN   [10]
RP   PROTEIN SEQUENCE OF 1-12.
RC   STRAIN=K12 / EMG2;
RX   PubMed=9298646; DOI=10.1002/elps.1150180807;
RA   Link A.J., Robison K., Church G.M.;
RT   "Comparing the predicted and observed properties of proteins encoded in the
RT   genome of Escherichia coli K-12.";
RL   Electrophoresis 18:1259-1313(1997).
RN   [11]
RP   PROTEIN SEQUENCE OF 1-10.
RC   STRAIN=K12;
RX   PubMed=9868784; DOI=10.1111/j.1574-6968.1998.tb13343.x;
RA   Wasinger V.C., Humphery-Smith I.;
RT   "Small genes/gene-products in Escherichia coli K-12.";
RL   FEMS Microbiol. Lett. 169:375-382(1998).
RN   [12]
RP   SUBUNIT.
RC   STRAIN=K12 / W3350 / ATCC 27020;
RX   PubMed=227733; DOI=10.1016/0014-5793(79)80518-9;
RA   Rouviere-Yaniv J., Kjeldgaard N.O.;
RT   "Native Escherichia coli HU protein is a heterotypic dimer.";
RL   FEBS Lett. 106:297-300(1979).
RN   [13]
RP   MUTAGENESIS OF ALA-30; LYS-37; PHE-47 AND 58-ARG--ARG-61.
RX   PubMed=2265752; DOI=10.1016/0378-1119(90)90355-u;
RA   Goshima N., Kohno K., Imamoto F., Kano Y.;
RT   "HU-1 mutants of Escherichia coli deficient in DNA binding.";
RL   Gene 96:141-145(1990).
RN   [14]
RP   IDENTIFICATION BY 2D-GEL.
RX   PubMed=9298644; DOI=10.1002/elps.1150180805;
RA   VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT   "Escherichia coli proteome analysis using the gene-protein database.";
RL   Electrophoresis 18:1243-1251(1997).
RN   [15]
RP   FUNCTION, ACTIVITY REGULATION, AND DNA-BINDING.
RX   PubMed=24916461; DOI=10.1038/ncomms5124;
RA   Bhowmick T., Ghosh S., Dixit K., Ganesan V., Ramagopal U.A., Dey D.,
RA   Sarma S.P., Ramakumar S., Nagaraja V.;
RT   "Targeting Mycobacterium tuberculosis nucleoid-associated protein HU with
RT   structure-based inhibitors.";
RL   Nat. Commun. 5:4124-4124(2014).
CC   -!- FUNCTION: Histone-like DNA-binding protein which is capable of wrapping
CC       DNA to stabilize it, and thus to prevent its denaturation under extreme
CC       environmental conditions. {ECO:0000305|PubMed:24916461}.
CC   -!- ACTIVITY REGULATION: Trans-stilbene derivative 4,4'-[(E)-ethene-1,2
CC       diylbis({5[(phenylcarbonyl)amino]benzene-2,1-diyl}sulfonylimino)]
CC       dibenzoic acid (SD1) inhibits DNA binding at 50uM. However SD1 did not
CC       inhibit growth in a range of 3-1600 uM. {ECO:0000269|PubMed:24916461}.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta chain.
CC       {ECO:0000269|PubMed:227733}.
CC   -!- INTERACTION:
CC       P0ACF4; P0ACF0: hupA; NbExp=9; IntAct=EBI-370411, EBI-547648;
CC       P0ACF4; P0ACF4: hupB; NbExp=2; IntAct=EBI-370411, EBI-370411;
CC   -!- SIMILARITY: Belongs to the bacterial histone-like protein family.
CC       {ECO:0000305}.
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DR   EMBL; X16540; CAA34539.1; -; Genomic_DNA.
DR   EMBL; U82664; AAB40196.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC73543.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76220.1; -; Genomic_DNA.
DR   EMBL; X53241; CAA37332.1; -; Genomic_DNA.
DR   EMBL; D82943; BAA11644.1; -; Genomic_DNA.
DR   PIR; S06880; DNECS1.
DR   RefSeq; NP_414974.1; NC_000913.3.
DR   RefSeq; WP_001043542.1; NZ_CP010438.1.
DR   PDB; 2O97; X-ray; 2.45 A; B=1-90.
DR   PDB; 4P3V; X-ray; 1.25 A; A=1-90.
DR   PDB; 4YEW; X-ray; 2.68 A; A=1-90.
DR   PDB; 4YFT; X-ray; 2.91 A; A=1-90.
DR   AlphaFoldDB; P0ACF4; -.
DR   BMRB; P0ACF4; -.
DR   SMR; P0ACF4; -.
DR   BioGRID; 4260733; 156.
DR   BioGRID; 853335; 4.
DR   ComplexPortal; CPX-1958; HU complex, variant hupAB.
DR   ComplexPortal; CPX-1960; HU complex variant 2.
DR   ComplexPortal; CPX-1961; DnaA-HU complex, variant hupAB.
DR   DIP; DIP-31833N; -.
DR   FunCoup; P0ACF4; 599.
DR   IntAct; P0ACF4; 77.
DR   STRING; 511145.b0440; -.
DR   jPOST; P0ACF4; -.
DR   PaxDb; 511145-b0440; -.
DR   EnsemblBacteria; AAC73543; AAC73543; b0440.
DR   GeneID; 86945354; -.
DR   GeneID; 949095; -.
DR   KEGG; ecj:JW0430; -.
DR   KEGG; eco:b0440; -.
DR   KEGG; ecoc:C3026_02155; -.
DR   PATRIC; fig|1411691.4.peg.1836; -.
DR   EchoBASE; EB0462; -.
DR   eggNOG; COG0776; Bacteria.
DR   HOGENOM; CLU_105066_3_2_6; -.
DR   InParanoid; P0ACF4; -.
DR   OMA; AFSAGKM; -.
DR   OrthoDB; 9799835at2; -.
DR   PhylomeDB; P0ACF4; -.
DR   BioCyc; EcoCyc:EG10467-MONOMER; -.
DR   EvolutionaryTrace; P0ACF4; -.
DR   PRO; PR:P0ACF4; -.
DR   Proteomes; UP000000625; Chromosome.
DR   AbasyAtlas; P0ACF4; -.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:1990103; C:DnaA-HU complex; IPI:ComplexPortal.
DR   GO; GO:1990178; C:HU-DNA complex; IPI:ComplexPortal.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR   GO; GO:0036386; P:bacterial nucleoid DNA packaging; NAS:ComplexPortal.
DR   GO; GO:0006281; P:DNA repair; NAS:ComplexPortal.
DR   GO; GO:0006270; P:DNA replication initiation; IDA:ComplexPortal.
DR   GO; GO:0006351; P:DNA-templated transcription; IDA:EcoCyc.
DR   CDD; cd13831; HU; 1.
DR   FunFam; 4.10.520.10:FF:000001; DNA-binding protein HU; 1.
DR   Gene3D; 4.10.520.10; IHF-like DNA-binding proteins; 1.
DR   InterPro; IPR000119; Hist_DNA-bd.
DR   InterPro; IPR020816; Histone-like_DNA-bd_CS.
DR   InterPro; IPR010992; IHF-like_DNA-bd_dom_sf.
DR   NCBIfam; NF007945; PRK10664.1; 1.
DR   PANTHER; PTHR33175; DNA-BINDING PROTEIN HU; 1.
DR   PANTHER; PTHR33175:SF3; DNA-BINDING PROTEIN HU-BETA; 1.
DR   Pfam; PF00216; Bac_DNA_binding; 1.
DR   PRINTS; PR01727; DNABINDINGHU.
DR   SMART; SM00411; BHL; 1.
DR   SUPFAM; SSF47729; IHF-like DNA-binding proteins; 1.
DR   PROSITE; PS00045; HISTONE_LIKE; 1.
DR   PDBsum; 2O97; -.
DR   PDBsum; 4P3V; -.
DR   PDBsum; 4YEW; -.
DR   PDBsum; 4YFT; -.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; DNA condensation; DNA-binding;
KW   Reference proteome.
FT   CHAIN           1..90
FT                   /note="DNA-binding protein HU-beta"
FT                   /id="PRO_0000104939"
FT   MUTAGEN         30
FT                   /note="A->D: No effect."
FT                   /evidence="ECO:0000269|PubMed:2265752"
FT   MUTAGEN         37
FT                   /note="K->Q: No effect."
FT                   /evidence="ECO:0000269|PubMed:2265752"
FT   MUTAGEN         47
FT                   /note="F->T: Reduced DNA-binding."
FT                   /evidence="ECO:0000269|PubMed:2265752"
FT   MUTAGEN         58..61
FT                   /note="RTGR->GTGG: Reduced DNA-binding."
FT                   /evidence="ECO:0000269|PubMed:2265752"
FT   CONFLICT        12
FT                   /note="A -> E (in Ref. 7; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        16
FT                   /note="I -> L (in Ref. 7; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        26
FT                   /note="D -> E (in Ref. 7; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   HELIX           3..14
FT                   /evidence="ECO:0007829|PDB:4P3V"
FT   HELIX           18..37
FT                   /evidence="ECO:0007829|PDB:4P3V"
FT   STRAND          42..44
FT                   /evidence="ECO:0007829|PDB:4P3V"
FT   TURN            45..47
FT                   /evidence="ECO:0007829|PDB:4P3V"
FT   STRAND          48..54
FT                   /evidence="ECO:0007829|PDB:4P3V"
FT   STRAND          75..81
FT                   /evidence="ECO:0007829|PDB:4P3V"
FT   HELIX           83..88
FT                   /evidence="ECO:0007829|PDB:4P3V"
SQ   SEQUENCE   90 AA;  9226 MW;  C56A3C766D53BB96 CRC64;
     MNKSQLIDKI AAGADISKAA AGRALDAIIA SVTESLKEGD DVALVGFGTF AVKERAARTG
     RNPQTGKEIT IAAAKVPSFR AGKALKDAVN
//