DBHB_ECOLI
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 03-AUG-2022, entry version 132.
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; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC 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.
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).
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.
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_STEB01000007.1.
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 PDBsum; 2O97; -.
DR PDBsum; 4P3V; -.
DR PDBsum; 4YEW; -.
DR PDBsum; 4YFT; -.
DR AlphaFoldDB; P0ACF4; -.
DR BMRB; P0ACF4; -.
DR SMR; P0ACF4; -.
DR BioGRID; 4260733; 44.
DR BioGRID; 853335; 1.
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 IntAct; P0ACF4; 77.
DR STRING; 511145.b0440; -.
DR jPOST; P0ACF4; -.
DR PaxDb; P0ACF4; -.
DR PRIDE; P0ACF4; -.
DR EnsemblBacteria; AAC73543; AAC73543; b0440.
DR EnsemblBacteria; BAE76220; BAE76220; BAE76220.
DR GeneID; 67416485; -.
DR GeneID; 949095; -.
DR KEGG; ecj:JW0430; -.
DR KEGG; eco:b0440; -.
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; PAHEGIN; -.
DR PhylomeDB; P0ACF4; -.
DR BioCyc; EcoCyc:EG10467-MON; -.
DR EvolutionaryTrace; P0ACF4; -.
DR PRO; PR:P0ACF4; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
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:UniProtKB-KW.
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 packaging; IC:ComplexPortal.
DR GO; GO:0030261; P:chromosome condensation; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IC:ComplexPortal.
DR GO; GO:0006270; P:DNA replication initiation; IDA:ComplexPortal.
DR GO; GO:0006351; P:transcription, DNA-templated; IDA:EcoCyc.
DR Gene3D; 4.10.520.10; -; 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 PANTHER; PTHR33175; PTHR33175; 1.
DR Pfam; PF00216; Bac_DNA_binding; 1.
DR PRINTS; PR01727; DNABINDINGHU.
DR SMART; SM00411; BHL; 1.
DR SUPFAM; SSF47729; SSF47729; 1.
DR PROSITE; PS00045; HISTONE_LIKE; 1.
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
