DBHA_ECOLI
ID DBHA_ECOLI Reviewed; 90 AA.
AC P0ACF0; P02342; Q2M8T7;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=DNA-binding protein HU-alpha;
DE AltName: Full=HU-2;
DE AltName: Full=NS2;
GN Name=hupA; OrderedLocusNames=b4000, JW3964;
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=3312963; DOI=10.1007/bf00329674;
RA Kano Y., Osato K., Wada M., Imamoto F.;
RT "Cloning and sequencing of the HU-2 gene of Escherichia coli.";
RL Mol. Gen. Genet. 209:408-410(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8265357; DOI=10.1093/nar/21.23.5408;
RA Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.;
RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the region
RT from 89.2 to 92.8 minutes.";
RL Nucleic Acids Res. 21:5408-5417(1993).
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.
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 1-28.
RC STRAIN=K12;
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 1-35.
RA Nishimura K., Inokuchi H.;
RL Submitted (JUL-1992) 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 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 [14]
RP SUBCELLULAR LOCATION.
RC STRAIN=K12 / BW25993;
RX PubMed=21903814; DOI=10.1126/science.1204697;
RA Wang W., Li G.W., Chen C., Xie X.S., Zhuang X.;
RT "Chromosome organization by a nucleoid-associated protein in live
RT bacteria.";
RL Science 333:1445-1449(2011).
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 P0ACF0; P03004: dnaA; NbExp=5; IntAct=EBI-547648, EBI-548951;
CC P0ACF0; P0ACF0: hupA; NbExp=2; IntAct=EBI-547648, EBI-547648;
CC P0ACF0; P0ACF4: hupB; NbExp=9; IntAct=EBI-547648, EBI-370411;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, nucleoid
CC {ECO:0000269|PubMed:21903814}. Note=Scattered throughout the nucleoid
CC (PubMed:21903814). {ECO:0000269|PubMed:21903814}.
CC -!- SIMILARITY: Belongs to the bacterial histone-like protein family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X05994; CAA29412.1; -; Genomic_DNA.
DR EMBL; U00006; AAC43098.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76974.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77319.1; -; Genomic_DNA.
DR EMBL; X54555; CAA38426.1; -; Genomic_DNA.
DR EMBL; D12624; BAA02149.1; -; Genomic_DNA.
DR PIR; S06269; DNECS2.
DR RefSeq; NP_418428.1; NC_000913.3.
DR RefSeq; WP_001044513.1; NZ_STEB01000045.1.
DR PDB; 1MUL; X-ray; 2.30 A; A=1-90.
DR PDB; 2O97; X-ray; 2.45 A; A=1-90.
DR PDB; 4YEW; X-ray; 2.68 A; C=1-90.
DR PDB; 4YEX; X-ray; 3.20 A; A/C=1-90.
DR PDB; 4YEY; X-ray; 3.35 A; A/C=1-90.
DR PDB; 4YF0; X-ray; 2.79 A; A/B=1-90.
DR PDB; 4YFH; X-ray; 3.49 A; A/B=1-90.
DR PDB; 4YFT; X-ray; 2.91 A; C=1-90.
DR PDB; 6O6K; X-ray; 3.60 A; A/B=1-90.
DR PDB; 6O8Q; X-ray; 3.22 A; A/B/C/D/E/F/G/H/I/J=1-90.
DR PDB; 6OAJ; X-ray; 4.09 A; A/B/C/D=1-90.
DR PDBsum; 1MUL; -.
DR PDBsum; 2O97; -.
DR PDBsum; 4YEW; -.
DR PDBsum; 4YEX; -.
DR PDBsum; 4YEY; -.
DR PDBsum; 4YF0; -.
DR PDBsum; 4YFH; -.
DR PDBsum; 4YFT; -.
DR PDBsum; 6O6K; -.
DR PDBsum; 6O8Q; -.
DR PDBsum; 6OAJ; -.
DR AlphaFoldDB; P0ACF0; -.
DR SASBDB; P0ACF0; -.
DR SMR; P0ACF0; -.
DR BioGRID; 4263459; 132.
DR ComplexPortal; CPX-1958; HU complex, variant hupAB.
DR ComplexPortal; CPX-1959; HU complex, variant hupA.
DR ComplexPortal; CPX-1961; DnaA-HU complex, variant hupAB.
DR ComplexPortal; CPX-1962; DnaA-HU complex, variant hupA.
DR DIP; DIP-35892N; -.
DR IntAct; P0ACF0; 77.
DR STRING; 511145.b4000; -.
DR jPOST; P0ACF0; -.
DR PaxDb; P0ACF0; -.
DR PRIDE; P0ACF0; -.
DR EnsemblBacteria; AAC76974; AAC76974; b4000.
DR EnsemblBacteria; BAE77319; BAE77319; BAE77319.
DR GeneID; 67415298; -.
DR GeneID; 948499; -.
DR KEGG; ecj:JW3964; -.
DR KEGG; eco:b4000; -.
DR PATRIC; fig|1411691.4.peg.2711; -.
DR EchoBASE; EB0461; -.
DR eggNOG; COG0776; Bacteria.
DR HOGENOM; CLU_105066_3_1_6; -.
DR InParanoid; P0ACF0; -.
DR OMA; ISQEKQC; -.
DR PhylomeDB; P0ACF0; -.
DR BioCyc; EcoCyc:EG10466-MON; -.
DR EvolutionaryTrace; P0ACF0; -.
DR PRO; PR:P0ACF0; -.
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; IDA:CACAO.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:EcoliWiki.
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:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
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; Cytoplasm; Direct protein sequencing; DNA condensation;
KW DNA-binding; Reference proteome.
FT CHAIN 1..90
FT /note="DNA-binding protein HU-alpha"
FT /id="PRO_0000104935"
FT CONFLICT 19..32
FT /note="TQAKAALESTLAAI -> AAAGRALDAIIASV (in Ref. 7; AA
FT sequence)"
FT /evidence="ECO:0000305"
FT HELIX 3..13
FT /evidence="ECO:0007829|PDB:1MUL"
FT HELIX 18..37
FT /evidence="ECO:0007829|PDB:1MUL"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:1MUL"
FT TURN 45..47
FT /evidence="ECO:0007829|PDB:1MUL"
FT STRAND 48..55
FT /evidence="ECO:0007829|PDB:1MUL"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:6O8Q"
FT TURN 63..66
FT /evidence="ECO:0007829|PDB:6O8Q"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:6O8Q"
FT STRAND 74..81
FT /evidence="ECO:0007829|PDB:1MUL"
FT HELIX 83..89
FT /evidence="ECO:0007829|PDB:1MUL"
SQ SEQUENCE 90 AA; 9535 MW; 6B5B8536FDBD13DC CRC64;
MNKTQLIDVI AEKAELSKTQ AKAALESTLA AITESLKEGD AVQLVGFGTF KVNHRAERTG
RNPQTGKEIK IAAANVPAFV SGKALKDAVK
