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 02-SEP-2026, entry version 153. 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; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; 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). 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 50 uM. 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 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_CP009789.1. 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 AlphaFoldDB; P0ACF0; -. DR SASBDB; P0ACF0; -. DR SMR; P0ACF0; -. DR BioGRID; 4263459; 248. DR BioGRID; 852793; 4. 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 FunCoup; P0ACF0; 680. DR IntAct; P0ACF0; 77. DR STRING; 511145.b4000; -. DR jPOST; P0ACF0; -. DR PaxDb; 511145-b4000; -. DR EnsemblBacteria; AAC76974; AAC76974; b4000. DR GeneID; 67175032; -. DR GeneID; 93777894; -. DR GeneID; 948499; -. DR KEGG; ecj:JW3964; -. DR KEGG; eco:b4000; -. DR KEGG; ecoc:C3026_21605; -. 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 OrthoDB; 9799835at2; -. DR PhylomeDB; P0ACF0; -. DR BioCyc; EcoCyc:EG10466-MONOMER; -. DR EvolutionaryTrace; P0ACF0; -. DR PRO; PR:P0ACF0; -. DR Proteomes; UP000000625; Chromosome. DR AbasyAtlas; P0ACF0; -. 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 DNA packaging; NAS:ComplexPortal. DR GO; GO:0006974; P:DNA damage response; IEP:EcoliWiki. 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; NF008023; PRK10753.1; 1. DR PANTHER; PTHR33175; DNA-BINDING PROTEIN HU; 1. DR PANTHER; PTHR33175:SF12; DNA-BINDING PROTEIN HU-ALPHA; 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. 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 //