DBH1_BACSU
ID DBH1_BACSU Reviewed; 92 AA.
AC P08821;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=DNA-binding protein HU 1;
DE AltName: Full=DNA-binding protein II;
DE AltName: Full=HB;
GN Name=hupA; Synonyms=dbpA, hbs, hbsU; OrderedLocusNames=BSU22790;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP PROTEIN SEQUENCE.
RC STRAIN=Globigii;
RX PubMed=3595600; DOI=10.1111/j.1432-1033.1987.tb11474.x;
RA Imber R., Kimura M., Groch N., Heinemann U.;
RT "DNA-binding properties and primary structure of HB protein from Bacillus
RT globigii.";
RL Eur. J. Biochem. 165:547-552(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1633819; DOI=10.1111/j.1432-1033.1992.tb17095.x;
RA Groch N., Schindelin H., Schollz A.S., Hahn U., Heinemann U.;
RT "Determination of DNA-binding parameters for the Bacillus subtilis histone-
RT like HBsu protein through introduction of fluorophores by site-directed
RT mutagenesis of a synthetic gene.";
RL Eur. J. Biochem. 207:677-685(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / JH642;
RX PubMed=1902464; DOI=10.1128/jb.173.10.3191-3198.1991;
RA Micka B., Groch N., Heinemann U., Marahiel M.A.;
RT "Molecular cloning, nucleotide sequence, and characterization of the
RT Bacillus subtilis gene encoding the DNA-binding protein HBsu.";
RL J. Bacteriol. 173:3191-3198(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Globigii;
RX PubMed=1644313; DOI=10.1016/0378-1119(92)90487-a;
RA Padas P.M., Wilson K.S., Vorgias C.E.;
RT "The DNA-binding protein HU from mesophilic and thermophilic bacilli: gene
RT cloning, overproduction and purification.";
RL Gene 117:39-44(1992).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [6]
RP PROTEIN SEQUENCE OF 1-11.
RX PubMed=8439548; DOI=10.1016/0167-4781(93)90275-i;
RA Le Hegarat F., Salti-Montesanto V., Hauck Y., Hirschbein L.;
RT "Purification and characterization of the HU-like protein HPB9 from the
RT Bacillus subtilis nucleoid.";
RL Biochim. Biophys. Acta 1172:101-107(1993).
RN [7]
RP PROTEIN SEQUENCE OF 42-53, INTERACTION WITH BACILLUS PHAGE SP01 GP46, AND
RP MUTAGENESIS OF ILE-71; LYS-80; LYS-83 AND LYS-86.
RX PubMed=35193978; DOI=10.1073/pnas.2116278119;
RA Zhang P., Zhao X., Wang Y., Du K., Wang Z., Yu J., Chang G., Matthews S.,
RA Wang H., Liu B.;
RT "Bacteriophage protein Gp46 is a cross-species inhibitor of nucleoid-
RT associated HU proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 119:0-0(2022).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-4, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=168;
RX PubMed=17218307; DOI=10.1074/mcp.m600464-mcp200;
RA Macek B., Mijakovic I., Olsen J.V., Gnad F., Kumar C., Jensen P.R.,
RA Mann M.;
RT "The serine/threonine/tyrosine phosphoproteome of the model bacterium
RT Bacillus subtilis.";
RL Mol. Cell. Proteomics 6:697-707(2007).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND DNA-BINDING.
RC STRAIN=168;
RX PubMed=21085634; DOI=10.1371/journal.pgen.1001207;
RA Smits W.K., Grossman A.D.;
RT "The transcriptional regulator Rok binds A+T-rich DNA and is involved in
RT repression of a mobile genetic element in Bacillus subtilis.";
RL PLoS Genet. 6:E1001207-E1001207(2010).
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. Binds evenly across chromosome, does not
CC display a preference for AT content (PubMed:21085634).
CC {ECO:0000269|PubMed:21085634}.
CC -!- SUBUNIT: Homodimer.
CC -!- SUBUNIT: (Microbial infection) Interacts with Bacillus phage SP01 Gp46;
CC the interaction replaces dsDNA from the hupA-DNA complex.
CC {ECO:0000269|PubMed:35193978}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, nucleoid
CC {ECO:0000269|PubMed:21085634}. Note=Evenly distributed in the nucleoid
CC (PubMed:21085634). {ECO:0000269|PubMed:21085634}.
CC -!- SIMILARITY: Belongs to the bacterial histone-like protein family.
CC {ECO:0000305}.
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DR EMBL; X66448; CAA47064.1; -; Genomic_DNA.
DR EMBL; X52418; CAA36669.1; -; Genomic_DNA.
DR EMBL; M73504; AAA22536.1; -; Genomic_DNA.
DR EMBL; M73503; AAA22535.1; -; Genomic_DNA.
DR EMBL; M80926; AAB59030.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14195.1; -; Genomic_DNA.
DR PIR; JC1208; JC1208.
DR PIR; S00015; S00015.
DR RefSeq; NP_390160.1; NC_000964.3.
DR RefSeq; WP_003153447.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P08821; -.
DR SMR; P08821; -.
DR IntAct; P08821; 1.
DR MINT; P08821; -.
DR STRING; 224308.BSU22790; -.
DR iPTMnet; P08821; -.
DR jPOST; P08821; -.
DR PaxDb; P08821; -.
DR PRIDE; P08821; -.
DR EnsemblBacteria; CAB14195; CAB14195; BSU_22790.
DR GeneID; 64304059; -.
DR GeneID; 66325938; -.
DR GeneID; 938995; -.
DR KEGG; bsu:BSU22790; -.
DR PATRIC; fig|224308.179.peg.2484; -.
DR eggNOG; COG0776; Bacteria.
DR InParanoid; P08821; -.
DR OMA; PAHEGIN; -.
DR PhylomeDB; P08821; -.
DR BioCyc; BSUB:BSU22790-MON; -.
DR PRO; PR:P08821; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0009295; C:nucleoid; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0030261; P:chromosome condensation; IEA:UniProtKB-KW.
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 Cytoplasm; Direct protein sequencing; DNA condensation; DNA-binding;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..92
FT /note="DNA-binding protein HU 1"
FT /id="PRO_0000104913"
FT MOD_RES 4
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:17218307"
FT MUTAGEN 71
FT /note="I->A: Weakens the interaction with Bacillus phage
FT SP01 Gp46."
FT /evidence="ECO:0000269|PubMed:35193978"
FT MUTAGEN 80
FT /note="K->Q: Disrupts interaction with Bacillus phage SP01
FT Gp46; when associated with Q-83 and Q-86."
FT /evidence="ECO:0000269|PubMed:35193978"
FT MUTAGEN 83
FT /note="K->Q: Disrupts interaction with Bacillus phage SP01
FT Gp46; when associated with Q-80 and Q-86."
FT /evidence="ECO:0000269|PubMed:35193978"
FT MUTAGEN 86
FT /note="K->Q: Disrupts interaction with Bacillus phage SP01
FT Gp46; when associated with Q-80 and Q-83."
FT /evidence="ECO:0000269|PubMed:35193978"
FT CONFLICT 40
FT /note="D -> K (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 92 AA; 9884 MW; 1372EE209687BD07 CRC64;
MNKTELINAV AEASELSKKD ATKAVDSVFD TILDALKNGD KIQLIGFGNF EVRERSARKG
RNPQTGEEIE IPASKVPAFK PGKALKDAVA GK
