DBH_BORBU
ID DBH_BORBU Reviewed; 108 AA.
AC Q57267; Q44834; Q44835; Q44836; Q44837; Q44838; Q44839; Q57030; Q57056;
AC Q57402;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=DNA-binding protein HU;
DE AltName: Full=HBbu;
GN Name=hup; Synonyms=hbb; OrderedLocusNames=BB_0232;
OS Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS (Borrelia burgdorferi).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX NCBI_TaxID=224326;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8451174; DOI=10.1093/nar/21.4.1040;
RA Tilly K., Campbell J.;
RT "A Borrelia burgdorferi homolog of the Escherichia coli rho gene.";
RL Nucleic Acids Res. 21:1040-1040(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=25015, A44S, CA128, CA2, CA55, DN127, NY13-87, POTIB1, POTIB2,
RC POTIB3, UK, and VS116;
RX PubMed=8995795; DOI=10.1099/00207713-47-1-1;
RA Valsangiacomo C., Balmelli T., Piffaretti J.C.;
RT "A phylogenetic analysis of Borrelia burgdorferi sensu lato based on
RT sequence information from the hbb gene, coding for a histone-like
RT protein.";
RL Int. J. Syst. Bacteriol. 47:1-10(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX PubMed=9403685; DOI=10.1038/37551;
RA Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA Smith H.O., Venter J.C.;
RT "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL Nature 390:580-586(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. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the bacterial histone-like protein family.
CC {ECO:0000305}.
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DR EMBL; U35673; AAB41461.1; -; Genomic_DNA.
DR EMBL; U48648; AAC73070.1; -; Genomic_DNA.
DR EMBL; U48649; AAC73071.1; -; Genomic_DNA.
DR EMBL; U48650; AAC73072.1; -; Genomic_DNA.
DR EMBL; U48651; AAC73073.1; -; Genomic_DNA.
DR EMBL; U48652; AAC73074.1; -; Genomic_DNA.
DR EMBL; U48653; AAC73075.1; -; Genomic_DNA.
DR EMBL; U48654; AAC73076.1; -; Genomic_DNA.
DR EMBL; U48663; AAC73085.1; -; Genomic_DNA.
DR EMBL; U48665; AAC73087.1; -; Genomic_DNA.
DR EMBL; U48666; AAC73088.1; -; Genomic_DNA.
DR EMBL; U48667; AAC73089.1; -; Genomic_DNA.
DR EMBL; U48668; AAC73090.1; -; Genomic_DNA.
DR EMBL; U48669; AAC73091.1; -; Genomic_DNA.
DR EMBL; U48670; AAC73092.1; -; Genomic_DNA.
DR EMBL; U48683; AAC73105.1; -; Genomic_DNA.
DR EMBL; U48684; AAC73106.1; -; Genomic_DNA.
DR EMBL; U48685; AAC73107.1; -; Genomic_DNA.
DR EMBL; AE000783; AAC66617.1; -; Genomic_DNA.
DR PIR; H70128; H70128.
DR RefSeq; NP_212366.1; NC_001318.1.
DR RefSeq; WP_002655986.1; NC_001318.1.
DR PDB; 2NP2; X-ray; 3.02 A; A/B=1-108.
DR PDBsum; 2NP2; -.
DR AlphaFoldDB; Q57267; -.
DR SMR; Q57267; -.
DR STRING; 224326.BB_0232; -.
DR EnsemblBacteria; AAC66617; AAC66617; BB_0232.
DR KEGG; bbu:BB_0232; -.
DR PATRIC; fig|224326.49.peg.631; -.
DR HOGENOM; CLU_105066_2_0_12; -.
DR OMA; PAHEGIN; -.
DR EvolutionaryTrace; Q57267; -.
DR Proteomes; UP000001807; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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 3D-structure; DNA condensation; DNA-binding; Reference proteome.
FT CHAIN 1..108
FT /note="DNA-binding protein HU"
FT /id="PRO_0000104917"
FT VARIANT 4
FT /note="S -> P (in strain: UK and VS116)"
FT VARIANT 9
FT /note="V -> I (in strain: UK and VS116)"
FT VARIANT 14..16
FT /note="IVD -> VVN (in strain: POTIB1, POTIB2 and POTIB3)"
FT VARIANT 19
FT /note="S -> A (in strain: A44S and NY13-87)"
FT VARIANT 23
FT /note="K -> R (in strain: 25015, CA2, CA55, CA128, DN127,
FT POTIB1, POTIB2, POTIB3, UK and VS116)"
FT VARIANT 33
FT /note="Y -> C (in strain: CA55, CA128 and DN127)"
FT VARIANT 65
FT /note="V -> L (in strain: 25015)"
FT VARIANT 69
FT /note="K -> R (in strain: DN127)"
FT VARIANT 81
FT /note="E -> V (in strain: NY13-87)"
FT STRAND 8..10
FT /evidence="ECO:0007829|PDB:2NP2"
FT HELIX 11..24
FT /evidence="ECO:0007829|PDB:2NP2"
FT HELIX 31..50
FT /evidence="ECO:0007829|PDB:2NP2"
FT STRAND 54..57
FT /evidence="ECO:0007829|PDB:2NP2"
FT TURN 58..60
FT /evidence="ECO:0007829|PDB:2NP2"
FT STRAND 61..68
FT /evidence="ECO:0007829|PDB:2NP2"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:2NP2"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:2NP2"
FT STRAND 88..95
FT /evidence="ECO:0007829|PDB:2NP2"
FT HELIX 97..104
FT /evidence="ECO:0007829|PDB:2NP2"
SQ SEQUENCE 108 AA; 12686 MW; 0CEF9A092B24BED9 CRC64;
MSFSRRPKVT KSDIVDQISL NIKNNNLKLE KKYIRLVIDA FFEELKSNLC SNNVIEFRSF
GTFEVRKRKG RLNARNPQTG EYVKVLDHHV AYFRPGKDLK ERVWGIKG
