ID   DBH_STRP3               Reviewed;          91 AA.
AC   P0DB64; P0A3I0; Q9XB23;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 1.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=DNA-binding protein HU;
GN   Name=hup; Synonyms=hlpA; OrderedLocusNames=SpyM3_1146;
OS   Streptococcus pyogenes serotype M3 (strain ATCC BAA-595 / MGAS315).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=198466;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-595 / MGAS315;
RX   PubMed=12122206; DOI=10.1073/pnas.152298499;
RA   Beres S.B., Sylva G.L., Barbian K.D., Lei B., Hoff J.S., Mammarella N.D.,
RA   Liu M.-Y., Smoot J.C., Porcella S.F., Parkins L.D., Campbell D.S.,
RA   Smith T.M., McCormick J.K., Leung D.Y.M., Schlievert P.M., Musser J.M.;
RT   "Genome sequence of a serotype M3 strain of group A Streptococcus: phage-
RT   encoded toxins, the high-virulence phenotype, and clone emergence.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:10078-10083(2002).
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. Seems also to act as a fortuitous virulence
CC       factor in delayed sequelae by binding to heparan sulfate-proteoglycans
CC       in the extracellular matrix of target organs and acting as a nidus for
CC       in situ immune complex formation (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the bacterial histone-like protein family.
CC       {ECO:0000305}.
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DR   EMBL; AE014074; AAM79753.1; -; Genomic_DNA.
DR   RefSeq; WP_002983920.1; NC_004070.1.
DR   AlphaFoldDB; P0DB64; -.
DR   SMR; P0DB64; -.
DR   EnsemblBacteria; AAM79753; AAM79753; SpyM3_1146.
DR   GeneID; 57852916; -.
DR   KEGG; spg:SpyM3_1146; -.
DR   HOGENOM; CLU_105066_3_1_9; -.
DR   OMA; PAHEGIN; -.
DR   Proteomes; UP000000564; 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   3: Inferred from homology;
KW   DNA condensation; DNA-binding; Virulence.
FT   CHAIN           1..91
FT                   /note="DNA-binding protein HU"
FT                   /id="PRO_0000104983"
SQ   SEQUENCE   91 AA;  9647 MW;  50C7119C6753BEF5 CRC64;
     MANKQDLIAK VAEATELTKK DSAAAVDAVF STIEAFLAEG EKVQLIGFGN FEVRERAARK
     GRNPQTGAEI EIAASKVPAF KAGKALKDAV K