ID   DBH_STRMU               Reviewed;          91 AA.
AC   Q9XB21;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=DNA-binding protein HU;
GN   Name=hup; Synonyms=hlpA; OrderedLocusNames=SMU_589;
OS   Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=210007;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9423866; DOI=10.1128/iai.66.1.259-265.1998;
RA   Stinson M.W., McLaughlin R., Choi S.H., Juarez Z.E., Barnard J.;
RT   "Streptococcal histone-like protein: primary structure of hlpA and protein
RT   binding to lipoteichoic acid and epithelial cells.";
RL   Infect. Immun. 66:259-265(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700610 / UA159;
RX   PubMed=12397186; DOI=10.1073/pnas.172501299;
RA   Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA   Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA   Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT   "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT   pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(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.
CC   -!- SIMILARITY: Belongs to the bacterial histone-like protein family.
CC       {ECO:0000305}.
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DR   EMBL; L40355; AAD40810.1; -; Genomic_DNA.
DR   EMBL; AE014133; AAN58328.1; -; Genomic_DNA.
DR   RefSeq; NP_721022.1; NC_004350.2.
DR   RefSeq; WP_002262099.1; NC_004350.2.
DR   PDB; 5FBM; X-ray; 1.90 A; A/B=1-91.
DR   PDBsum; 5FBM; -.
DR   AlphaFoldDB; Q9XB21; -.
DR   SMR; Q9XB21; -.
DR   STRING; 210007.SMU_589; -.
DR   PRIDE; Q9XB21; -.
DR   EnsemblBacteria; AAN58328; AAN58328; SMU_589.
DR   GeneID; 66817942; -.
DR   KEGG; smu:SMU_589; -.
DR   PATRIC; fig|210007.7.peg.522; -.
DR   eggNOG; COG0776; Bacteria.
DR   HOGENOM; CLU_105066_3_1_9; -.
DR   OMA; PAHEGIN; -.
DR   PhylomeDB; Q9XB21; -.
DR   Proteomes; UP000002512; 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; Virulence.
FT   CHAIN           1..91
FT                   /note="DNA-binding protein HU"
FT                   /id="PRO_0000104980"
FT   HELIX           4..15
FT                   /evidence="ECO:0007829|PDB:5FBM"
FT   HELIX           19..38
FT                   /evidence="ECO:0007829|PDB:5FBM"
FT   STRAND          43..45
FT                   /evidence="ECO:0007829|PDB:5FBM"
FT   TURN            46..48
FT                   /evidence="ECO:0007829|PDB:5FBM"
FT   STRAND          49..56
FT                   /evidence="ECO:0007829|PDB:5FBM"
FT   STRAND          75..82
FT                   /evidence="ECO:0007829|PDB:5FBM"
FT   HELIX           84..91
FT                   /evidence="ECO:0007829|PDB:5FBM"
SQ   SEQUENCE   91 AA;  9706 MW;  F3870AF616FA14FA CRC64;
     MANKQDLIAK VAEATELTKK DSAAAVDAVF SAVSSYLAKG EKVQLIGFGN FEVRERAARK
     GRNPQTGEEI KIKASKVPAF KAGKALKDAV K