DBH_MYCLE
ID DBH_MYCLE Reviewed; 200 AA.
AC O33125;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=DNA-binding protein HU homolog;
DE AltName: Full=21 kDa laminin-2-binding protein;
DE AltName: Full=Histone-like protein;
DE Short=Hlp;
GN Name=hup; Synonyms=hlp, lbp21; OrderedLocusNames=ML1683;
GN ORFNames=MLCB637.34;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10449784; DOI=10.1073/pnas.96.17.9857;
RA Shimoji Y., Ng V., Matsumura K., Fischetti V.A., Rambukkana A.;
RT "A 21-kDa surface protein of Mycobacterium leprae binds peripheral nerve
RT laminin-2 and mediates Schwann cell invasion.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:9857-9862(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
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 -!- SUBUNIT: Binds to laminin-2.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the bacterial histone-like protein family.
CC {ECO:0000305}.
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DR EMBL; AB022517; BAA84958.1; -; Genomic_DNA.
DR EMBL; Z99263; CAB16449.1; -; Genomic_DNA.
DR EMBL; AL583923; CAC30636.1; -; Genomic_DNA.
DR PIR; T45427; T45427.
DR RefSeq; NP_302157.1; NC_002677.1.
DR RefSeq; WP_010908478.1; NC_002677.1.
DR AlphaFoldDB; O33125; -.
DR SMR; O33125; -.
DR STRING; 272631.ML1683; -.
DR EnsemblBacteria; CAC30636; CAC30636; CAC30636.
DR KEGG; mle:ML1683; -.
DR PATRIC; fig|272631.5.peg.3175; -.
DR Leproma; ML1683; -.
DR eggNOG; COG0776; Bacteria.
DR HOGENOM; CLU_085366_0_0_11; -.
DR OMA; AQFKAVI; -.
DR Proteomes; UP000000806; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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 Cell wall; DNA condensation; DNA-binding; Reference proteome; Repeat;
KW Secreted.
FT CHAIN 1..200
FT /note="DNA-binding protein HU homolog"
FT /id="PRO_0000104948"
FT REGION 1..90
FT /note="Bacterial histone-like domain"
FT REGION 101..200
FT /note="Degenerate repeats region"
FT REGION 179..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..200
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 200 AA; 20970 MW; F30D5C1A2BB53769 CRC64;
MNKAELIDVL TQKLGSDRRQ ATAAVENVVD TIVRAVHKGD SVTITGFGVF EQRRRAARVA
RNPRTGETVK VKPTSVPAFR PGAQFKAVVA GAQRLPLEGP AVKRGVATSA AKKAAIKKAP
VKKALAKKAA TKAPAKKAVK APAKKITTAV KVPAKKATKV VKKVAAKAPV RKATTRALAK
KAAVKKAPAK KVTAAKRGRK