DBH_MYCTU
ID DBH_MYCTU Reviewed; 216 AA.
AC P9WMK7; L0TBG2; P95109;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 25-MAY-2022, sequence version 2.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=DNA-binding protein HU homolog;
DE AltName: Full=21 kDa laminin-2-binding protein;
DE AltName: Full=28 kDa iron-regulated protein;
DE Short=Irep-28;
DE AltName: Full=Histone-like protein;
DE Short=Hlp;
DE Contains:
DE RecName: Full=DNA-binding protein HU homolog, propeptide removed;
GN Name=hup; Synonyms=hlp, hupB, lbp21; OrderedLocusNames=Rv2986c;
GN ORFNames=MTCY349.01;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 35801 / TMC 107 / Erdman;
RX PubMed=10569769; DOI=10.1128/iai.67.12.6510-6517.1999;
RA Cohavy O., Harth G., Horwitz M., Eggena M., Landers C., Sutton C.,
RA Targan S.R., Braun J.;
RT "Identification of a novel mycobacterial histone H1 homologue (HupB) as an
RT antigenic target of pANCA monoclonal antibody and serum immunoglobulin A
RT from patients with Crohn's disease.";
RL Infect. Immun. 67:6510-6517(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [3]
RP PROTEIN SEQUENCE OF 2-15, AND SEQUENCE REVISION TO N-TERMINUS.
RC STRAIN=H37Rv;
RX PubMed=34915127; DOI=10.1016/j.ygeno.2021.12.001;
RA Shi J., Meng S., Wan L., Zhang Z., Jiang S., Zhu H., Dai E., Chang L.,
RA Gao H., Wan K., Zhang L., Zhao X., Liu H., Lyu Z., Zhang Y., Xu P.;
RT "Deep N-terminomics of Mycobacterium tuberculosis H37Rv extensively correct
RT annotated encoding genes.";
RL Genomics 114:292-304(2021).
RN [4]
RP PROTEIN SEQUENCE OF 6-15 AND 75-87.
RC STRAIN=ATCC 27294 / TMC 102 / H37Rv;
RX PubMed=12438350; DOI=10.1128/iai.70.12.6751-6760.2002;
RA Mueller-Ortiz S.L., Sepulveda E., Olsen M.R., Jagannath C., Wanger A.R.,
RA Norris S.J.;
RT "Decreased infectivity despite unaltered C3 binding by a DeltahbhA mutant
RT of Mycobacterium tuberculosis.";
RL Infect. Immun. 70:6751-6760(2002).
RN [5]
RP PROTEIN SEQUENCE OF 22-36; 89-96 AND 97-105, SUBCELLULAR LOCATION, AND
RP INDUCTION.
RC STRAIN=ATCC 27294 / TMC 102 / H37Rv;
RX PubMed=17028216; DOI=10.1128/cvi.00125-06;
RA Yeruva V.C., Duggirala S., Lakshmi V., Kolarich D., Altmann F.,
RA Sritharan M.;
RT "Identification and characterization of a major cell wall-associated iron-
RT regulated envelope protein (Irep-28) in Mycobacterium tuberculosis.";
RL Clin. Vaccine Immunol. 13:1137-1142(2006).
RN [6]
RP PROTEIN SEQUENCE OF 73-88, AND FUNCTION.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=10645441; DOI=10.1054/tuld.1998.0004;
RA Prabhakar S., Annapurna P.S., Jain N.K., Dey A.B., Tyagi J.S., Prasad H.K.;
RT "Identification of an immunogenic histone-like protein (HLPMt) of
RT Mycobacterium tuberculosis.";
RL Tuber. Lung Dis. 79:43-53(1998).
RN [7]
RP IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
RX PubMed=19099550; DOI=10.1186/1752-0509-2-109;
RA Raman K., Yeturu K., Chandra N.;
RT "targetTB: a target identification pipeline for Mycobacterium tuberculosis
RT through an interactome, reactome and genome-scale structural analysis.";
RL BMC Syst. Biol. 2:109-109(2008).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-3, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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 DNA non-specifically. Induces
CC lymphoproliferation, particularly in health tuberculin reactors, and is
CC immunogenic. Maybe involved in pathogenesis of inflammatory bowel
CC disease (IBD) in patients with ulcerative colitis and Crohn disease
CC (CD). Bound by anti-neutrophil cytoplasmic antibodies (pANCA), which
CC are a hallmark of IBD. The binding is due to pANCA directed against H1-
CC 3 cross-reacting with DBH epitopes. In CD, target of a strong IgA
CC response. {ECO:0000269|PubMed:10569769, ECO:0000269|PubMed:10645441}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000269|PubMed:17028216}.
CC -!- INDUCTION: By iron limitation. {ECO:0000269|PubMed:17028216}.
CC -!- MISCELLANEOUS: Was identified as a high-confidence drug target.
CC -!- SIMILARITY: Belongs to the bacterial histone-like protein family.
CC {ECO:0000305}.
CC -!- CAUTION: The revised start codon for the 216 residue version of this
CC protein is GTT. {ECO:0000269|PubMed:34915127}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CCP45791.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000269|PubMed:34915127};
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DR EMBL; AL123456; CCP45791.1; ALT_INIT; Genomic_DNA.
DR PIR; G70673; G70673.
DR RefSeq; NP_217502.1; NC_000962.3.
DR RefSeq; WP_003415107.1; NZ_NVQJ01000041.1.
DR PDB; 4DKY; X-ray; 2.48 A; A/B=3-102.
DR PDB; 4PT4; X-ray; 2.04 A; A/B=3-101.
DR PDBsum; 4DKY; -.
DR PDBsum; 4PT4; -.
DR AlphaFoldDB; P9WMK7; -.
DR SMR; P9WMK7; -.
DR MINT; P9WMK7; -.
DR STRING; 83332.Rv2986c; -.
DR iPTMnet; P9WMK7; -.
DR PaxDb; P9WMK7; -.
DR DNASU; 888166; -.
DR GeneID; 45426975; -.
DR GeneID; 888166; -.
DR KEGG; mtu:Rv2986c; -.
DR TubercuList; Rv2986c; -.
DR eggNOG; COG0776; Bacteria.
DR OMA; AQFKAVI; -.
DR Proteomes; UP000001584; Chromosome.
DR CollecTF; EXPREG_00000c50; -.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0032993; C:protein-DNA complex; IPI:CollecTF.
DR GO; GO:0003684; F:damaged DNA binding; IDA:MTBBASE.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0001216; F:DNA-binding transcription activator activity; IPI:CollecTF.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:MTBBASE.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0097100; F:supercoiled DNA binding; IDA:MTBBASE.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:CollecTF.
DR GO; GO:0010106; P:cellular response to iron ion starvation; IEP:MTBBASE.
DR GO; GO:0030261; P:chromosome condensation; IEA:UniProtKB-KW.
DR GO; GO:0042262; P:DNA protection; IDA:MTBBASE.
DR GO; GO:0090143; P:nucleoid organization; IDA:MTBBASE.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; EXP:CollecTF.
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; Acetylation; Cell wall; Direct protein sequencing;
KW DNA condensation; DNA-binding; Reference proteome; Repeat; Secreted.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:34915127"
FT CHAIN 2..216
FT /note="DNA-binding protein HU homolog"
FT /id="PRO_0000104950"
FT PROPEP 2
FT /note="Removed; alternate"
FT /evidence="ECO:0000269|PubMed:21969609"
FT /id="PRO_0000455388"
FT CHAIN 3..216
FT /note="DNA-binding protein HU homolog, propeptide removed"
FT /id="PRO_0000455389"
FT REGION 3..92
FT /note="Bacterial histone-like domain"
FT REGION 102..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 103..216
FT /note="Degenerate repeats region"
FT COMPBIAS 117..134
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..179
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 3
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:21969609"
FT CONFLICT 210
FT /note="T -> A (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT HELIX 3..14
FT /evidence="ECO:0007829|PDB:4PT4"
FT HELIX 18..37
FT /evidence="ECO:0007829|PDB:4PT4"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:4PT4"
FT TURN 45..47
FT /evidence="ECO:0007829|PDB:4PT4"
FT STRAND 48..55
FT /evidence="ECO:0007829|PDB:4PT4"
FT STRAND 57..61
FT /evidence="ECO:0007829|PDB:4PT4"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:4PT4"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:4PT4"
FT STRAND 74..81
FT /evidence="ECO:0007829|PDB:4PT4"
FT HELIX 83..89
FT /evidence="ECO:0007829|PDB:4PT4"
SQ SEQUENCE 216 AA; 22376 MW; C13A8B5DBCE1554B CRC64;
MGMNKAELID VLTQKLGSDR RQATAAVENV VDTIVRAVHK GDSVTITGFG VFEQRRRAAR
VARNPRTGET VKVKPTSVPA FRPGAQFKAV VSGAQRLPAE GPAVKRGVGA SAAKKVAKKA
PAKKATKAAK KAATKAPARK AATKAPAKKA ATKAPAKKAV KATKSPAKKV TKAVKKTAVK
ASVRKAATKA PAKKAAAKRP ATKAPAKKAT ARRGRK
