ID A0A1A1YSG7_9MYCO Unreviewed; 213 AA.
AC A0A1A1YSG7;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=DNA-binding protein HupB {ECO:0000256|ARBA:ARBA00035692};
DE EC=1.16.3.1 {ECO:0000256|ARBA:ARBA00013107};
DE AltName: Full=DNA-binding protein HU homolog {ECO:0000256|ARBA:ARBA00035729};
DE AltName: Full=Histone-like protein {ECO:0000256|ARBA:ARBA00032423};
GN ORFNames=A5724_16985 {ECO:0000313|EMBL:OBF34244.1};
OS Mycobacterium sp. ACS1612.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1834117 {ECO:0000313|EMBL:OBF34244.1, ECO:0000313|Proteomes:UP000092025};
RN [1] {ECO:0000313|Proteomes:UP000092025}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACS1612 {ECO:0000313|Proteomes:UP000092025};
RA Sutton G., Brinkac L., Sanka R., Adams M., Lau E., Kiyimba A., Mayanja H.,
RA Musoke P., Ssengooba W., Joloba M.;
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4 Fe(2+) + 4 H(+) + O2 = 4 Fe(3+) + 2 H2O;
CC Xref=Rhea:RHEA:11148, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.16.3.1;
CC Evidence={ECO:0000256|ARBA:ARBA00035572};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11149;
CC Evidence={ECO:0000256|ARBA:ARBA00035572};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, nucleoid
CC {ECO:0000256|ARBA:ARBA00004453}.
CC -!- SIMILARITY: Belongs to the bacterial histone-like protein family. Long
CC actinobacterial subfamily. {ECO:0000256|ARBA:ARBA00035660}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OBF34244.1}.
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DR EMBL; LZHZ01000032; OBF34244.1; -; Genomic_DNA.
DR RefSeq; WP_067802231.1; NZ_LZHZ01000032.1.
DR AlphaFoldDB; A0A1A1YSG7; -.
DR STRING; 1834117.A5724_16985; -.
DR OrthoDB; 9799835at2; -.
DR Proteomes; UP000092025; Unassembled WGS sequence.
DR GO; GO:0009295; C:nucleoid; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; 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 CDD; cd13831; HU; 1.
DR Gene3D; 4.10.520.10; IHF-like DNA-binding proteins; 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; DNA-BINDING PROTEIN HU; 1.
DR PANTHER; PTHR33175:SF3; DNA-BINDING PROTEIN HU-BETA; 1.
DR Pfam; PF00216; Bac_DNA_binding; 1.
DR PRINTS; PR01727; DNABINDINGHU.
DR SMART; SM00411; BHL; 1.
DR SUPFAM; SSF47729; IHF-like DNA-binding proteins; 1.
DR PROSITE; PS00045; HISTONE_LIKE; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW DNA condensation {ECO:0000256|ARBA:ARBA00023067};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000313|EMBL:OBF34244.1};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000092025};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT REGION 189..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 213 AA; 22301 MW; 49FF30D0FC6ECCB4 CRC64;
MNKAELIDVL TEKLGSDRRQ ATAAVENVVD TIVRAVHKGD SVTITGFGVF EQRRRAARVA
RNPRTGETVK VKPTSVPAFR PGAQFKAVVS GAQKLPAEGP AVKRGVTAGG GARKAVKRAA
AKKAVKRAAV KKAVKKAAVK KAVKRTAAKK AVKRTAVKKA VKRSAAKKAV KKAAAKKAVK
KAAAKKVVAK RAAAKKTARK APARKAPAKR GGR
//
