NORG_STAAB
ID NORG_STAAB Reviewed; 442 AA.
AC Q2YUS3;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 2.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=HTH-type transcriptional regulator NorG;
GN Name=norG; OrderedLocusNames=SAB0047;
OS Staphylococcus aureus (strain bovine RF122 / ET3-1).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=273036;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=bovine RF122 / ET3-1;
RX PubMed=17971880; DOI=10.1371/journal.pone.0001120;
RA Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.;
RT "Molecular correlates of host specialization in Staphylococcus aureus.";
RL PLoS ONE 2:E1120-E1120(2007).
CC -!- FUNCTION: Positively regulates the expression of the NorB efflux pump
CC and negatively regulates the expression of the AbcA efflux pump. Binds
CC specifically to the promoters of norA, norB and norC and abcA genes.
CC Could also have an aminotransferase activity (By similarity).
CC {ECO:0000250}.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000305};
CC -!- SIMILARITY: In the C-terminal section; belongs to the class-I
CC pyridoxal-phosphate-dependent aminotransferase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAI79735.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ938182; CAI79735.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q2YUS3; -.
DR SMR; Q2YUS3; -.
DR KEGG; sab:SAB0047; -.
DR HOGENOM; CLU_017584_0_0_9; -.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR CDD; cd07377; WHTH_GntR; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR000524; Tscrpt_reg_HTH_GntR.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR Pfam; PF00392; GntR; 1.
DR PRINTS; PR00035; HTHGNTR.
DR SMART; SM00345; HTH_GNTR; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS50949; HTH_GNTR; 1.
PE 3: Inferred from homology;
KW Activator; Aminotransferase; DNA-binding; Pyridoxal phosphate; Repressor;
KW Transcription; Transcription regulation; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..442
FT /note="HTH-type transcriptional regulator NorG"
FT /id="PRO_0000305319"
FT DOMAIN 2..46
FT /note="HTH gntR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00307"
FT DNA_BIND 6..25
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00307"
FT MOD_RES 288
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 442 AA; 51179 MW; D3B0CD4416DD3B22 CRC64;
MKIPSQRQLA IQYNVNRVTI IKSIELLEAE GFIYTKVGSG TYVNDYLNEA HITNKWSEMM
LWSSRQRSQY TVQLINKIET DASYIHISKG ELGQPLMPHI QLKKAMSNTA SHIEDLSFGY
NNGYGYIKLR DIIVERMSKQ GINVGRENVM ITSGALHAIQ LLSIGFLGQD AIIISNTPSY
IHSTNVFEQL NFRHIDAPYN QINEINTIID RFINFKNKAL YIEPRFNNPT GCSLTNEQKQ
NIITYSERHN IPIIEDDIFR DIFFSDPTPA IKTFDKLGKV IHISSFSKTI APAIRIGWIV
ASEKIIEQLA DVRMQIDYGS SILSQMVVYE MLKNKSYDKH LVKLRYVLKD KRDFMLNILN
NLFKDIAHWE VSSGGYFVWL VFKIDIDIKY LFYELLSKEK ILINPGYIYG SKEKSIRLSF
AFESNENIKH ALYKIYTYVK KV