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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
 
 
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