ID   NORG_STAA8              Reviewed;         442 AA.
AC   Q2G1P1;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 2.
DT   25-MAY-2022, entry version 105.
DE   RecName: Full=HTH-type transcriptional regulator NorG;
GN   Name=norG; OrderedLocusNames=SAOUHSC_00064;
OS   Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 8325 / PS 47;
RA   Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT   "The Staphylococcus aureus NCTC 8325 genome.";
RL   (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL   Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL   D.C. (2006).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-13, FUNCTION AS A TRANSCRIPTIONAL REGULATOR, AND
RP   INDUCTION.
RX   PubMed=17277059; DOI=10.1128/jb.01819-06;
RA   Truong-Bolduc Q.C., Hooper D.C.;
RT   "The transcriptional regulators norG and mgrA modulate resistance to both
RT   quinolones and beta-lactams in Staphylococcus aureus.";
RL   J. Bacteriol. 189:2996-3005(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       Overexpression of norG leads to an increase in the level of resistance
CC       to quinolones, associated with a threefold increase in norB
CC       transcripts. Disruption of norG leads to an increase in the level of
CC       resistance to methicillin, cefotaxime, penicillin G, and nafcillin,
CC       associated with a threefold increase in abcA transcripts. Could also
CC       have an aminotransferase activity. {ECO:0000269|PubMed:17277059}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000305};
CC   -!- INDUCTION: Down-regulated by MgrA. {ECO:0000269|PubMed:17277059}.
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=ABD29250.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000253; ABD29250.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_498667.1; NC_007795.1.
DR   AlphaFoldDB; Q2G1P1; -.
DR   SMR; Q2G1P1; -.
DR   STRING; 93061.SAOUHSC_00064; -.
DR   EnsemblBacteria; ABD29250; ABD29250; SAOUHSC_00064.
DR   GeneID; 3919094; -.
DR   KEGG; sao:SAOUHSC_00064; -.
DR   PATRIC; fig|93061.5.peg.56; -.
DR   HOGENOM; CLU_017584_0_0_9; -.
DR   Proteomes; UP000008816; Chromosome.
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; IBA:GO_Central.
DR   GO; GO:1901605; P:alpha-amino acid metabolic process; IBA:GO_Central.
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   1: Evidence at protein level;
KW   Activator; Aminotransferase; Direct protein sequencing; DNA-binding;
KW   Pyridoxal phosphate; Reference proteome; Repressor; Transcription;
KW   Transcription regulation; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:17277059"
FT   CHAIN           2..442
FT                   /note="HTH-type transcriptional regulator NorG"
FT                   /id="PRO_0000305323"
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"
FT   CONFLICT        5
FT                   /note="S -> P (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        6
FT                   /note="H -> Q (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   442 AA;  51303 MW;  340EC99245972319 CRC64;
     MKIPSHRQLA IQYNVNRVTI IKSIELLEAE GFIYTKVGSG TYVNDYLNEA HITNKWSEMM
     LWSSQQRSQY TVQLINKIET DDSYIHISKG ELGISLMPHI QLKKAMSNTA SHIEDLSFGY
     NNGYGYIKLR DIIVERMSKQ GINVGRENVM ITSGALHAIQ LLSIGFLGQD AIIISNTPSY
     IHSTNVFEQL NFRHIDVPYN QINEIDTIID RFINFKNKAI YIEPRFNNPT GRSLTNEQKK
     NIITYSERHN IPIIEDDIFR DIFFSDPTPS IKTYDKLGKV IHISSFSKTI APAIRIGWIV
     ASEKIIEQLA DVRMQIDYGS SILSQMVVYE MLKNKSYDKH LVKLRYVLKD KRDFMLNILN
     NLFKDIAHWE VPSGGYFVWL VFKIDIDIKY LFYELLSKEK ILINPGYIYG SKEKSIRLSF
     AFESNENIKH ALYKIYTYVK KV