ID   NORG_STAAN              Reviewed;         442 AA.
AC   Q7A875;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 114.
DE   RecName: Full=HTH-type transcriptional regulator NorG;
GN   Name=norG; OrderedLocusNames=SA0104;
OS   Staphylococcus aureus (strain N315).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=158879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N315;
RX   PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA   Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA   Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA   Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA   Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL   Lancet 357:1225-1240(2001).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BA000018; BAB41323.1; -; Genomic_DNA.
DR   PIR; H89770; H89770.
DR   AlphaFoldDB; Q7A875; -.
DR   SMR; Q7A875; -.
DR   EnsemblBacteria; BAB41323; BAB41323; BAB41323.
DR   KEGG; sau:SA0104; -.
DR   HOGENOM; CLU_017584_0_0_9; -.
DR   OMA; GGCFNNY; -.
DR   Proteomes; UP000000751; 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; 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_0000305322"
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;  51287 MW;  2B315715D82C7A92 CRC64;
     MKIPPQRQLA IQYNVNRVTI IKSIELLEAE GFIYTKVGSG TYVNDYLNEA HITNKWSEMM
     LWSSQQRSQY TVQLINKIET DDSYIHISKG ELGISLMPHI QLKKAMSNTA SHIEDLSFGY
     NNGYGYIKLR DIIVERMSKQ GINVGRENVM ITSGALHAIQ LLSIGFLGQD AIIISNTPSY
     IHSTNVFEQL NFRHIDVPYN QINEINTIID RFINFKNKAI YIEPRFNNPT GRSLTNEQKK
     NIITYSERHN IPIIEDDIFR DIFFSDPTPA IKTYDKLGKV IHISSFSKTI APAIRIGWIV
     ASEKIIEQLA DVRMQIDYGS SILSQMVVYE MLKNKSYDKH LVKLRYVLKD KRDFMLNILN
     NLFKDIAHWE VPSGGYFVWL VFKIDIDIKY LFYELLSKEK ILINPGYIYG SKEKSIRLSF
     AFESNENIKH ALYKIYTYVK KV