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 27-MAR-2024, entry version 120.
DE RecName: Full=HTH-type transcriptional regulator NorG;
GN Name=norG; OrderedLocusNames=SA0104;
OS Staphylococcus aureus (strain N315).
OC Bacteria; Bacillota; 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}.
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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 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; cd00609; AAT_like; 1.
DR CDD; cd07377; WHTH_GntR; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 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 PANTHER; PTHR42790; AMINOTRANSFERASE; 1.
DR PANTHER; PTHR42790:SF19; AROMATIC AMINO ACID AMINOTRANSFERASE DDB_G0272014; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR Pfam; PF00392; GntR; 1.
DR PRINTS; PR00035; HTHGNTR.
DR SMART; SM00345; HTH_GNTR; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 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
//
