NORG_STAA3
ID NORG_STAA3 Reviewed; 442 AA.
AC Q2FKF1;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 2.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=HTH-type transcriptional regulator NorG;
GN Name=norG; OrderedLocusNames=SAUSA300_0110;
OS Staphylococcus aureus (strain USA300).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=367830;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USA300;
RX PubMed=16517273; DOI=10.1016/s0140-6736(06)68231-7;
RA Diep B.A., Gill S.R., Chang R.F., Phan T.H., Chen J.H., Davidson M.G.,
RA Lin F., Lin J., Carleton H.A., Mongodin E.F., Sensabaugh G.F.,
RA Perdreau-Remington F.;
RT "Complete genome sequence of USA300, an epidemic clone of community-
RT acquired meticillin-resistant Staphylococcus aureus.";
RL Lancet 367:731-739(2006).
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=ABD22343.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000255; ABD22343.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q2FKF1; -.
DR SMR; Q2FKF1; -.
DR EnsemblBacteria; ABD22343; ABD22343; SAUSA300_0110.
DR KEGG; saa:SAUSA300_0110; -.
DR HOGENOM; CLU_017584_0_0_9; -.
DR Proteomes; UP000001939; 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_0000305324"
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; 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