CYSB_ECOL6
ID CYSB_ECOL6 Reviewed; 324 AA.
AC P0A9F4; P06613; P76834;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=HTH-type transcriptional regulator CysB;
DE AltName: Full=Cys regulon transcriptional activator;
GN Name=cysB; OrderedLocusNames=c1742;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC -!- FUNCTION: This protein is a positive regulator of gene expression for
CC the cysteine regulon. The inducer for CysB is N-acetylserine (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the LysR transcriptional regulatory family.
CC {ECO:0000305}.
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DR EMBL; AE014075; AAN80208.1; -; Genomic_DNA.
DR RefSeq; WP_000776253.1; NC_004431.1.
DR AlphaFoldDB; P0A9F4; -.
DR SMR; P0A9F4; -.
DR STRING; 199310.c1742; -.
DR PRIDE; P0A9F4; -.
DR EnsemblBacteria; AAN80208; AAN80208; c1742.
DR GeneID; 66674903; -.
DR KEGG; ecc:c1742; -.
DR eggNOG; COG0583; Bacteria.
DR HOGENOM; CLU_039613_6_2_6; -.
DR OMA; FLRTYMY; -.
DR BioCyc; ECOL199310:C1742-MON; -.
DR Proteomes; UP000001410; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0019344; P:cysteine biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR005119; LysR_subst-bd.
DR InterPro; IPR000847; Tscrpt_reg_HTH_LysR.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00126; HTH_1; 1.
DR Pfam; PF03466; LysR_substrate; 1.
DR PRINTS; PR00039; HTHLYSR.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS50931; HTH_LYSR; 1.
PE 3: Inferred from homology;
KW Activator; Amino-acid biosynthesis; Cysteine biosynthesis; Cytoplasm;
KW DNA-binding; Transcription; Transcription regulation.
FT CHAIN 1..324
FT /note="HTH-type transcriptional regulator CysB"
FT /id="PRO_0000105615"
FT DOMAIN 1..59
FT /note="HTH lysR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00253"
FT DNA_BIND 19..38
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00253"
SQ SEQUENCE 324 AA; 36150 MW; 3B35E9CFEF6F4C84 CRC64;
MKLQQLRYIV EVVNHNLNVS STAEGLYTSQ PGISKQVRML EDELGIQIFS RSGKHLTQVT
PAGQEIIRIA REVLSKVDAI KSVAGEHTWP DKGSLYIATT HTQARYALPN VIKGFIERYP
RVSLHMHQGS PTQIADAVSK GNADFAIATE ALHLYEDLVM LPCYHWNRAI VVTPDHPLAG
KKAITIEELA QYPLVTYTFG FTGRSELDTA FNRAGLTPRI VFTATDADVI KTYVRLGLGV
GVIASMAVDP VADPDLVRVD AHDIFSHSTT KIGFRRSTFL RSYMYDFIQR FAPHLTRDVV
DAAVALRSNE EIEVMFKDIK LPEK