ID   CYSB_KLEPN              Reviewed;         324 AA.
AC   P45600;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 2.
DT   25-MAY-2022, entry version 117.
DE   RecName: Full=HTH-type transcriptional regulator CysB;
DE   AltName: Full=Cys regulon transcriptional activator;
GN   Name=cysB;
OS   Klebsiella pneumoniae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=573;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 15380 / DSM 2026 / NCTC 418 / NCIMB 418;
RX   PubMed=8166630; DOI=10.1042/bj2990129;
RA   Lynch A.S., Tyrrell R., Smerdon S.J., Briggs G.S., Wilkinson A.J.;
RT   "Characterization of the CysB protein of Klebsiella aerogenes: direct
RT   evidence that N-acetylserine rather than O-acetylserine serves as the
RT   inducer of the cysteine regulon.";
RL   Biochem. J. 299:129-136(1994).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 88-324, AND SEQUENCE REVISION TO
RP   182.
RC   STRAIN=ATCC 15380 / DSM 2026 / NCTC 418 / NCIMB 418;
RX   PubMed=9309218; DOI=10.1016/s0969-2126(97)00254-2;
RA   Tyrrell R., Verschueren K.H., Dodson E.J., Murshudov G.N., Addy C.,
RA   Wilkinson A.J.;
RT   "The structure of the cofactor-binding fragment of the LysR family member,
RT   CysB: a familiar fold with a surprising subunit arrangement.";
RL   Structure 5:1017-1032(1997).
CC   -!- FUNCTION: This protein is a positive regulator of gene expression for
CC       the cysteine regulon. The inducer for CysB is N-acetylserine.
CC       Thiosulfate and sulfide act as anti-inducers.
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the LysR transcriptional regulatory family.
CC       {ECO:0000305}.
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DR   EMBL; X78729; CAA55380.1; -; Genomic_DNA.
DR   RefSeq; WP_002901772.1; NZ_WYAM01000004.1.
DR   PDB; 1AL3; X-ray; 1.80 A; A=1-324.
DR   PDBsum; 1AL3; -.
DR   AlphaFoldDB; P45600; -.
DR   SMR; P45600; -.
DR   OMA; FLRTYMY; -.
DR   OrthoDB; 990666at2; -.
DR   EvolutionaryTrace; P45600; -.
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   1: Evidence at protein level;
KW   3D-structure; Activator; Amino-acid biosynthesis; Cysteine biosynthesis;
KW   Cytoplasm; DNA-binding; Transcription; Transcription regulation.
FT   CHAIN           1..324
FT                   /note="HTH-type transcriptional regulator CysB"
FT                   /id="PRO_0000105618"
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"
FT   CONFLICT        182
FT                   /note="G -> A (in Ref. 1; CAA55380)"
FT                   /evidence="ECO:0000305"
FT   STRAND          92..99
FT                   /evidence="ECO:0007829|PDB:1AL3"
FT   HELIX           101..106
FT                   /evidence="ECO:0007829|PDB:1AL3"
FT   HELIX           109..118
FT                   /evidence="ECO:0007829|PDB:1AL3"
FT   STRAND          121..128
FT                   /evidence="ECO:0007829|PDB:1AL3"
FT   HELIX           131..139
FT                   /evidence="ECO:0007829|PDB:1AL3"
FT   STRAND          144..150
FT                   /evidence="ECO:0007829|PDB:1AL3"
FT   STRAND          158..166
FT                   /evidence="ECO:0007829|PDB:1AL3"
FT   STRAND          168..172
FT                   /evidence="ECO:0007829|PDB:1AL3"
FT   TURN            177..181
FT                   /evidence="ECO:0007829|PDB:1AL3"
FT   HELIX           186..190
FT                   /evidence="ECO:0007829|PDB:1AL3"
FT   STRAND          192..197
FT                   /evidence="ECO:0007829|PDB:1AL3"
FT   HELIX           204..214
FT                   /evidence="ECO:0007829|PDB:1AL3"
FT   STRAND          219..226
FT                   /evidence="ECO:0007829|PDB:1AL3"
FT   HELIX           227..236
FT                   /evidence="ECO:0007829|PDB:1AL3"
FT   STRAND          240..244
FT                   /evidence="ECO:0007829|PDB:1AL3"
FT   HELIX           245..247
FT                   /evidence="ECO:0007829|PDB:1AL3"
FT   TURN            250..252
FT                   /evidence="ECO:0007829|PDB:1AL3"
FT   STRAND          256..260
FT                   /evidence="ECO:0007829|PDB:1AL3"
FT   STRAND          268..275
FT                   /evidence="ECO:0007829|PDB:1AL3"
FT   HELIX           282..291
FT                   /evidence="ECO:0007829|PDB:1AL3"
FT   HELIX           297..305
FT                   /evidence="ECO:0007829|PDB:1AL3"
FT   HELIX           309..318
FT                   /evidence="ECO:0007829|PDB:1AL3"
SQ   SEQUENCE   324 AA;  35963 MW;  24B40A6001E0E009 CRC64;
     MKLQQLRYIV EVVNHNLNVS STAEGLYTSQ PGISKQVRML EDELGIQIFA RSGKHLTQVT
     PAGQEIIRIA REVLSKVDAI KSVAGEHTWP DKGSLYVATT HTQARYALPG VIKGFIERYP
     RVSLHMHQGS PTQIAEAVSK GNADFAIATE ALHLYDDLVM LPCYHWNRSI VVTPEHPLAT
     KGSVSIEELA QYPLVTYTFG FTGRSELDTA FNRAGLTPRI VFTATDADVI KTYVRLGLGV
     GVIASMAVDP VSDPDLVKLD ANGIFSHSTT KIGFRRSTFL RSYMYDFIQR FAPHLTRDVV
     DTAVALRSNE DIEAMFKDIK LPEK