ID   PCHR_BACSU              Reviewed;         169 AA.
AC   P40762;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=HTH-type transcriptional regulator PchR {ECO:0000305};
DE   AltName: Full=Pulcherriminic acid biosynthetis regulator {ECO:0000305};
GN   Name=pchR {ECO:0000303|PubMed:27542896}; Synonyms=yvmB, yzhA;
GN   OrderedLocusNames=BSU35080;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / BD170;
RA   Walther T., Hofemeister J.W.;
RT   "Transposon Tn917 mutants of Bacillus subtilis involved in protein
RT   secretion.";
RL   Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Lazarevic V., Soldo B., Rivolta C., Reynolds S., Mauel C., Karamata D.;
RT   "Nucleotide sequence of the 300-304 chromosomal segment of Bacillus
RT   subtilis.";
RL   Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [4]
RP   FUNCTION, DNA-BINDING, SUBUNIT, DEVELOPMENTAL STAGE, INDUCTION, AND
RP   DISRUPTION PHENOTYPE.
RX   PubMed=27542896; DOI=10.1186/s12866-016-0807-3;
RA   Randazzo P., Aubert-Frambourg A., Guillot A., Auger S.;
RT   "The MarR-like protein PchR (YvmB) regulates expression of genes involved
RT   in pulcherriminic acid biosynthesis and in the initiation of sporulation in
RT   Bacillus subtilis.";
RL   BMC Microbiol. 16:190-190(2016).
CC   -!- FUNCTION: Represses the expression of the yvmC-cypX operon, which is
CC       involved in pulcherriminic acid biosynthesis. Also negatively regulates
CC       yvmA, yvnB and its own expression. Positively regulates yisI
CC       expression. Acts by binding specifically to a 14-bp palindromic motif,
CC       the YvmB box, which is present in the promoter region of the target
CC       genes. {ECO:0000269|PubMed:27542896}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:27542896}.
CC   -!- DEVELOPMENTAL STAGE: Expression increases during entry into stationary
CC       phase. {ECO:0000269|PubMed:27542896}.
CC   -!- INDUCTION: Up-regulated in response to iron starvation. Negatively
CC       autoregulated. Also repressed by CcpA in stationary growth phase.
CC       {ECO:0000269|PubMed:27542896}.
CC   -!- DISRUPTION PHENOTYPE: Deletion of the gene induces changes of proteins
CC       involved in cellular processes depending on iron availability. In iron-
CC       rich medium, mutants overproduce a red pigment after entry into the
CC       stationary growth phase. {ECO:0000269|PubMed:27542896}.
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DR   EMBL; Z36881; CAA85355.1; -; Genomic_DNA.
DR   EMBL; AF017113; AAC67278.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15513.1; -; Genomic_DNA.
DR   PIR; S47218; S47218.
DR   RefSeq; NP_391388.1; NC_000964.3.
DR   RefSeq; WP_003228073.1; NZ_JNCM01000033.1.
DR   AlphaFoldDB; P40762; -.
DR   SMR; P40762; -.
DR   IntAct; P40762; 1.
DR   STRING; 224308.BSU35080; -.
DR   PaxDb; P40762; -.
DR   PRIDE; P40762; -.
DR   EnsemblBacteria; CAB15513; CAB15513; BSU_35080.
DR   GeneID; 936625; -.
DR   KEGG; bsu:BSU35080; -.
DR   PATRIC; fig|224308.179.peg.3798; -.
DR   eggNOG; COG1846; Bacteria.
DR   InParanoid; P40762; -.
DR   OMA; GQHEPIN; -.
DR   PhylomeDB; P40762; -.
DR   BioCyc; BSUB:BSU35080-MON; -.
DR   Proteomes; UP000001570; 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:0045892; P:negative regulation of transcription, DNA-templated; IMP:CACAO.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:CACAO.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR000835; HTH_MarR-typ.
DR   InterPro; IPR023187; Tscrpt_reg_MarR-type_CS.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF01047; MarR; 1.
DR   SMART; SM00347; HTH_MARR; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   PROSITE; PS01117; HTH_MARR_1; 1.
DR   PROSITE; PS50995; HTH_MARR_2; 1.
PE   1: Evidence at protein level;
KW   Activator; DNA-binding; Reference proteome; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..169
FT                   /note="HTH-type transcriptional regulator PchR"
FT                   /id="PRO_0000054403"
FT   DOMAIN          10..153
FT                   /note="HTH marR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00345"
FT   DNA_BIND        64..87
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00345"
SQ   SEQUENCE   169 AA;  19682 MW;  E33FBE3EAA5A48B3 CRC64;
     MSDLTKQMIY DIYVRLLHLN EQKANTSLQQ FFKEAAEEDV AEIPKNMTSI HVIDCIGQHE
     PINNAGIARK MNLSKANVTK ISTKLIKEEF INSYQLTDNK KEVYFKLTRK GRRIFDLHEK
     LHKKKELAFY QFLDSFSQEE QKAVLKFLEQ LTSTLEAEQT DGTPDKPVK