HPR_BACSU
ID HPR_BACSU Reviewed; 203 AA.
AC P11065;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=DNA-binding transcriptional repressor ScoC;
DE AltName: Full=HTH-type transcriptional regulator Hpr {ECO:0000255|HAMAP-Rule:MF_01911};
DE AltName: Full=Protease production regulatory protein Hpr {ECO:0000255|HAMAP-Rule:MF_01911};
GN Name=hpr {ECO:0000255|HAMAP-Rule:MF_01911, ECO:0000303|Ref.11};
GN Synonyms=catA, scoC; OrderedLocusNames=BSU09990;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3131303; DOI=10.1128/jb.170.6.2560-2567.1988;
RA Perego M., Hoch J.A.;
RT "Sequence analysis and regulation of the hpr locus, a regulatory gene for
RT protease production and sporulation in Bacillus subtilis.";
RL J. Bacteriol. 170:2560-2567(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9579061; DOI=10.1099/00221287-144-4-859;
RA Noback M.A., Holsappel S., Kiewiet R., Terpstra P., Wambutt R., Wedler H.,
RA Venema G., Bron S.;
RT "The 172 kb prkA-addAB region from 83 degrees to 97 degrees of the Bacillus
RT subtilis chromosome contains several dysfunctional genes, the glyB marker,
RT many genes encoding transporter proteins, and the ubiquitous hit gene.";
RL Microbiology 144:859-875(1998).
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 PROTEIN SEQUENCE OF 1-10, AND FUNCTION.
RX PubMed=1906467; DOI=10.1016/s0021-9258(18)98855-1;
RA Kallio P.T., Fagelson J.E., Hoch J.A., Strauch M.A.;
RT "The transition state regulator Hpr of Bacillus subtilis is a DNA-binding
RT protein.";
RL J. Biol. Chem. 266:13411-13417(1991).
RN [5]
RP FUNCTION.
RC STRAIN=168 / JH642;
RX PubMed=10383984; DOI=10.1128/jb.181.13.4114-4117.1999;
RA Koide A., Perego M., Hoch J.A.;
RT "ScoC regulates peptide transport and sporulation initiation in Bacillus
RT subtilis.";
RL J. Bacteriol. 181:4114-4117(1999).
RN [6]
RP INTERACTION WITH SINR.
RX PubMed=15104138; DOI=10.1023/b:bile.0000018259.66762.ed;
RA Sanchez A., Olmos J.;
RT "Bacillus subtilis transcriptional regulators interaction.";
RL Biotechnol. Lett. 26:403-407(2004).
RN [7]
RP REGULATION BY SALA.
RX PubMed=15126467; DOI=10.1128/jb.186.10.3056-3064.2004;
RA Ogura M., Matsuzawa A., Yoshikawa H., Tanaka T.;
RT "Bacillus subtilis SalA (YbaL) negatively regulates expression of scoC,
RT which encodes the repressor for the alkaline exoprotease gene, aprE.";
RL J. Bacteriol. 186:3056-3064(2004).
RN [8]
RP REGULATION BY SENS.
RC STRAIN=168 / CU741;
RX PubMed=16321961; DOI=10.1128/jb.187.24.8526-8530.2005;
RA Kawachi E., Abe S., Tanaka T.;
RT "Inhibition of Bacillus subtilis scoC expression by multicopy senS.";
RL J. Bacteriol. 187:8526-8530(2005).
RN [9]
RP FUNCTION, AND INTERACTION WITH SINR.
RC STRAIN=168;
RX PubMed=16923912; DOI=10.1128/jb.00427-06;
RA Kodgire P., Dixit M., Rao K.K.;
RT "ScoC and SinR negatively regulate epr by corepression in Bacillus
RT subtilis.";
RL J. Bacteriol. 188:6425-6428(2006).
RN [10]
RP FUNCTION, AND DNA-BINDING.
RC STRAIN=168 / PY79;
RX PubMed=32324221; DOI=10.1093/nar/gkaa266;
RA Nye T.M., van Gijtenbeek L.A., Stevens A.G., Schroeder J.W., Randall J.R.,
RA Matthews L.A., Simmons L.A.;
RT "Methyltransferase DnmA is responsible for genome-wide N6-methyladenosine
RT modifications at non-palindromic recognition sites in Bacillus subtilis.";
RL Nucleic Acids Res. 48:5332-5348(2020).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), AND SUBUNIT.
RA Cuff M.E., Skarina T., Edwards A., Savchenko A., Joachimiak A.;
RT "Structure of the protease production regulatory protein hpr from Bacillus
RT subtilis.";
RL Submitted (FEB-2006) to the PDB data bank.
CC -!- FUNCTION: Negative regulator of protease production and sporulation.
CC Acts by binding directly to the promoter of protease genes (aprE and
CC nprE), and by repressing oligopeptide permease operons (appABCDF and
CC oppABCDF), thereby preventing uptake of oligopeptides required for
CC initiation of sporulation. Acts with SinR as a corepressor of epr
CC expression. Binds to non-m6A-5-methylated 5'-GACGAG-3' sites, tested
CC with scpA; when the target is methylated by DnmA, this repressor no
CC longer binds and transcription is up-regulated (PubMed:32324221).
CC {ECO:0000255|HAMAP-Rule:MF_01911, ECO:0000269|PubMed:10383984,
CC ECO:0000269|PubMed:16923912, ECO:0000269|PubMed:1906467,
CC ECO:0000269|PubMed:32324221}.
CC -!- SUBUNIT: Homodimer. Interacts with SinR. {ECO:0000255|HAMAP-
CC Rule:MF_01911, ECO:0000269|PubMed:15104138,
CC ECO:0000269|PubMed:16923912, ECO:0000269|Ref.11}.
CC -!- INTERACTION:
CC P11065; O34483: hprK; NbExp=3; IntAct=EBI-2121844, EBI-5242785;
CC -!- INDUCTION: Negatively regulated by the Mrp homolog protein SalA and by
CC SenS. {ECO:0000269|PubMed:15126467, ECO:0000269|PubMed:16321961}.
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DR EMBL; M20237; AAA22525.1; -; Genomic_DNA.
DR EMBL; Y14077; CAA74414.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12839.1; -; Genomic_DNA.
DR PIR; A32009; A32009.
DR RefSeq; NP_388880.1; NC_000964.3.
DR RefSeq; WP_003239501.1; NZ_CP053102.1.
DR PDB; 2FXA; X-ray; 2.40 A; A/B/C/D=1-203.
DR PDBsum; 2FXA; -.
DR AlphaFoldDB; P11065; -.
DR SMR; P11065; -.
DR IntAct; P11065; 3.
DR STRING; 224308.BSU09990; -.
DR jPOST; P11065; -.
DR PaxDb; P11065; -.
DR PRIDE; P11065; -.
DR EnsemblBacteria; CAB12839; CAB12839; BSU_09990.
DR GeneID; 939765; -.
DR KEGG; bsu:BSU09990; -.
DR PATRIC; fig|224308.179.peg.1074; -.
DR eggNOG; COG1846; Bacteria.
DR OMA; EKDWQNW; -.
DR BioCyc; BSUB:BSU09990-MON; -.
DR EvolutionaryTrace; P11065; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:CACAO.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.10.10; -; 1.
DR HAMAP; MF_01911; HTH_type_Hpr; 1.
DR InterPro; IPR000835; HTH_MarR-typ.
DR InterPro; IPR023488; HTH_tscrpt_reg_Hpr.
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 3D-structure; Direct protein sequencing; DNA-binding; Reference proteome;
KW Repressor; Sporulation; Transcription; Transcription regulation.
FT CHAIN 1..203
FT /note="DNA-binding transcriptional repressor ScoC"
FT /id="PRO_0000054361"
FT DOMAIN 13..157
FT /note="HTH marR-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01911"
FT DNA_BIND 63..86
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01911"
FT REGION 183..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 10..38
FT /evidence="ECO:0007829|PDB:2FXA"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:2FXA"
FT HELIX 46..58
FT /evidence="ECO:0007829|PDB:2FXA"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:2FXA"
FT HELIX 63..69
FT /evidence="ECO:0007829|PDB:2FXA"
FT HELIX 74..86
FT /evidence="ECO:0007829|PDB:2FXA"
FT STRAND 89..93
FT /evidence="ECO:0007829|PDB:2FXA"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:2FXA"
FT HELIX 108..120
FT /evidence="ECO:0007829|PDB:2FXA"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:2FXA"
FT HELIX 127..131
FT /evidence="ECO:0007829|PDB:2FXA"
FT HELIX 133..139
FT /evidence="ECO:0007829|PDB:2FXA"
FT HELIX 146..161
FT /evidence="ECO:0007829|PDB:2FXA"
FT TURN 162..165
FT /evidence="ECO:0007829|PDB:2FXA"
FT HELIX 169..174
FT /evidence="ECO:0007829|PDB:2FXA"
FT STRAND 175..178
FT /evidence="ECO:0007829|PDB:2FXA"
FT STRAND 181..184
FT /evidence="ECO:0007829|PDB:2FXA"
SQ SEQUENCE 203 AA; 23713 MW; 26F46DFBD3E2F5AD CRC64;
MNRVEPPYDV KEALVFTQKM AQLSKALWKS IEKDWQQWLK PYDLNINEHH ILWIAYQLNG
ASISEIAKFG VMHVSTAFNF SKKLEERGYL RFSKRLNDKR NTYVQLTEEG TEVFWSLLEE
FDPTRNAVFK GSQPLYHLFG KFPEVAEMMC MIRHIYGDDF MEIFETSLTN IDNDFESVNG
KLKKKAKDSA ADEPAEELEP VNS
