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Protein

HTH-type transcriptional regulator Hpr

Gene

hpr

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Negative regulator of protease production and sporulation. Acts by binding directly to the promoter of protease genes (aprE and nprE), and by repressing oligopeptide permease operons (appABCDF and oppABCDF), thereby preventing uptake of oligopeptides required for initiation of sporulation. Acts with SinR as a corepressor of epr expression.UniRule annotation3 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi63 – 8624H-T-H motifUniRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Sporulation, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciBSUB:BSU09990-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
HTH-type transcriptional regulator HprUniRule annotation
Alternative name(s):
Protease production regulatory protein HprUniRule annotation
Gene namesi
Name:hprUniRule annotation
Synonyms:catA, scoC
Ordered Locus Names:BSU09990
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 203203HTH-type transcriptional regulator HprPRO_0000054361Add
BLAST

Proteomic databases

PaxDbiP11065.

Expressioni

Inductioni

Negatively regulated by the Mrp homolog protein SalA and by SenS.

Interactioni

Subunit structurei

Homodimer. Interacts with SinR.UniRule annotation3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
hprKO344833EBI-2121844,EBI-5242785

Protein-protein interaction databases

IntActiP11065. 3 interactions.
STRINGi224308.Bsubs1_010100005556.

Structurei

Secondary structure

1
203
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 3829Combined sources
Helixi40 – 423Combined sources
Helixi46 – 5813Combined sources
Beta strandi60 – 623Combined sources
Helixi63 – 697Combined sources
Helixi74 – 8613Combined sources
Beta strandi89 – 935Combined sources
Beta strandi103 – 1064Combined sources
Helixi108 – 12013Combined sources
Helixi123 – 1253Combined sources
Helixi127 – 1315Combined sources
Helixi133 – 1397Combined sources
Helixi146 – 16116Combined sources
Turni162 – 1654Combined sources
Helixi169 – 1746Combined sources
Beta strandi175 – 1784Combined sources
Beta strandi181 – 1844Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FXAX-ray2.40A/B/C/D1-203[»]
ProteinModelPortaliP11065.
SMRiP11065. Positions 8-187.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11065.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini13 – 157145HTH marR-typeUniRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 HTH marR-type DNA-binding domain.UniRule annotation

Phylogenomic databases

eggNOGiCOG1846. LUCA.
HOGENOMiHOG000246900.
KOiK09682.
OMAiEKDWQNW.
OrthoDBiEOG6C015Q.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
HAMAPiMF_01911. HTH_type_Hpr.
InterProiIPR000835. HTH_MarR-typ.
IPR023488. HTH_tscrpt_reg_Hpr.
IPR023187. Tscrpt_reg_MarR-type_CS.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF01047. MarR. 1 hit.
[Graphical view]
SMARTiSM00347. HTH_MARR. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
PROSITEiPS01117. HTH_MARR_1. 1 hit.
PS50995. HTH_MARR_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P11065-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNRVEPPYDV KEALVFTQKM AQLSKALWKS IEKDWQQWLK PYDLNINEHH
60 70 80 90 100
ILWIAYQLNG ASISEIAKFG VMHVSTAFNF SKKLEERGYL RFSKRLNDKR
110 120 130 140 150
NTYVQLTEEG TEVFWSLLEE FDPTRNAVFK GSQPLYHLFG KFPEVAEMMC
160 170 180 190 200
MIRHIYGDDF MEIFETSLTN IDNDFESVNG KLKKKAKDSA ADEPAEELEP

VNS
Length:203
Mass (Da):23,713
Last modified:July 1, 1989 - v1
Checksum:i26F46DFBD3E2F5AD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M20237 Genomic DNA. Translation: AAA22525.1.
Y14077 Genomic DNA. Translation: CAA74414.1.
AL009126 Genomic DNA. Translation: CAB12839.1.
PIRiA32009.
RefSeqiNP_388880.1. NC_000964.3.
WP_003239501.1. NZ_CP010052.1.

Genome annotation databases

EnsemblBacteriaiCAB12839; CAB12839; BSU09990.
GeneIDi939765.
KEGGibsu:BSU09990.
PATRICi18973692. VBIBacSub10457_1040.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M20237 Genomic DNA. Translation: AAA22525.1.
Y14077 Genomic DNA. Translation: CAA74414.1.
AL009126 Genomic DNA. Translation: CAB12839.1.
PIRiA32009.
RefSeqiNP_388880.1. NC_000964.3.
WP_003239501.1. NZ_CP010052.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FXAX-ray2.40A/B/C/D1-203[»]
ProteinModelPortaliP11065.
SMRiP11065. Positions 8-187.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP11065. 3 interactions.
STRINGi224308.Bsubs1_010100005556.

Proteomic databases

PaxDbiP11065.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB12839; CAB12839; BSU09990.
GeneIDi939765.
KEGGibsu:BSU09990.
PATRICi18973692. VBIBacSub10457_1040.

Phylogenomic databases

eggNOGiCOG1846. LUCA.
HOGENOMiHOG000246900.
KOiK09682.
OMAiEKDWQNW.
OrthoDBiEOG6C015Q.

Enzyme and pathway databases

BioCyciBSUB:BSU09990-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP11065.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
HAMAPiMF_01911. HTH_type_Hpr.
InterProiIPR000835. HTH_MarR-typ.
IPR023488. HTH_tscrpt_reg_Hpr.
IPR023187. Tscrpt_reg_MarR-type_CS.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF01047. MarR. 1 hit.
[Graphical view]
SMARTiSM00347. HTH_MARR. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
PROSITEiPS01117. HTH_MARR_1. 1 hit.
PS50995. HTH_MARR_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence analysis and regulation of the hpr locus, a regulatory gene for protease production and sporulation in Bacillus subtilis."
    Perego M., Hoch J.A.
    J. Bacteriol. 170:2560-2567(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The 172 kb prkA-addAB region from 83 degrees to 97 degrees of the Bacillus subtilis chromosome contains several dysfunctional genes, the glyB marker, many genes encoding transporter proteins, and the ubiquitous hit gene."
    Noback M.A., Holsappel S., Kiewiet R., Terpstra P., Wambutt R., Wedler H., Venema G., Bron S.
    Microbiology 144:859-875(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168.
  3. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
    Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.
  4. "The transition state regulator Hpr of Bacillus subtilis is a DNA-binding protein."
    Kallio P.T., Fagelson J.E., Hoch J.A., Strauch M.A.
    J. Biol. Chem. 266:13411-13417(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-10, FUNCTION.
  5. "ScoC regulates peptide transport and sporulation initiation in Bacillus subtilis."
    Koide A., Perego M., Hoch J.A.
    J. Bacteriol. 181:4114-4117(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
    Strain: 168 / JH642.
  6. "Bacillus subtilis transcriptional regulators interaction."
    Sanchez A., Olmos J.
    Biotechnol. Lett. 26:403-407(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SINR.
  7. "Bacillus subtilis SalA (YbaL) negatively regulates expression of scoC, which encodes the repressor for the alkaline exoprotease gene, aprE."
    Ogura M., Matsuzawa A., Yoshikawa H., Tanaka T.
    J. Bacteriol. 186:3056-3064(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: REGULATION BY SALA.
  8. "Inhibition of Bacillus subtilis scoC expression by multicopy senS."
    Kawachi E., Abe S., Tanaka T.
    J. Bacteriol. 187:8526-8530(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: REGULATION BY SENS.
    Strain: 168 / CU741.
  9. "ScoC and SinR negatively regulate epr by corepression in Bacillus subtilis."
    Kodgire P., Dixit M., Rao K.K.
    J. Bacteriol. 188:6425-6428(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SINR.
    Strain: 168.
  10. "Structure of the protease production regulatory protein hpr from Bacillus subtilis."
    Cuff M.E., Skarina T., Edwards A., Savchenko A., Joachimiak A.
    Submitted (FEB-2006) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), SUBUNIT.

Entry informationi

Entry nameiHPR_BACSU
AccessioniPrimary (citable) accession number: P11065
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: June 8, 2016
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.