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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)DescriptionActionsGraphical viewLength
DNA bindingi63 – 86H-T-H motifUniRule annotationAdd BLAST24

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)DescriptionActionsGraphical viewLength
ChainiPRO_00000543611 – 203HTH-type transcriptional regulator HprAdd BLAST203

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 interactors.
STRINGi224308.Bsubs1_010100005556.

Structurei

Secondary structure

1203
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi10 – 38Combined sources29
Helixi40 – 42Combined sources3
Helixi46 – 58Combined sources13
Beta strandi60 – 62Combined sources3
Helixi63 – 69Combined sources7
Helixi74 – 86Combined sources13
Beta strandi89 – 93Combined sources5
Beta strandi103 – 106Combined sources4
Helixi108 – 120Combined sources13
Helixi123 – 125Combined sources3
Helixi127 – 131Combined sources5
Helixi133 – 139Combined sources7
Helixi146 – 161Combined sources16
Turni162 – 165Combined sources4
Helixi169 – 174Combined sources6
Beta strandi175 – 178Combined sources4
Beta strandi181 – 184Combined sources4

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP11065.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini13 – 157HTH marR-typeUniRule annotationAdd BLAST145

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG1846. LUCA.
HOGENOMiHOG000246900.
KOiK09682.
OMAiEKDWQNW.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
HAMAPiMF_01911. HTH_type_Hpr. 1 hit.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2FXAX-ray2.40A/B/C/D1-203[»]
ProteinModelPortaliP11065.
SMRiP11065.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP11065. 3 interactors.
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.

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. 1 hit.
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...

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: November 2, 2016
This is version 128 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.