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Protein

HPr-like protein Crh

Gene

crh

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Along with seryl-phosphorylated HPr, phosphorylated Crh is implicated in carbon catabolite repression (CCR) of levanase, inositol dehydrogenase, and beta-xylosidase. Exerts its effect on CCR by interacting with CcpA.2 Publications

Enzyme and pathway databases

BioCyciBSUB:BSU34740-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
HPr-like protein Crh
Alternative name(s):
Catabolite repression HPr
Gene namesi
Name:crh
Synonyms:yvcM
Ordered Locus Names:BSU34740
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi15 – 151Q → H: Cannot fulfill its catalytic role within PTS transport. Does not affect dimerization. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 8585HPr-like protein CrhPRO_0000107899Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei46 – 461Phosphoserine; by HPrK/PPROSITE-ProRule annotation2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiO06976.

PTM databases

iPTMnetiO06976.

Interactioni

Subunit structurei

Mixture of monomers and homodimers. Interacts with CcpA as a monomer.2 Publications

Protein-protein interaction databases

IntActiO06976. 2 interactions.
STRINGi224308.Bsubs1_010100018816.

Structurei

Secondary structure

1
85
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 76Combined sources
Beta strandi12 – 143Combined sources
Helixi16 – 2611Combined sources
Beta strandi29 – 379Combined sources
Beta strandi40 – 434Combined sources
Helixi47 – 526Combined sources
Beta strandi60 – 678Combined sources
Helixi70 – 8112Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K1CNMR-A2-85[»]
1MO1X-ray1.80A/B/C/D1-85[»]
1MU4X-ray1.80A/B1-85[»]
1ZVVX-ray2.98J/P/W1-85[»]
2AK7X-ray2.00A/B1-85[»]
2RLZNMR-A/B1-85[»]
ProteinModelPortaliO06976.
SMRiO06976. Positions 1-85.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO06976.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 8585HPrPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the HPr family.Curated
Contains 1 HPr domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4105KRI. Bacteria.
COG1925. LUCA.
HOGENOMiHOG000278399.
InParanoidiO06976.
KOiK11184.
OMAiFVQEANK.
OrthoDBiEOG6XDGX2.
PhylomeDBiO06976.

Family and domain databases

Gene3Di3.30.1340.10. 1 hit.
InterProiIPR000032. HPr-like.
IPR002114. PTS_HPr_Ser_P_site.
[Graphical view]
PfamiPF00381. PTS-HPr. 1 hit.
[Graphical view]
PRINTSiPR00107. PHOSPHOCPHPR.
SUPFAMiSSF55594. SSF55594. 1 hit.
TIGRFAMsiTIGR01003. PTS_HPr_family. 1 hit.
PROSITEiPS51350. PTS_HPR_DOM. 1 hit.
PS00589. PTS_HPR_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O06976-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVQQKVEVRL KTGLQARPAA LFVQEANRFT SDVFLEKDGK KVNAKSIMGL
60 70 80
MSLAVSTGTE VTLIAQGEDE QEALEKLAAY VQEEV
Length:85
Mass (Da):9,327
Last modified:July 1, 1997 - v1
Checksum:i1801425F51B9B3F6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z94043 Genomic DNA. Translation: CAB08060.1.
AL009126 Genomic DNA. Translation: CAB15479.1.
PIRiD69607.
RefSeqiNP_391354.1. NC_000964.3.
WP_003219835.1. NZ_JNCM01000033.1.

Genome annotation databases

EnsemblBacteriaiCAB15479; CAB15479; BSU34740.
GeneIDi11241079.
938474.
KEGGibsu:BSU34740.
PATRICi18978954. VBIBacSub10457_3639.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z94043 Genomic DNA. Translation: CAB08060.1.
AL009126 Genomic DNA. Translation: CAB15479.1.
PIRiD69607.
RefSeqiNP_391354.1. NC_000964.3.
WP_003219835.1. NZ_JNCM01000033.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K1CNMR-A2-85[»]
1MO1X-ray1.80A/B/C/D1-85[»]
1MU4X-ray1.80A/B1-85[»]
1ZVVX-ray2.98J/P/W1-85[»]
2AK7X-ray2.00A/B1-85[»]
2RLZNMR-A/B1-85[»]
ProteinModelPortaliO06976.
SMRiO06976. Positions 1-85.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO06976. 2 interactions.
STRINGi224308.Bsubs1_010100018816.

PTM databases

iPTMnetiO06976.

Proteomic databases

PaxDbiO06976.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB15479; CAB15479; BSU34740.
GeneIDi11241079.
938474.
KEGGibsu:BSU34740.
PATRICi18978954. VBIBacSub10457_3639.

Phylogenomic databases

eggNOGiENOG4105KRI. Bacteria.
COG1925. LUCA.
HOGENOMiHOG000278399.
InParanoidiO06976.
KOiK11184.
OMAiFVQEANK.
OrthoDBiEOG6XDGX2.
PhylomeDBiO06976.

Enzyme and pathway databases

BioCyciBSUB:BSU34740-MONOMER.

Miscellaneous databases

EvolutionaryTraceiO06976.

Family and domain databases

Gene3Di3.30.1340.10. 1 hit.
InterProiIPR000032. HPr-like.
IPR002114. PTS_HPr_Ser_P_site.
[Graphical view]
PfamiPF00381. PTS-HPr. 1 hit.
[Graphical view]
PRINTSiPR00107. PHOSPHOCPHPR.
SUPFAMiSSF55594. SSF55594. 1 hit.
TIGRFAMsiTIGR01003. PTS_HPr_family. 1 hit.
PROSITEiPS51350. PTS_HPR_DOM. 1 hit.
PS00589. PTS_HPR_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Denizot F.
    Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "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.
  3. "The Bacillus subtilis crh gene encodes a HPr-like protein involved in carbon catabolite repression."
    Galinier A., Haiech J., Kilhoffer M.-C., Jaquinod M., Stuelke J., Deutscher J., Martin-Verstraete I.
    Proc. Natl. Acad. Sci. U.S.A. 94:8439-8444(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION.
    Strain: QB5081.
  4. "Solution structure and dynamics of Crh, the Bacillus subtilis catabolite repression HPr."
    Favier A., Brutscher B., Blackledge M., Galinier A., Deutscher J., Penin F., Marion D.
    J. Mol. Biol. 317:131-144(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 2-85, SUBUNIT.
  5. "Crystal Structure at 1.8 A of the Bacillus subtilis catabolite repression containing protein (Crh) reveals an unexpected swapping domain as an untertwinned dimer."
    Juy M.R., Bockmann A., Galinier A., Penin F., Haser R.
    Submitted (SEP-2002) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS).
  6. "Dimerization of Crh by reversible 3D domain swapping induces structural adjustments to its monomeric homologue Hpr."
    Juy M., Penin F., Favier A., Galinier A., Montserret R., Haser R., Deutscher J., Bockmann A.
    J. Mol. Biol. 332:767-776(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS), MUTAGENESIS OF GLN-15.
  7. "Phosphoprotein Crh-Ser46-P displays altered binding to CcpA to effect carbon catabolite regulation."
    Schumacher M.A., Seidel G., Hillen W., Brennan R.G.
    J. Biol. Chem. 281:6793-6800(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.98 ANGSTROMS) IN COMPLEX WITH CCPA, FUNCTION, SUBUNIT, PHOSPHORYLATION AT SER-46.
  8. "X-ray structure of a domain-swapped dimer of Ser46-phosphorylated Crh from Bacillus subtilis."
    Chaptal V., Lariviere L., Gueguen-Chaignon V., Galinier A., Nessler S., Morera S.
    Proteins 63:249-251(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS), PHOSPHORYLATION AT SER-46.
  9. "3D structure determination of the Crh protein from highly ambiguous solid-state NMR restraints."
    Loquet A., Bardiaux B., Gardiennet C., Blanchet C., Baldus M., Nilges M., Malliavin T., Bockmann A.
    J. Am. Chem. Soc. 130:3579-3589(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.

Entry informationi

Entry nameiCRH_BACSU
AccessioniPrimary (citable) accession number: O06976
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 2002
Last sequence update: July 1, 1997
Last modified: July 6, 2016
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Not phosphorylated by PEP and by enzyme I.

Keywords - Technical termi

3D-structure, Complete proteome, 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.