CRH_BACSU
ID CRH_BACSU Reviewed; 85 AA.
AC O06976;
DT 13-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=HPr-like protein Crh;
DE AltName: Full=Catabolite repression HPr;
GN Name=crh; Synonyms=yvcM; OrderedLocusNames=BSU34740;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Denizot F.;
RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
RP FUNCTION, AND PHOSPHORYLATION.
RC STRAIN=QB5081;
RX PubMed=9237995; DOI=10.1073/pnas.94.16.8439;
RA Galinier A., Haiech J., Kilhoffer M.-C., Jaquinod M., Stuelke J.,
RA Deutscher J., Martin-Verstraete I.;
RT "The Bacillus subtilis crh gene encodes a HPr-like protein involved in
RT carbon catabolite repression.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:8439-8444(1997).
RN [4]
RP STRUCTURE BY NMR OF 2-85, AND SUBUNIT.
RX PubMed=11916384; DOI=10.1006/jmbi.2002.5397;
RA Favier A., Brutscher B., Blackledge M., Galinier A., Deutscher J.,
RA Penin F., Marion D.;
RT "Solution structure and dynamics of Crh, the Bacillus subtilis catabolite
RT repression HPr.";
RL J. Mol. Biol. 317:131-144(2002).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS).
RA Juy M.R., Bockmann A., Galinier A., Penin F., Haser R.;
RT "Crystal Structure at 1.8 A of the Bacillus subtilis catabolite repression
RT containing protein (Crh) reveals an unexpected swapping domain as an
RT untertwinned dimer.";
RL Submitted (SEP-2002) to the PDB data bank.
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS), AND MUTAGENESIS OF GLN-15.
RX PubMed=12972249; DOI=10.1016/s0022-2836(03)00918-5;
RA Juy M., Penin F., Favier A., Galinier A., Montserret R., Haser R.,
RA Deutscher J., Bockmann A.;
RT "Dimerization of Crh by reversible 3D domain swapping induces structural
RT adjustments to its monomeric homologue Hpr.";
RL J. Mol. Biol. 332:767-776(2003).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.98 ANGSTROMS) IN COMPLEX WITH CCPA, FUNCTION,
RP SUBUNIT, AND PHOSPHORYLATION AT SER-46.
RX PubMed=16316990; DOI=10.1074/jbc.m509977200;
RA Schumacher M.A., Seidel G., Hillen W., Brennan R.G.;
RT "Phosphoprotein Crh-Ser46-P displays altered binding to CcpA to effect
RT carbon catabolite regulation.";
RL J. Biol. Chem. 281:6793-6800(2006).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS), AND PHOSPHORYLATION AT SER-46.
RX PubMed=16411239; DOI=10.1002/prot.20816;
RA Chaptal V., Lariviere L., Gueguen-Chaignon V., Galinier A., Nessler S.,
RA Morera S.;
RT "X-ray structure of a domain-swapped dimer of Ser46-phosphorylated Crh from
RT Bacillus subtilis.";
RL Proteins 63:249-251(2006).
RN [9]
RP STRUCTURE BY NMR.
RX PubMed=18284240; DOI=10.1021/ja078014t;
RA Loquet A., Bardiaux B., Gardiennet C., Blanchet C., Baldus M., Nilges M.,
RA Malliavin T., Bockmann A.;
RT "3D structure determination of the Crh protein from highly ambiguous solid-
RT state NMR restraints.";
RL J. Am. Chem. Soc. 130:3579-3589(2008).
CC -!- FUNCTION: Along with seryl-phosphorylated HPr, phosphorylated Crh is
CC implicated in carbon catabolite repression (CCR) of levanase, inositol
CC dehydrogenase, and beta-xylosidase. Exerts its effect on CCR by
CC interacting with CcpA. {ECO:0000269|PubMed:16316990,
CC ECO:0000269|PubMed:9237995}.
CC -!- SUBUNIT: Mixture of monomers and homodimers. Interacts with CcpA as a
CC monomer. {ECO:0000269|PubMed:11916384, ECO:0000269|PubMed:16316990}.
CC -!- MISCELLANEOUS: Not phosphorylated by PEP and by enzyme I.
CC -!- SIMILARITY: Belongs to the HPr family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z94043; CAB08060.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15479.1; -; Genomic_DNA.
DR PIR; D69607; D69607.
DR RefSeq; NP_391354.1; NC_000964.3.
DR RefSeq; WP_003219835.1; NZ_JNCM01000033.1.
DR PDB; 1K1C; NMR; -; A=2-85.
DR PDB; 1MO1; X-ray; 1.80 A; A/B/C/D=1-85.
DR PDB; 1MU4; X-ray; 1.80 A; A/B=1-85.
DR PDB; 1ZVV; X-ray; 2.98 A; J/P/W=1-85.
DR PDB; 2AK7; X-ray; 2.00 A; A/B=1-85.
DR PDB; 2RLZ; NMR; -; A/B=1-85.
DR PDBsum; 1K1C; -.
DR PDBsum; 1MO1; -.
DR PDBsum; 1MU4; -.
DR PDBsum; 1ZVV; -.
DR PDBsum; 2AK7; -.
DR PDBsum; 2RLZ; -.
DR AlphaFoldDB; O06976; -.
DR BMRB; O06976; -.
DR SMR; O06976; -.
DR IntAct; O06976; 2.
DR STRING; 224308.BSU34740; -.
DR iPTMnet; O06976; -.
DR PaxDb; O06976; -.
DR PRIDE; O06976; -.
DR EnsemblBacteria; CAB15479; CAB15479; BSU_34740.
DR GeneID; 64305231; -.
DR GeneID; 938474; -.
DR KEGG; bsu:BSU34740; -.
DR PATRIC; fig|224308.179.peg.3762; -.
DR eggNOG; COG1925; Bacteria.
DR InParanoid; O06976; -.
DR OMA; MSLAIGH; -.
DR PhylomeDB; O06976; -.
DR BioCyc; BSUB:BSU34740-MON; -.
DR EvolutionaryTrace; O06976; -.
DR PRO; PR:O06976; -.
DR Proteomes; UP000001570; Chromosome.
DR CDD; cd00367; PTS-HPr_like; 1.
DR Gene3D; 3.30.1340.10; -; 1.
DR InterPro; IPR000032; HPr-like.
DR InterPro; IPR035895; HPr-like_sf.
DR InterPro; IPR002114; PTS_HPr_Ser_P_site.
DR Pfam; PF00381; PTS-HPr; 1.
DR PRINTS; PR00107; PHOSPHOCPHPR.
DR SUPFAM; SSF55594; SSF55594; 1.
DR TIGRFAMs; TIGR01003; PTS_HPr_family; 1.
DR PROSITE; PS51350; PTS_HPR_DOM; 1.
DR PROSITE; PS00589; PTS_HPR_SER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Phosphoprotein; Reference proteome.
FT CHAIN 1..85
FT /note="HPr-like protein Crh"
FT /id="PRO_0000107899"
FT DOMAIN 1..85
FT /note="HPr"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00681"
FT MOD_RES 46
FT /note="Phosphoserine; by HPrK/P"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00681,
FT ECO:0000269|PubMed:16316990, ECO:0000269|PubMed:16411239"
FT MUTAGEN 15
FT /note="Q->H: Cannot fulfill its catalytic role within PTS
FT transport. Does not affect dimerization."
FT /evidence="ECO:0000269|PubMed:12972249"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:1MO1"
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:1MO1"
FT HELIX 16..26
FT /evidence="ECO:0007829|PDB:1MO1"
FT STRAND 29..37
FT /evidence="ECO:0007829|PDB:1MO1"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:1MO1"
FT HELIX 47..52
FT /evidence="ECO:0007829|PDB:1MO1"
FT STRAND 60..67
FT /evidence="ECO:0007829|PDB:1MO1"
FT HELIX 70..81
FT /evidence="ECO:0007829|PDB:1MO1"
SQ SEQUENCE 85 AA; 9327 MW; 1801425F51B9B3F6 CRC64;
MVQQKVEVRL KTGLQARPAA LFVQEANRFT SDVFLEKDGK KVNAKSIMGL MSLAVSTGTE
VTLIAQGEDE QEALEKLAAY VQEEV
