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LOCUS P39765 181 aa linear BCT 03-MAR-2009
DEFINITION RecName: Full=Bifunctional protein pyrR; Includes: RecName:
Full=Pyrimidine operon regulatory protein; Includes: RecName:
Full=Uracil phosphoribosyltransferase; Short=UPRTase.
ACCESSION P39765
VERSION P39765.2 GI:20141743
DBSOURCE UniProtKB: locus PYRR_BACSU, accession P39765;
class: standard.
extra accessions:P25982,Q45483
created: Feb 1, 1995.
sequence updated: Jan 31, 2002.
annotation updated: Mar 3, 2009.
xrefs: M59757.2, AAA21265.2, Z99112.2, CAB13421.1, U48870.1,
AAB57770.1, B57986, NP_389430.1, 1A3C_A, 1A4X_A, 1A4X_B
xrefs (non-sequence databases): PDBsum:1A3C, PDBsum:1A4X,
GeneID:938030, GenomeReviews:AL009126_GR, KEGG:bsu:BSU15470,
NMPDR:fig|224308.1.peg.1549, SubtiList:BG10712, HOGENOM:P39765,
BioCyc:BSUB224308:BSU1549-MON, BRENDA:2.4.2.9, GO:0003723,
GO:0004845, GO:0009116, GO:0006355, GO:0006353, HAMAP:MF_01219,
InterPro:IPR000836, Pfam:PF00156, PROSITE:PS00103
KEYWORDS 3D-structure; Complete proteome; Glycosyltransferase; RNA-binding;
Transcription; Transcription regulation; Transcription termination;
Transferase.
SOURCE Bacillus subtilis
ORGANISM Bacillus subtilis
Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
REFERENCE 1 (residues 1 to 181)
AUTHORS Quinn,C.L., Stephenson,B.T. and Switzer,R.L.
TITLE Functional organization and nucleotide sequence of the Bacillus
subtilis pyrimidine biosynthetic operon
JOURNAL J. Biol. Chem. 266 (14), 9113-9127 (1991)
PUBMED 1709162
REMARK NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=1A610, and JH861
REFERENCE 2 (residues 1 to 181)
AUTHORS Turner,R.J., Lu,Y. and Switzer,R.L.
TITLE Regulation of the Bacillus subtilis pyrimidine biosynthetic (pyr)
gene cluster by an autogenous transcriptional attenuation mechanism
JOURNAL J. Bacteriol. 176 (12), 3708-3722 (1994)
PUBMED 8206849
REMARK SEQUENCE REVISION, AND CHARACTERIZATION.
REFERENCE 3 (residues 1 to 181)
AUTHORS Switzer,R.L.
TITLE Direct Submission
JOURNAL Submitted (??-MAY-1999)
REMARK SEQUENCE REVISION TO 34 AND 53.
REFERENCE 4 (residues 1 to 181)
AUTHORS 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. and Danchin,A.
TITLE The complete genome sequence of the gram-positive bacterium
Bacillus subtilis
JOURNAL Nature 390 (6657), 249-256 (1997)
PUBMED 9384377
REMARK NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=168
REFERENCE 5 (residues 1 to 181)
AUTHORS Pragai,Z., Tjalsma,H., Bolhuis,A., van Dijl,J.M., Venema,G. and
Bron,S.
TITLE The signal peptidase II (Isp) gene of Bacillus subtilis
JOURNAL Microbiology (Reading, Engl.) 143 (PT 4), 1327-1333 (1997)
PUBMED 9141696
REMARK NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-173.
STRAIN=168
REFERENCE 6 (residues 1 to 181)
AUTHORS Martinussen,J., Glaser,P., Andersen,P.S. and Saxild,H.H.
TITLE Two genes encoding uracil phosphoribosyltransferase are present in
Bacillus subtilis
JOURNAL J. Bacteriol. 177 (1), 271-274 (1995)
PUBMED 7798145
REMARK ENZYME ACTIVITY.
REFERENCE 7 (residues 1 to 181)
AUTHORS Turner,R.J., Bonner,E.R., Grabner,G.K. and Switzer,R.L.
TITLE Purification and characterization of Bacillus subtilis PyrR, a
bifunctional pyr mRNA-binding attenuation protein/uracil
phosphoribosyltransferase
JOURNAL J. Biol. Chem. 273 (10), 5932-5938 (1998)
PUBMED 9488732
REMARK CHARACTERIZATION, AND MASS SPECTROMETRY.
REFERENCE 8 (residues 1 to 181)
AUTHORS Savacool,H.K. and Switzer,R.L.
TITLE Characterization of the interaction of Bacillus subtilis PyrR with
pyr mRNA by site-directed mutagenesis of the protein
JOURNAL J. Bacteriol. 184 (9), 2521-2528 (2002)
PUBMED 11948166
REMARK MUTAGENESIS OF ARG-15; THR-18; ARG-19; HIS-22; ARG-27; THR-41;
HIS-140; ARG-141; ARG-146 AND LYS-152.
REFERENCE 9 (residues 1 to 181)
AUTHORS Tomchick,D.R., Turner,R.J., Switzer,R.L. and Smith,J.L.
TITLE Adaptation of an enzyme to regulatory function: structure of
Bacillus subtilis PyrR, a pyr RNA-binding attenuation protein and
uracil phosphoribosyltransferase
JOURNAL Structure 6 (3), 337-350 (1998)
PUBMED 9551555
REMARK X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
COMMENT On or before Sep 27, 2005 this sequence version replaced
gi:11376215, gi:730440.
[FUNCTION] Regulates transcriptional attenuation of the pyrimidine
nucleotide (pyr) operon by binding in a uridine-dependent manner to
specific sites on pyr mRNA. This disrupts an antiterminator hairpin
in the RNA and favors formation of a downstream transcription
terminator, leading to a reduced expression of downstream genes.
[FUNCTION] Also displays a weak uracil phosphoribosyltransferase
activity which is not physiologically significant.
[CATALYTIC ACTIVITY] UMP + diphosphate = uracil +
5-phospho-alpha-D-ribose 1-diphosphate.
[BIOPHYSICOCHEMICAL PROPERTIES] pH dependence: Optimum pH is 8.2
for UPRTase activity.
[SUBUNIT] Homodimer and homohexamer; in equilibrium.
[MASS SPECTROMETRY] Mass=20263; Mass_error=2; Method=Electrospray;
Range=1-181; Source=PubMed:9488732.
[MISCELLANEOUS] Mutagenesis studies identified four amino acid
residues that seem to be involved directly in binding of the
protein to pyr mRNA: Thr-18, His-22, Arg-141 and Arg-146. Arg-27
and Lys-152 were also likely to be involved in RNA-binding, but
mutations may have altered their subunit-subunit interactions.
Arg-19 was implicated in pyr regulation, but a specific role in
RNA-binding could not be demonstrated.
[MISCELLANEOUS] UMP and UTP incresase the affinity of pyrR for RNA.
[SIMILARITY] Belongs to the purine/pyrimidine
phosphoribosyltransferase family. PyrR subfamily.
FEATURES Location/Qualifiers
source 1..181
/organism="Bacillus subtilis"
/db_xref="taxon:1423"
gene 1..181
/gene="pyrR"
/locus_tag="BSU15470"
Protein 1..181
/gene="pyrR"
/locus_tag="BSU15470"
/product="Bifunctional protein pyrR"
/EC_number="2.4.2.9"
Region 1..181
/gene="pyrR"
/locus_tag="BSU15470"
/region_name="Mature chain"
/experiment="experimental evidence, no additional details
recorded"
/note="Bifunctional protein pyrR. /FTId=PRO_0000183030."
Region 3..179
/gene="pyrR"
/locus_tag="BSU15470"
/region_name="Pribosyltran"
/note="Phosphoribosyl transferase domain; cl00309"
/db_xref="CDD:119714"
Region 4..8
/gene="pyrR"
/locus_tag="BSU15470"
/region_name="Beta-strand region"
/experiment="experimental evidence, no additional details
recorded"
Region 10..28
/gene="pyrR"
/locus_tag="BSU15470"
/region_name="Helical region"
/experiment="experimental evidence, no additional details
recorded"
Site 15
/gene="pyrR"
/locus_tag="BSU15470"
/site_type="mutagenized"
/experiment="experimental evidence, no additional details
recorded"
/note="R->Q: No effect on ability to regulate the pyr
operon; no effect on uprtase activity."
Site 18
/gene="pyrR"
/locus_tag="BSU15470"
/site_type="mutagenized"
/experiment="experimental evidence, no additional details
recorded"
/note="T->A: No effect on ability to regulate the pyr
operon only in presence of excess pyrimidines; reduced
affinity for RNA; no effect on UPRTase activity."
Site 19
/gene="pyrR"
/locus_tag="BSU15470"
/site_type="mutagenized"
/experiment="experimental evidence, no additional details
recorded"
/note="R->Q: Loss of ability to regulate the pyr operon;
no effect on UPRTase activity."
Site 22
/gene="pyrR"
/locus_tag="BSU15470"
/site_type="mutagenized"
/experiment="experimental evidence, no additional details
recorded"
/note="H->A: Loss of ability to regulate the pyr operon
and to bind to RNA; no effect on UPRTase activity."
Site 27
/gene="pyrR"
/locus_tag="BSU15470"
/site_type="mutagenized"
/experiment="experimental evidence, no additional details
recorded"
/note="R->Q: No effect on ability to regulate the pyr
operon only in presence of excess pyrimidines; reduced
affinity for RNA; no effect on UPRTase activity."
Region 35..40
/gene="pyrR"
/locus_tag="BSU15470"
/region_name="Beta-strand region"
/experiment="experimental evidence, no additional details
recorded"
Region 41..58
/gene="pyrR"
/locus_tag="BSU15470"
/region_name="Helical region"
/experiment="experimental evidence, no additional details
recorded"
Region 41..42
/gene="pyrR"
/locus_tag="BSU15470"
/region_name="Region of interest in the sequence"
/inference="non-experimental evidence, no additional
details recorded"
/note="Substrate-binding (By similarity)."
Site 41
/gene="pyrR"
/locus_tag="BSU15470"
/site_type="mutagenized"
/experiment="experimental evidence, no additional details
recorded"
/note="T->I: Reduced ability to regulate the pyr operon;
reduced affinity for RNA; loss of UPRTase activity."
Region 63..70
/gene="pyrR"
/locus_tag="BSU15470"
/region_name="Beta-strand region"
/experiment="experimental evidence, no additional details
recorded"
Region 86..91
/gene="pyrR"
/locus_tag="BSU15470"
/region_name="Beta-strand region"
/experiment="experimental evidence, no additional details
recorded"
Region 99..111
/gene="pyrR"
/locus_tag="BSU15470"
/region_name="Beta-strand region"
/experiment="experimental evidence, no additional details
recorded"
Region 101..113
/gene="pyrR"
/locus_tag="BSU15470"
/region_name="Short sequence motif of biological interest"
/inference="non-experimental evidence, no additional
details recorded"
/note="PRPP-binding (By similarity)."
Region 105..113
/gene="pyrR"
/locus_tag="BSU15470"
/region_name="Region of interest in the sequence"
/inference="non-experimental evidence, no additional
details recorded"
/note="Substrate binding (By similarity)."
Region 112..124
/gene="pyrR"
/locus_tag="BSU15470"
/region_name="Helical region"
/experiment="experimental evidence, no additional details
recorded"
Region 128..137
/gene="pyrR"
/locus_tag="BSU15470"
/region_name="Beta-strand region"
/experiment="experimental evidence, no additional details
recorded"
Site 138
/gene="pyrR"
/locus_tag="BSU15470"
/site_type="binding"
/inference="non-experimental evidence, no additional
details recorded"
/note="Substrate (By similarity)."
Site 140
/gene="pyrR"
/locus_tag="BSU15470"
/site_type="mutagenized"
/experiment="experimental evidence, no additional details
recorded"
/note="H->A: Reduced ability to regulate the pyr operon;
decreased UPRTase activity."
Site 141
/gene="pyrR"
/locus_tag="BSU15470"
/site_type="mutagenized"
/experiment="experimental evidence, no additional details
recorded"
/note="R->Q: Loss of ability to regulate the pyr operon;
highly reduced affinity for RNA; no effect on UPRTase
activity."
Region 142..144
/gene="pyrR"
/locus_tag="BSU15470"
/region_name="Beta-strand region"
/experiment="experimental evidence, no additional details
recorded"
Site 146
/gene="pyrR"
/locus_tag="BSU15470"
/site_type="mutagenized"
/experiment="experimental evidence, no additional details
recorded"
/note="R->Q: Reduced ability to regulate the pyr operon,
and loss of ability to bind to RNA; no effect on UPRTase
activity."
Region 148..153
/gene="pyrR"
/locus_tag="BSU15470"
/region_name="Beta-strand region"
/experiment="experimental evidence, no additional details
recorded"
Site 152
/gene="pyrR"
/locus_tag="BSU15470"
/site_type="mutagenized"
/experiment="experimental evidence, no additional details
recorded"
/note="K->Q: No effect on ability to regulate the pyr
operon only in presence of excess pyrimidines; reduced
affinity for RNA; no effect on UPRTase activity."
Region 161..165
/gene="pyrR"
/locus_tag="BSU15470"
/region_name="Beta-strand region"
/experiment="experimental evidence, no additional details
recorded"
Site 162
/gene="pyrR"
/locus_tag="BSU15470"
/site_type="binding"
/inference="non-experimental evidence, no additional
details recorded"
/note="Substrate (By similarity)."
Region 167..170
/gene="pyrR"
/locus_tag="BSU15470"
/region_name="Helical region"
/experiment="experimental evidence, no additional details
recorded"
Region 174..178
/gene="pyrR"
/locus_tag="BSU15470"
/region_name="Beta-strand region"
/experiment="experimental evidence, no additional details
recorded"
ORIGIN
1 mnqkavilde qairraltri ahemiernkg mnncilvgik trgiylakrl aerieqiegn
61 pvtvgeidit lyrddlskkt sndeplvkga dipvditdqk vilvddvlyt grtvragmda
121 lvdvgrpssi qlavlvdrgh relpiradyi gkniptskse kvmvqldevd qndlvaiyen
181 e
//
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