| blob | 4a95f93e9c096eb6cf152ef68d6ed7e8c406db32 |
1 LOCUS P39765 181 aa linear BCT 03-MAR-2009
2 DEFINITION RecName: Full=Bifunctional protein pyrR; Includes: RecName:
3 Full=Pyrimidine operon regulatory protein; Includes: RecName:
4 Full=Uracil phosphoribosyltransferase; Short=UPRTase.
5 ACCESSION P39765
6 VERSION P39765.2 GI:20141743
7 DBSOURCE UniProtKB: locus PYRR_BACSU, accession P39765;
8 class: standard.
9 extra accessions:P25982,Q45483
10 created: Feb 1, 1995.
11 sequence updated: Jan 31, 2002.
12 annotation updated: Mar 3, 2009.
13 xrefs: M59757.2, AAA21265.2, Z99112.2, CAB13421.1, U48870.1,
14 AAB57770.1, B57986, NP_389430.1, 1A3C_A, 1A4X_A, 1A4X_B
15 xrefs (non-sequence databases): PDBsum:1A3C, PDBsum:1A4X,
16 GeneID:938030, GenomeReviews:AL009126_GR, KEGG:bsu:BSU15470,
17 NMPDR:fig|224308.1.peg.1549, SubtiList:BG10712, HOGENOM:P39765,
18 BioCyc:BSUB224308:BSU1549-MON, BRENDA:2.4.2.9, GO:0003723,
19 GO:0004845, GO:0009116, GO:0006355, GO:0006353, HAMAP:MF_01219,
20 InterPro:IPR000836, Pfam:PF00156, PROSITE:PS00103
21 KEYWORDS 3D-structure; Complete proteome; Glycosyltransferase; RNA-binding;
22 Transcription; Transcription regulation; Transcription termination;
23 Transferase.
24 SOURCE Bacillus subtilis
25 ORGANISM Bacillus subtilis
26 Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
27 REFERENCE 1 (residues 1 to 181)
28 AUTHORS Quinn,C.L., Stephenson,B.T. and Switzer,R.L.
29 TITLE Functional organization and nucleotide sequence of the Bacillus
30 subtilis pyrimidine biosynthetic operon
31 JOURNAL J. Biol. Chem. 266 (14), 9113-9127 (1991)
32 PUBMED 1709162
33 REMARK NUCLEOTIDE SEQUENCE [GENOMIC DNA].
34 STRAIN=1A610, and JH861
35 REFERENCE 2 (residues 1 to 181)
36 AUTHORS Turner,R.J., Lu,Y. and Switzer,R.L.
37 TITLE Regulation of the Bacillus subtilis pyrimidine biosynthetic (pyr)
38 gene cluster by an autogenous transcriptional attenuation mechanism
39 JOURNAL J. Bacteriol. 176 (12), 3708-3722 (1994)
40 PUBMED 8206849
41 REMARK SEQUENCE REVISION, AND CHARACTERIZATION.
42 REFERENCE 3 (residues 1 to 181)
43 AUTHORS Switzer,R.L.
44 TITLE Direct Submission
45 JOURNAL Submitted (??-MAY-1999)
46 REMARK SEQUENCE REVISION TO 34 AND 53.
47 REFERENCE 4 (residues 1 to 181)
48 AUTHORS Kunst,F., Ogasawara,N., Moszer,I., Albertini,A.M., Alloni,G.,
49 Azevedo,V., Bertero,M.G., Bessieres,P., Bolotin,A., Borchert,S.,
50 Borriss,R., Boursier,L., Brans,A., Braun,M., Brignell,S.C.,
51 Bron,S., Brouillet,S., Bruschi,C.V., Caldwell,B., Capuano,V.,
52 Carter,N.M., Choi,S.-K., Codani,J.-J., Connerton,I.F.,
53 Cummings,N.J., Daniel,R.A., Denizot,F., Devine,K.M.,
54 Duesterhoeft,A., Ehrlich,S.D., Emmerson,P.T., Entian,K.-D.,
55 Errington,J., Fabret,C., Ferrari,E., Foulger,D., Fritz,C.,
56 Fujita,M., Fujita,Y., Fuma,S., Galizzi,A., Galleron,N., Ghim,S.-Y.,
57 Glaser,P., Goffeau,A., Golightly,E.J., Grandi,G., Guiseppi,G.,
58 Guy,B.J., Haga,K., Haiech,J., Harwood,C.R., Henaut,A., Hilbert,H.,
59 Holsappel,S., Hosono,S., Hullo,M.-F., Itaya,M., Jones,L.-M.,
60 Joris,B., Karamata,D., Kasahara,Y., Klaerr-Blanchard,M., Klein,C.,
61 Kobayashi,Y., Koetter,P., Koningstein,G., Krogh,S., Kumano,M.,
62 Kurita,K., Lapidus,A., Lardinois,S., Lauber,J., Lazarevic,V.,
63 Lee,S.-M., Levine,A., Liu,H., Masuda,S., Mauel,C., Medigue,C.,
64 Medina,N., Mellado,R.P., Mizuno,M., Moestl,D., Nakai,S., Noback,M.,
65 Noone,D., O'Reilly,M., Ogawa,K., Ogiwara,A., Oudega,B., Park,S.-H.,
66 Parro,V., Pohl,T.M., Portetelle,D., Porwollik,S., Prescott,A.M.,
67 Presecan,E., Pujic,P., Purnelle,B., Rapoport,G., Rey,M.,
68 Reynolds,S., Rieger,M., Rivolta,C., Rocha,E., Roche,B., Rose,M.,
69 Sadaie,Y., Sato,T., Scanlan,E., Schleich,S., Schroeter,R.,
70 Scoffone,F., Sekiguchi,J., Sekowska,A., Seror,S.J., Serror,P.,
71 Shin,B.-S., Soldo,B., Sorokin,A., Tacconi,E., Takagi,T.,
72 Takahashi,H., Takemaru,K., Takeuchi,M., Tamakoshi,A., Tanaka,T.,
73 Terpstra,P., Tognoni,A., Tosato,V., Uchiyama,S., Vandenbol,M.,
74 Vannier,F., Vassarotti,A., Viari,A., Wambutt,R., Wedler,E.,
75 Wedler,H., Weitzenegger,T., Winters,P., Wipat,A., Yamamoto,H.,
76 Yamane,K., Yasumoto,K., Yata,K., Yoshida,K., Yoshikawa,H.-F.,
77 Zumstein,E., Yoshikawa,H. and Danchin,A.
78 TITLE The complete genome sequence of the gram-positive bacterium
79 Bacillus subtilis
80 JOURNAL Nature 390 (6657), 249-256 (1997)
81 PUBMED 9384377
82 REMARK NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
83 STRAIN=168
84 REFERENCE 5 (residues 1 to 181)
85 AUTHORS Pragai,Z., Tjalsma,H., Bolhuis,A., van Dijl,J.M., Venema,G. and
86 Bron,S.
87 TITLE The signal peptidase II (Isp) gene of Bacillus subtilis
88 JOURNAL Microbiology (Reading, Engl.) 143 (PT 4), 1327-1333 (1997)
89 PUBMED 9141696
90 REMARK NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-173.
91 STRAIN=168
92 REFERENCE 6 (residues 1 to 181)
93 AUTHORS Martinussen,J., Glaser,P., Andersen,P.S. and Saxild,H.H.
94 TITLE Two genes encoding uracil phosphoribosyltransferase are present in
95 Bacillus subtilis
96 JOURNAL J. Bacteriol. 177 (1), 271-274 (1995)
97 PUBMED 7798145
98 REMARK ENZYME ACTIVITY.
99 REFERENCE 7 (residues 1 to 181)
100 AUTHORS Turner,R.J., Bonner,E.R., Grabner,G.K. and Switzer,R.L.
101 TITLE Purification and characterization of Bacillus subtilis PyrR, a
102 bifunctional pyr mRNA-binding attenuation protein/uracil
103 phosphoribosyltransferase
104 JOURNAL J. Biol. Chem. 273 (10), 5932-5938 (1998)
105 PUBMED 9488732
106 REMARK CHARACTERIZATION, AND MASS SPECTROMETRY.
107 REFERENCE 8 (residues 1 to 181)
108 AUTHORS Savacool,H.K. and Switzer,R.L.
109 TITLE Characterization of the interaction of Bacillus subtilis PyrR with
110 pyr mRNA by site-directed mutagenesis of the protein
111 JOURNAL J. Bacteriol. 184 (9), 2521-2528 (2002)
112 PUBMED 11948166
113 REMARK MUTAGENESIS OF ARG-15; THR-18; ARG-19; HIS-22; ARG-27; THR-41;
114 HIS-140; ARG-141; ARG-146 AND LYS-152.
115 REFERENCE 9 (residues 1 to 181)
116 AUTHORS Tomchick,D.R., Turner,R.J., Switzer,R.L. and Smith,J.L.
117 TITLE Adaptation of an enzyme to regulatory function: structure of
118 Bacillus subtilis PyrR, a pyr RNA-binding attenuation protein and
119 uracil phosphoribosyltransferase
120 JOURNAL Structure 6 (3), 337-350 (1998)
121 PUBMED 9551555
122 REMARK X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
123 COMMENT On or before Sep 27, 2005 this sequence version replaced
124 gi:11376215, gi:730440.
125 [FUNCTION] Regulates transcriptional attenuation of the pyrimidine
126 nucleotide (pyr) operon by binding in a uridine-dependent manner to
127 specific sites on pyr mRNA. This disrupts an antiterminator hairpin
128 in the RNA and favors formation of a downstream transcription
129 terminator, leading to a reduced expression of downstream genes.
130 [FUNCTION] Also displays a weak uracil phosphoribosyltransferase
131 activity which is not physiologically significant.
132 [CATALYTIC ACTIVITY] UMP + diphosphate = uracil +
133 5-phospho-alpha-D-ribose 1-diphosphate.
134 [BIOPHYSICOCHEMICAL PROPERTIES] pH dependence: Optimum pH is 8.2
135 for UPRTase activity.
136 [SUBUNIT] Homodimer and homohexamer; in equilibrium.
137 [MASS SPECTROMETRY] Mass=20263; Mass_error=2; Method=Electrospray;
138 Range=1-181; Source=PubMed:9488732.
139 [MISCELLANEOUS] Mutagenesis studies identified four amino acid
140 residues that seem to be involved directly in binding of the
141 protein to pyr mRNA: Thr-18, His-22, Arg-141 and Arg-146. Arg-27
142 and Lys-152 were also likely to be involved in RNA-binding, but
143 mutations may have altered their subunit-subunit interactions.
144 Arg-19 was implicated in pyr regulation, but a specific role in
145 RNA-binding could not be demonstrated.
146 [MISCELLANEOUS] UMP and UTP incresase the affinity of pyrR for RNA.
147 [SIMILARITY] Belongs to the purine/pyrimidine
148 phosphoribosyltransferase family. PyrR subfamily.
149 FEATURES Location/Qualifiers
150 source 1..181
151 /organism="Bacillus subtilis"
152 /db_xref="taxon:1423"
153 gene 1..181
154 /gene="pyrR"
155 /locus_tag="BSU15470"
156 Protein 1..181
157 /gene="pyrR"
158 /locus_tag="BSU15470"
159 /product="Bifunctional protein pyrR"
160 /EC_number="2.4.2.9"
161 Region 1..181
162 /gene="pyrR"
163 /locus_tag="BSU15470"
164 /region_name="Mature chain"
165 /experiment="experimental evidence, no additional details
166 recorded"
167 /note="Bifunctional protein pyrR. /FTId=PRO_0000183030."
168 Region 3..179
169 /gene="pyrR"
170 /locus_tag="BSU15470"
171 /region_name="Pribosyltran"
172 /note="Phosphoribosyl transferase domain; cl00309"
173 /db_xref="CDD:119714"
174 Region 4..8
175 /gene="pyrR"
176 /locus_tag="BSU15470"
177 /region_name="Beta-strand region"
178 /experiment="experimental evidence, no additional details
179 recorded"
180 Region 10..28
181 /gene="pyrR"
182 /locus_tag="BSU15470"
183 /region_name="Helical region"
184 /experiment="experimental evidence, no additional details
185 recorded"
186 Site 15
187 /gene="pyrR"
188 /locus_tag="BSU15470"
189 /site_type="mutagenized"
190 /experiment="experimental evidence, no additional details
191 recorded"
192 /note="R->Q: No effect on ability to regulate the pyr
193 operon; no effect on uprtase activity."
194 Site 18
195 /gene="pyrR"
196 /locus_tag="BSU15470"
197 /site_type="mutagenized"
198 /experiment="experimental evidence, no additional details
199 recorded"
200 /note="T->A: No effect on ability to regulate the pyr
201 operon only in presence of excess pyrimidines; reduced
202 affinity for RNA; no effect on UPRTase activity."
203 Site 19
204 /gene="pyrR"
205 /locus_tag="BSU15470"
206 /site_type="mutagenized"
207 /experiment="experimental evidence, no additional details
208 recorded"
209 /note="R->Q: Loss of ability to regulate the pyr operon;
210 no effect on UPRTase activity."
211 Site 22
212 /gene="pyrR"
213 /locus_tag="BSU15470"
214 /site_type="mutagenized"
215 /experiment="experimental evidence, no additional details
216 recorded"
217 /note="H->A: Loss of ability to regulate the pyr operon
218 and to bind to RNA; no effect on UPRTase activity."
219 Site 27
220 /gene="pyrR"
221 /locus_tag="BSU15470"
222 /site_type="mutagenized"
223 /experiment="experimental evidence, no additional details
224 recorded"
225 /note="R->Q: No effect on ability to regulate the pyr
226 operon only in presence of excess pyrimidines; reduced
227 affinity for RNA; no effect on UPRTase activity."
228 Region 35..40
229 /gene="pyrR"
230 /locus_tag="BSU15470"
231 /region_name="Beta-strand region"
232 /experiment="experimental evidence, no additional details
233 recorded"
234 Region 41..58
235 /gene="pyrR"
236 /locus_tag="BSU15470"
237 /region_name="Helical region"
238 /experiment="experimental evidence, no additional details
239 recorded"
240 Region 41..42
241 /gene="pyrR"
242 /locus_tag="BSU15470"
243 /region_name="Region of interest in the sequence"
244 /inference="non-experimental evidence, no additional
245 details recorded"
246 /note="Substrate-binding (By similarity)."
247 Site 41
248 /gene="pyrR"
249 /locus_tag="BSU15470"
250 /site_type="mutagenized"
251 /experiment="experimental evidence, no additional details
252 recorded"
253 /note="T->I: Reduced ability to regulate the pyr operon;
254 reduced affinity for RNA; loss of UPRTase activity."
255 Region 63..70
256 /gene="pyrR"
257 /locus_tag="BSU15470"
258 /region_name="Beta-strand region"
259 /experiment="experimental evidence, no additional details
260 recorded"
261 Region 86..91
262 /gene="pyrR"
263 /locus_tag="BSU15470"
264 /region_name="Beta-strand region"
265 /experiment="experimental evidence, no additional details
266 recorded"
267 Region 99..111
268 /gene="pyrR"
269 /locus_tag="BSU15470"
270 /region_name="Beta-strand region"
271 /experiment="experimental evidence, no additional details
272 recorded"
273 Region 101..113
274 /gene="pyrR"
275 /locus_tag="BSU15470"
276 /region_name="Short sequence motif of biological interest"
277 /inference="non-experimental evidence, no additional
278 details recorded"
279 /note="PRPP-binding (By similarity)."
280 Region 105..113
281 /gene="pyrR"
282 /locus_tag="BSU15470"
283 /region_name="Region of interest in the sequence"
284 /inference="non-experimental evidence, no additional
285 details recorded"
286 /note="Substrate binding (By similarity)."
287 Region 112..124
288 /gene="pyrR"
289 /locus_tag="BSU15470"
290 /region_name="Helical region"
291 /experiment="experimental evidence, no additional details
292 recorded"
293 Region 128..137
294 /gene="pyrR"
295 /locus_tag="BSU15470"
296 /region_name="Beta-strand region"
297 /experiment="experimental evidence, no additional details
298 recorded"
299 Site 138
300 /gene="pyrR"
301 /locus_tag="BSU15470"
302 /site_type="binding"
303 /inference="non-experimental evidence, no additional
304 details recorded"
305 /note="Substrate (By similarity)."
306 Site 140
307 /gene="pyrR"
308 /locus_tag="BSU15470"
309 /site_type="mutagenized"
310 /experiment="experimental evidence, no additional details
311 recorded"
312 /note="H->A: Reduced ability to regulate the pyr operon;
313 decreased UPRTase activity."
314 Site 141
315 /gene="pyrR"
316 /locus_tag="BSU15470"
317 /site_type="mutagenized"
318 /experiment="experimental evidence, no additional details
319 recorded"
320 /note="R->Q: Loss of ability to regulate the pyr operon;
321 highly reduced affinity for RNA; no effect on UPRTase
322 activity."
323 Region 142..144
324 /gene="pyrR"
325 /locus_tag="BSU15470"
326 /region_name="Beta-strand region"
327 /experiment="experimental evidence, no additional details
328 recorded"
329 Site 146
330 /gene="pyrR"
331 /locus_tag="BSU15470"
332 /site_type="mutagenized"
333 /experiment="experimental evidence, no additional details
334 recorded"
335 /note="R->Q: Reduced ability to regulate the pyr operon,
336 and loss of ability to bind to RNA; no effect on UPRTase
337 activity."
338 Region 148..153
339 /gene="pyrR"
340 /locus_tag="BSU15470"
341 /region_name="Beta-strand region"
342 /experiment="experimental evidence, no additional details
343 recorded"
344 Site 152
345 /gene="pyrR"
346 /locus_tag="BSU15470"
347 /site_type="mutagenized"
348 /experiment="experimental evidence, no additional details
349 recorded"
350 /note="K->Q: No effect on ability to regulate the pyr
351 operon only in presence of excess pyrimidines; reduced
352 affinity for RNA; no effect on UPRTase activity."
353 Region 161..165
354 /gene="pyrR"
355 /locus_tag="BSU15470"
356 /region_name="Beta-strand region"
357 /experiment="experimental evidence, no additional details
358 recorded"
359 Site 162
360 /gene="pyrR"
361 /locus_tag="BSU15470"
362 /site_type="binding"
363 /inference="non-experimental evidence, no additional
364 details recorded"
365 /note="Substrate (By similarity)."
366 Region 167..170
367 /gene="pyrR"
368 /locus_tag="BSU15470"
369 /region_name="Helical region"
370 /experiment="experimental evidence, no additional details
371 recorded"
372 Region 174..178
373 /gene="pyrR"
374 /locus_tag="BSU15470"
375 /region_name="Beta-strand region"
376 /experiment="experimental evidence, no additional details
377 recorded"
378 ORIGIN
379 1 mnqkavilde qairraltri ahemiernkg mnncilvgik trgiylakrl aerieqiegn
380 61 pvtvgeidit lyrddlskkt sndeplvkga dipvditdqk vilvddvlyt grtvragmda
381 121 lvdvgrpssi qlavlvdrgh relpiradyi gkniptskse kvmvqldevd qndlvaiyen
382 181 e
383 //