ID LIAG_BACSU Reviewed; 290 AA. AC O32200; Q7B2J6; DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 14-APR-2009, sequence version 2. DT 22-FEB-2012, entry version 58. DE RecName: Full=Protein liaG; DE Flags: Precursor; GN Name=liaG; Synonyms=yvqG; OrderedLocusNames=BSU33110; OS Bacillus subtilis. OC Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1423; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=168; RX MEDLINE=98304083; PubMed=9639930; RA Wipat A., Brignell C.S., Guy J.B., Rose M., Emmerson P.T., RA Harwood C.R.; RT "The yvsA-yvqA (293 degrees - 289 degrees) region of the Bacillus RT subtilis chromosome containing genes involved in metal ion uptake and RT a putative sigma factor."; RL Microbiology 144:1593-1600(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=168; RX MEDLINE=98044033; PubMed=9384377; DOI=10.1038/36786; RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., RA Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., RA Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., RA Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M., RA Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., RA Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., RA Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., RA Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., RA Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., RA Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., RA Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., RA Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., RA Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., RA 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., RA Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., RA Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., RA Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., RA Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., RA Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., RA Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., RA Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., RA 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 SEQUENCE REVISION TO N-TERMINUS. RX PubMed=19383706; DOI=10.1099/mic.0.027839-0; RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., RA Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.; RT "From a consortium sequence to a unified sequence: the Bacillus RT subtilis 168 reference genome a decade later."; RL Microbiology 155:1758-1775(2009). RN [4] RP INDUCTION BY VANCOMYCIN. RC STRAIN=168 / CU1065; RX MEDLINE=22199418; PubMed=12207695; RX DOI=10.1046/j.1365-2958.2002.03050.x; RA Cao M., Wang T., Ye R., Helmann J.D.; RT "Antibiotics that inhibit cell wall biosynthesis induce expression of RT the Bacillus subtilis sigma(W) and sigma(M) regulons."; RL Mol. Microbiol. 45:1267-1276(2002). RN [5] RP INDUCTION BY BACITRACIN. RC STRAIN=168 / CU1065; RX PubMed=14651641; DOI=10.1046/j.1365-2958.2003.03786.x; RA Mascher T., Margulis N.G., Wang T., Ye R.W., Helmann J.D.; RT "Cell wall stress responses in Bacillus subtilis: the regulatory RT network of the bacitracin stimulon."; RL Mol. Microbiol. 50:1591-1604(2003). RN [6] RP INDUCTION BY ANTIBIOTICS. RX PubMed=15273097; DOI=10.1128/AAC.48.8.2888-2896.2004; RA Mascher T., Zimmer S.L., Smith T.-A., Helmann J.D.; RT "Antibiotic-inducible promoter regulated by the cell envelope stress- RT sensing two-component system LiaRS of Bacillus subtilis."; RL Antimicrob. Agents Chemother. 48:2888-2896(2004). RN [7] RP INDUCTION BY STRESS. RX PubMed=15856219; DOI=10.1007/s00253-005-1898-1; RA Hyyrylaeinen H.-L., Sarvas M., Kontinen V.P.; RT "Transcriptome analysis of the secretion stress response of Bacillus RT subtilis."; RL Appl. Microbiol. Biotechnol. 67:389-396(2005). RN [8] RP INDUCTION BY LL-37; PG-1 AND TRITON X-100. RC STRAIN=168; RX PubMed=15870467; DOI=10.1099/mic.0.27761-0; RA Pietiaeinen M., Gardemeister M., Mecklin M., Leskelae S., Sarvas M., RA Kontinen V.P.; RT "Cationic antimicrobial peptides elicit a complex stress response in RT Bacillus subtilis that involves ECF-type sigma factors and two- RT component signal transduction systems."; RL Microbiology 151:1577-1592(2005). RN [9] RP DISRUPTION PHENOTYPE. RC STRAIN=168; RX PubMed=17921301; DOI=10.1128/JB.01181-07; RA Butcher B.G., Lin Y.-P., Helmann J.D.; RT "The yydFGHIJ operon of Bacillus subtilis encodes a peptide that RT induces the LiaRS two-component system."; RL J. Bacteriol. 189:8616-8625(2007). CC -!- INDUCTION: Induced, via the two-component regulatory system CC liaS/liaR, by antibiotics (vancomycin, bacitracin, nisin and CC ramoplanin), cationic antimicrobial peptides (human LL-37 and CC porcine PG-1), Triton X-100 and severe secretion stress. CC -!- DISRUPTION PHENOTYPE: Upregulates expression of liaI which in turn CC induces the liaRS two-component regulatory system. CC -!- SEQUENCE CAUTION: CC Sequence=CAA11742.1; Type=Frameshift; Positions=32; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJ223978; CAA11742.1; ALT_FRAME; Genomic_DNA. DR EMBL; AL009126; CAB15301.2; -; Genomic_DNA. DR PIR; H70045; H70045. DR RefSeq; NP_391191.2; NC_000964.3. DR ProteinModelPortal; O32200; -. DR EnsemblBacteria; EBBACT00000000990; EBBACP00000000990; EBBACG00000000988. DR GeneID; 938471; -. DR GenomeReviews; AL009126_GR; BSU33110. DR KEGG; bsu:BSU33110; -. DR PATRIC; 18978610; VBIBacSub10457_3468. DR GenoList; BSU33110; -. DR eggNOG; COG3595; -. DR HOGENOM; HBG338307; -. DR KO; K11621; -. DR ProtClustDB; CLSK887858; -. DR BioCyc; BSUB:BSU33110-MONOMER; -. DR GO; GO:0006950; P:response to stress; IEA:UniProtKB-KW. PE 2: Evidence at transcript level; KW Complete proteome; Reference proteome; Signal; Stress response. FT SIGNAL 1 27 Potential. FT CHAIN 28 290 Protein liaG. FT /FTId=PRO_0000084415. SQ SEQUENCE 290 AA; 30262 MW; 214584684EF570F7 CRC64; MKKMLGKLLI TAGILVFFAV VVKDVFAAGL GFINGTEADS ASASPRDIDS MVIESDSKDV RIIAEERSDI SAGISGDSGK LFVTENKRKL ELTVKEKEFQ FLNGFNRSTL IVRLPYDYKG DLAVRTSSGD VSVAGNDHLA LSGLNAVSAS GNTSVTDVRI QDLKVKASSG DVSISNTVSK TAGIDLASGD ANLVHVSGSL DVKMTSGDFN AVLKKVTGPV SVTLTSGDAN VSLPQNGSFA VNALSASGDV SSPYSFADKG HKEQHHITGT QGSGRHPIDI KTDSGDLAIR // ID GLSA1_BACSU Reviewed; 327 AA. AC O31465; DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 22-FEB-2012, entry version 85. DE RecName: Full=Glutaminase 1; DE EC=3.5.1.2; GN Name=glsA1; Synonyms=glsA, ybgJ; OrderedLocusNames=BSU02430; OS Bacillus subtilis. OC Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1423; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=168; RA Haga K., Liu H., Yasumoto K., Takahashi H., Yoshikawa H.; RT "Sequence analysis of the 70kb region between 17 and 23 degree of the RT Bacillus subtilis chromosome."; RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=168; RX MEDLINE=98044033; PubMed=9384377; DOI=10.1038/36786; RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., RA Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., RA Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., RA Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M., RA Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., RA Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., RA Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., RA Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., RA Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., RA Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., RA Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., RA Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., RA Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., RA 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., RA Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., RA Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., RA Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., RA Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., RA Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., RA Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., RA Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., RA 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 GENE NAME. RC STRAIN=168; RX PubMed=15995196; DOI=10.1128/JB.187.14.4813-4821.2005; RA Satomura T., Shimura D., Asai K., Sadaie Y., Hirooka K., Fujita Y.; RT "Enhancement of glutamine utilization in Bacillus subtilis through the RT GlnK-GlnL two-component regulatory system."; RL J. Bacteriol. 187:4813-4821(2005). CC -!- CATALYTIC ACTIVITY: L-glutamine + H(2)O = L-glutamate + NH(3). CC -!- SIMILARITY: Belongs to the glutaminase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB006424; BAA33141.1; -; Genomic_DNA. DR EMBL; AL009126; CAB12037.1; -; Genomic_DNA. DR PIR; D69751; D69751. DR RefSeq; NP_388125.1; NC_000964.3. DR PDB; 1MKI; X-ray; 2.00 A; A/B=1-327. DR PDB; 2OSU; X-ray; 2.29 A; A/B=1-327. DR PDB; 3AGF; X-ray; 2.60 A; A/B=1-327. DR PDB; 3BRM; X-ray; 2.29 A; A/B=1-327. DR PDBsum; 1MKI; -. DR PDBsum; 2OSU; -. DR PDBsum; 3AGF; -. DR PDBsum; 3BRM; -. DR ProteinModelPortal; O31465; -. DR SMR; O31465; 1-327. DR EnsemblBacteria; EBBACT00000000712; EBBACP00000000712; EBBACG00000000710. DR GeneID; 938416; -. DR GenomeReviews; AL009126_GR; BSU02430. DR KEGG; bsu:BSU02430; -. DR PATRIC; 18972037; VBIBacSub10457_0247. DR GenoList; BSU02430; -. DR eggNOG; COG2066; -. DR HOGENOM; HBG512335; -. DR KO; K01425; -. DR OMA; KNDEERF; -. DR PhylomeDB; O31465; -. DR ProtClustDB; PRK12357; -. DR BioCyc; BSUB:BSU02430-MONOMER; -. DR GO; GO:0004359; F:glutaminase activity; IEA:EC. DR GO; GO:0006541; P:glutamine metabolic process; IEA:InterPro. DR HAMAP; MF_00313; Glutaminase; 1; -. DR InterPro; IPR012338; Beta-lactam/transpept-like. DR InterPro; IPR015868; Glutaminase. DR Gene3D; G3DSA:3.40.710.20; Glutaminase_core; 2. DR PANTHER; PTHR12544; Glutaminase; 1. DR Pfam; PF04960; Glutaminase; 1. DR SUPFAM; SSF56601; PBP_transp_fold; 1. DR TIGRFAMs; TIGR03814; Gln_ase; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Hydrolase; Reference proteome. FT CHAIN 1 327 Glutaminase 1. FT /FTId=PRO_0000110594. FT HELIX 14 25 FT HELIX 26 31 FT STRAND 50 54 FT STRAND 60 65 FT HELIX 73 75 FT HELIX 76 88 FT HELIX 90 94 FT HELIX 110 114 FT STRAND 123 125 FT HELIX 126 135 FT STRAND 136 140 FT HELIX 141 156 FT HELIX 164 173 FT HELIX 175 186 FT HELIX 194 205 FT STRAND 207 209 FT HELIX 211 222 FT TURN 223 225 FT TURN 228 231 FT HELIX 237 250 FT HELIX 253 255 FT HELIX 256 262 FT STRAND 267 269 FT STRAND 273 279 FT TURN 281 284 FT TURN 288 291 FT STRAND 293 298 FT STRAND 306 308 FT HELIX 309 322 SQ SEQUENCE 327 AA; 36187 MW; BE3A1C2366460287 CRC64; MKELIKEHQK DINPALQLHD WVEYYRPFAA NGQSANYIPA LGKVNDSQLG ICVLEPDGTM IHAGDWNVSF TMQSISKVIS FIAACMSRGI PYVLDRVDVE PTGDAFNSII RLEINKPGKP FNPMINAGAL TIASILPGES AYEKLEFLYS VMETLIGKRP RIHEEVFRSE WETAHRNRAL AYYLKETNFL EAEVEETLEV YLKQCAMEST TEDIALIGLI LAHDGYHPIR HEQVIPKDVA KLAKALMLTC GMYNASGKYA AFVGVPAKSG VSGGIMALVP PSARREQPFQ SGCGIGIYGP AIDEYGNSLT GGMLLKHMAQ EWELSIF //