MURB_BACSU
ID MURB_BACSU Reviewed; 303 AA.
AC P18579; P16669; P37581;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=UDP-N-acetylenolpyruvoylglucosamine reductase;
DE EC=1.3.1.98;
DE AltName: Full=UDP-N-acetylmuramate dehydrogenase;
GN Name=murB; Synonyms=ylxC; OrderedLocusNames=BSU15230;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2556375; DOI=10.1128/jb.171.12.6821-6834.1989;
RA Beall B., Lutkenhaus J.;
RT "Nucleotide sequence and insertional inactivation of a Bacillus subtilis
RT gene that affects cell division, sporulation, and temperature
RT sensitivity.";
RL J. Bacteriol. 171:6821-6834(1989).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-23.
RX PubMed=1387377; DOI=10.1016/0378-1119(92)90264-p;
RA Miyao A., Yoshimura A., Sato T., Yamamoto T., Theeragool G., Kobayashi Y.;
RT "Sequence of the Bacillus subtilis homolog of the Escherichia coli cell-
RT division gene murG.";
RL Gene 118:147-148(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 250-303.
RX PubMed=2556376; DOI=10.1128/jb.171.12.6835-6839.1989;
RA Harry E.J., Wake R.G.;
RT "Cloning and expression of a Bacillus subtilis division initiation gene for
RT which a homolog has not been identified in another organism.";
RL J. Bacteriol. 171:6835-6839(1989).
RN [5]
RP FUNCTION.
RX PubMed=7590298; DOI=10.1016/0378-1119(95)00467-k;
RA Rowland S.L., Errington J., Wake R.G.;
RT "The Bacillus subtilis cell-division 135-137 degrees region contains an
RT essential orf with significant similarity to murB and a dispensable sbp
RT gene.";
RL Gene 164:113-116(1995).
CC -!- FUNCTION: Cell wall formation. {ECO:0000269|PubMed:7590298}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-
CC N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine;
CC Xref=Rhea:RHEA:12248, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:68483, ChEBI:CHEBI:70757; EC=1.3.1.98;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the MurB family. {ECO:0000305}.
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DR EMBL; M31827; AAA83969.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13396.1; -; Genomic_DNA.
DR EMBL; D10602; BAA01455.1; -; Genomic_DNA.
DR EMBL; M31800; AAA22392.1; -; Genomic_DNA.
DR PIR; S26500; A43727.
DR RefSeq; NP_389406.1; NC_000964.3.
DR RefSeq; WP_003232182.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; P18579; -.
DR SMR; P18579; -.
DR IntAct; P18579; 1.
DR MINT; P18579; -.
DR STRING; 224308.BSU15230; -.
DR jPOST; P18579; -.
DR PaxDb; P18579; -.
DR PRIDE; P18579; -.
DR EnsemblBacteria; CAB13396; CAB13396; BSU_15230.
DR GeneID; 939804; -.
DR KEGG; bsu:BSU15230; -.
DR PATRIC; fig|224308.179.peg.1661; -.
DR eggNOG; COG0812; Bacteria.
DR InParanoid; P18579; -.
DR OMA; KMNAGMK; -.
DR PhylomeDB; P18579; -.
DR BioCyc; BSUB:BSU15230-MON; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0008762; F:UDP-N-acetylmuramate dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0071555; P:cell wall organization; IBA:GO_Central.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR Gene3D; 3.30.43.10; -; 1.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.90.78.10; -; 1.
DR HAMAP; MF_00037; MurB; 1.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR003170; MurB.
DR InterPro; IPR011601; MurB_C.
DR InterPro; IPR036635; MurB_C_sf.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR PANTHER; PTHR21071; PTHR21071; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR Pfam; PF02873; MurB_C; 1.
DR SUPFAM; SSF56176; SSF56176; 1.
DR SUPFAM; SSF56194; SSF56194; 1.
DR TIGRFAMs; TIGR00179; murB; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 3: Inferred from homology;
KW Cell cycle; Cell division; Cell shape; Cell wall biogenesis/degradation;
KW Cytoplasm; FAD; Flavoprotein; NADP; Oxidoreductase;
KW Peptidoglycan synthesis; Reference proteome.
FT CHAIN 1..303
FT /note="UDP-N-acetylenolpyruvoylglucosamine reductase"
FT /id="PRO_0000179178"
FT DOMAIN 29..196
FT /note="FAD-binding PCMH-type"
FT ACT_SITE 174
FT /evidence="ECO:0000250"
FT ACT_SITE 225
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 295
FT /evidence="ECO:0000250"
SQ SEQUENCE 303 AA; 32808 MW; C33F5367C84E8A6E CRC64;
MEKVIQELKE REVGKVLANE PLANHTTMKI GGPADVLVIP SSVDAVKDIM DVIKKYDVKW
TVIGRGSNLL VLDEGIRGVV IKLGAGLDHL ELEGEQVTVG GGYSVVRLAT SLSKKGLSGL
EFAAGIPGSV GGAVYMNAGA HGSDMSEILV KAHILFEDGT IEWLTNEQMD FSYRTSVLQK
KRPGVCLEAV LQLEQKDKES IVQQMQSNKD YRKNTQPYSS PCAGSIFRNP LPNHAGNLVE
KAGLKGYQIG GAKISEMHGN FIVNAGGASA KDVLDLIDHV KKTIREKYEI DMHTEVEIIG
GNR
