Reviewed, UniProtKB/Swiss-Prot P37585 (MURG_BACSU)

Names and origin

Protein names

Recommended name:
    UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase
    EC=2.4.1.227
Alternative name(s):
    Undecaprenyl-PP-MurNAc-pentapeptide-UDPGlcNAc GlcNAc transferase

Gene names

Name:	murG
Ordered Locus Names:	BSU15220

Organism

Bacillus subtilis [Complete proteome] [HAMAP]

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	363 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II). HAMAP MF_00033
Catalytic activity	UDP-N-acetylglucosamine + Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol = UDP + GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol. HAMAP MF_00033
Pathway	Cell wall biogenesis; peptidoglycan biosynthesis. HAMAP MF_00033
Subcellular location	Cell membrane; Peripheral membrane protein By similarity.
Sequence similarities	Belongs to the glycosyltransferase 28 family. MurG subfamily.

Ontologies

Keywords
Biological process	Cell cycle Cell division Cell shape Cell wall biogenesis/degradation Peptidoglycan synthesis
Cellular component	Cell membrane Membrane
Molecular function	Glycosyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	UDP-N-acetylgalactosamine biosynthetic process Inferred from electronic annotation. Source: InterPro cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cell division Inferred from electronic annotation. Source: UniProtKB-KW cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW lipid glycosylation Inferred from electronic annotation. Source: HAMAP peptidoglycan biosynthetic process Inferred from electronic annotation. Source: HAMAP regulation of cell shape Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	Gram-negative-bacterium-type cell wall Inferred from electronic annotation. Source: InterPro extrinsic to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: HAMAP
Molecular function	carbohydrate binding Inferred from electronic annotation. Source: InterPro undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 363	363	UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase HAMAP MF_00033		PRO_0000109143
Experimental info
	Sequence conflict	181	1	G → K in CAA45558. Ref.2
	Sequence conflict	270	1	T → A in CAA45558. Ref.2
	Sequence conflict	270	1	T → A in AAA83968. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	P37585-1 [UniParc]. Last modified June 16, 2009. Version 3. Checksum: 99CB0A8FFC6B64B0	FASTA	363	39,936
	10 20 30 40 50 60 MRIAISGGGT GGHIYPALAF IKEVQRRHPN VEFLYIGTEN GLEKKIVERE NIPFRSIEIT 70 80 90 100 110 120 GFKRKLSFEN VKTVMRFLKG VKKSKSYLAE FKPDAVIGTG GYVCGPVVYA AAKMGIPTIV 130 140 150 160 170 180 HEQNSLPGIT NKFLSKYVNK VAICFEEAKS HFPSEKVVFT GNPRASEVVS IKTGRSLAEF 190 200 210 220 230 240 GLSEDKKTVL IFGGSRGAAP INRAVIDMQD VLKTRDYQVL YITGEVHYEK VMNELKSKGA 250 260 270 280 290 300 ADNMVTKPFL HQMPEYLKAI DVIVARAGAT TIAEITALGI PSVLIPSPYV TANHQEVNAR 310 320 330 340 350 360 SLGQHDAAIV LKETELSGEK LIEALDRIVL NEQTLKEMSE RTKSLGVPDA AARLYSVLEE LKK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence of the Bacillus subtilis homolog of the Escherichia coli cell-division gene murG." Miyao A., Yoshimura A., Sato T., Yamamoto T., Theeragool G., Kobayashi Y. Gene 118:147-148(1992) [PubMed: 1387377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"A Bacillus subtilis morphogene cluster that includes spoVE is homologous to the mra region of Escherichia coli." Henriques A.O., de Lencastre H., Piggot P.J. Biochimie 74:735-748(1992) [PubMed: 1391053] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[3]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." 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., Danchin A. Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[4]	"From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later." Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A. Microbiology 155:1758-1775(2009) [PubMed: 19383706] [Abstract] Cited for: SEQUENCE REVISION TO 181 AND 270.
[5]	"Nucleotide sequence and insertional inactivation of a Bacillus subtilis gene that affects cell division, sporulation, and temperature sensitivity." Beall B., Lutkenhaus J. J. Bacteriol. 171:6821-6834(1989) [PubMed: 2556375] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 216-363.

Cross-references

Sequence databases
EMBLGenBankDDBJ	D10602 Genomic DNA. Translation: BAA01454.1. X64259 Genomic DNA. Translation: CAA45558.1. AL009126 Genomic DNA. Translation: CAB13395.2. M31827 Genomic DNA. Translation: AAA83968.1.
PIR	JC1275. S25763.
RefSeq	NP_389405.2.
3D structure databases
HSSP	HSSP built from PDB template 1F0K based on UniProtKB P17443.
ModBase	Search...
Protein family/group databases
CAZy	GT28. Glycosyltransferase Family 28.
Genome annotation databases
GeneID	935929.
GenomeReviews	Gene locus BSU15220 in contig AL009126_GR.
KEGG	bsu:BSU15220.
Organism-specific databases
SubtiList	BG10227. murG. [Micado]
CMR	Search...
Phylogenomic databases
HOGENOM	P37585.
OMA	YVCGPVV.
Enzyme and pathway databases
BioCyc	BSUB224308:BSU1524-MON.
BRENDA	2.4.1.227. 150.
Family and domain databases
HAMAP	MF_00033. [Tree]
InterPro	IPR006009. GlcNAc_MurG. IPR004276. Glyco_trans_28. IPR007235. Glyco_trans_28_C. [Graphical view]
Pfam	PF04101. Glyco_tran_28_C. 1 hit. PF03033. Glyco_transf_28. 1 hit. [Graphical view]
TIGRFAMs	TIGR01133. murG. 1 hit.
ProtoNet	Search...

Entry information

Entry name

MURG_BACSU

Accession

Primary (citable) accession number: P37585
Secondary accession number(s): P18578, Q59247

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	June 16, 2009
Last modified:	November 3, 2009
This is version 82 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)