Reviewed, UniProtKB/Swiss-Prot Q89AQ1 (MURF_BUCBP)

Names and origin

Protein names

Recommended name:
    UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase
    EC=6.3.2.10
Alternative name(s):
    UDP-MurNAc-pentapeptide synthetase
    D-alanyl-D-alanine-adding enzyme

Gene names

Name:	murF
Ordered Locus Names:	bbp_202

Organism

Buchnera aphidicola subsp. Baizongia pistaciae [Complete proteome] [HAMAP]

Taxonomic identifier

135842 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera

Protein attributes

Sequence length	460 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Involved in cell wall formation. Catalyzes the final step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the precursor of murein By similarity.
Catalytic activity	ATP + UDP-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-L-lysine + D-alanyl-D-alanine = ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-alanine.
Pathway	Cell wall biogenesis; peptidoglycan biosynthesis.
Subunit structure	Monomer By similarity.
Subcellular location	Cytoplasm Probable.
Sequence similarities	Belongs to the murCDEF family.

Ontologies

Keywords
Biological process	Cell cycle Cell division Cell shape Cell wall biogenesis/degradation Peptidoglycan synthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	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 peptidoglycan biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW regulation of cell shape Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase activity Inferred from electronic annotation. Source: EC UDP-N-acetylmuramoylalanyl-D-glutamyl-2,6-diaminopimelate-D-alanyl-D-alanine ligase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 460	460	UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase		PRO_0000101697
Regions
	Nucleotide binding	115 – 121	7	ATP Potential

Sequences

	Sequence		Length	Mass (Da)
	Q89AQ1-1 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: A0C2DE8052949E2C	FASTA	460	51,092
	10 20 30 40 50 60 MISINLIKLT SITNGILYCS NYATLHSISI HSITTDTRKI TPKCLFIALI GKNFDAHMFV 70 80 90 100 110 120 NEAISKGAAA LLLEKQCYPK NVIPQIIVQN TTIALGKIAS WIRDQTNATV IAITGSSGKT 130 140 150 160 170 180 SVKEMTSSIL KNCGNTISTF QNLNNNIGVP LTLLNLNKSH KYAILELGAN YPKDIEYTTK 190 200 210 220 230 240 ITKPNIALIN NIYHSHLAGF KSLFGVAQAK QEIFLGLRKN GIAIYNKDSN YWSKWKKNLL 250 260 270 280 290 300 TQKIINFSIK KNSTIFASNI TTSNQGSKFK IHSPNGEIYV TLPLLGYHNI SNALAAATIA 310 320 330 340 350 360 ISINIPLEII KIGLSSLPIL KNRLQIIRLN KYKTIINDTY NANTASMIVA IKILENISGY 370 380 390 400 410 420 KLFVAGDMLE LGKNDVLYHK IIGNTIYNSN INEVFSIGKL SKEISIASKK GHHFYNSDEL 430 440 450 460 LKNLKNKLLN KKIITILVKA SRSEKLDVIV EQLIKEYHKA

References

[1]

"Reductive genome evolution in Buchnera aphidicola." van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F., Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J., Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A. Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003) [PubMed: 12522265] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE016826 Genomic DNA. Translation: AAO26934.1.
RefSeq	NP_777829.1.
3D structure databases
HSSP	HSSP built from PDB template 1GG4 based on UniProtKB P11880.
ModBase	Search...
Genome annotation databases
GeneID	1058402.
GenomeReviews	Gene locus bbp_202 in contig AE016826_GR.
KEGG	bab:bbp202.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q89AQ1.
OMA	Q89AQ1. LDDTYNA.
Enzyme and pathway databases
BioCyc	BAPH224915:BBP_202-MON.
Family and domain databases
InterPro	IPR004101. Mur_ligase_C. IPR013221. Mur_ligase_cen. IPR000713. Mur_ligase_N. IPR005863. UDP-N-AcMur-3pep_AlaAla_ligase. [Graphical view]
Gene3D	G3DSA:3.90.190.20. Mur_ligase_C. 1 hit. G3DSA:3.40.1190.10. Mur_ligase_cen. 1 hit.
PANTHER	PTHR23135:SF3. MurF. 1 hit.
Pfam	PF01225. Mur_ligase. 1 hit. PF02875. Mur_ligase_C. 1 hit. PF08245. Mur_ligase_M. 1 hit. [Graphical view]
TIGRFAMs	TIGR01143. murF. 1 hit.
ProtoNet	Search...

Entry information

Entry name

MURF_BUCBP

Accession

Primary (citable) accession number: Q89AQ1

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 13, 2004
Last sequence update:	June 1, 2003
Last modified:	June 16, 2009
This is version 45 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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