Reviewed, UniProtKB/Swiss-Prot Q44777 (MURF_BORBU)

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:	BB_0304

Organism

Borrelia burgdorferi (Lyme disease spirochete) [Complete proteome] [HAMAP]

Taxonomic identifier

139 [NCBI]

Taxonomic lineage

Bacteria › Spirochaetes › Spirochaetales › Spirochaetaceae › Borrelia › Borrelia burgdorferi group

Protein attributes

Sequence length	464 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.
Subcellular location	Cytoplasm By similarity.
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 – 464	464	UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase		PRO_0000101695
Regions
	Nucleotide binding	125 – 131	7	ATP Potential
Experimental info
	Sequence conflict	462 – 464	3	IFR → YI in AAA85627. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q44777-1 [UniParc]. Last modified December 15, 1998. Version 2. Checksum: 29038B0C533799BC	FASTA	464	53,446
	10 20 30 40 50 60 MRIKIKDILI SSKDVKFVGN IKNIERVVSF YSLDSREIKD DNINDSLYFA YKGNKVDGFS 70 80 90 100 110 120 FVKYLIDLGV KCFACSREHE SECIKYLNDN EGLVFLLTSN VIKLLQALAS FLIEKTSFKR 130 140 150 160 170 180 IAITGSNGKT TTKEMLYSIL SKKYKTYKTW GNLNSDIGLP LSILRVEGNE EYAVFEVGVS 190 200 210 220 230 240 YVGEMDLLSQ ILKPEIVIIT NISYAHMQAF KELQAIAFEK SKIIGKNIEI FVVNEMNDYC 250 260 270 280 290 300 VYLEKRAKIA NPNVKIVYFD FENLSIKSFS FLDGKFSFDF VYKGFEYSIL LLGRHNIFNA 310 320 330 340 350 360 IGCINLALFL GMREKEIKEG LIETAFQKGR AEILTKNGYL ILNDSYNGNM GSFMALKNMI 370 380 390 400 410 420 LDLNIQNKKF IVLGSFKELG ELAYKTHKDL IQEAISMNFD KIFLIGEEFL DVRDSENLVE 430 440 450 460 KCLYYFSEFD KFIDFFLKSL EPSVFIVIKG SRFNRLERIL NIFR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi." Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A., Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L., Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L., Peterson J.D., Kerlavage A.R., Quackenbush J. , Salzberg S.L., Hanson M., van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F., Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C., Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B., Smith H.O., Venter J.C. Nature 390:580-586(1997) [PubMed: 9403685] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 35210 / B31 / CIP 102532 / DSM 4680.
[2]	Dunn J.J., Butler-Loffredo L., Kieleczawa J., Medalle J., Luft B.J. Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 67-464. Strain: ATCC 35210 / B31 / CIP 102532 / DSM 4680.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE000783 Genomic DNA. Translation: AAC66644.1. U43739 Genomic DNA. Translation: AAA85627.1.
PIR	H70137.
RefSeq	NP_212438.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	1195141.
GenomeReviews	Gene locus BB_0304 in contig AE000783_GR.
KEGG	bbu:BB0304.
NMPDR	fig|224326.1.peg.688.
TIGR	BB_0304.
Phylogenomic databases
HOGENOM	Q44777.
OMA	Q44777. VEGNEEY.
Enzyme and pathway databases
BioCyc	BBUR224326:BB_0304-MON.
BRENDA	6.3.2.10. 142596.
Family and domain databases
InterPro	IPR004101. Mur_ligase_C. IPR013221. Mur_ligase_cen. 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	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_BORBU

Accession

Primary (citable) accession number: Q44777
Secondary accession number(s): O51284

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	December 15, 1998
Last modified:	June 16, 2009
This is version 69 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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