UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase - Borrelia burgdorferi (Lyme disease spirochete)

Contribute

Send feedback

Read comments (?) or add your own

Q44777 (MURF_BORBU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 88. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase
EC=6.3.2.10

Alternative name(s):
D-alanyl-D-alanine-adding enzyme
UDP-MurNAc-pentapeptide synthetase

Gene names

Name:	murF
Ordered Locus Names:	BB_0304

Organism

Borrelia burgdorferi (Lyme disease spirochete)

Taxonomic identifier

139 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	464 AA.
Sequence status	Complete.
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 Reference proteome
Gene Ontology (GO)
Biological process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cell division Inferred from electronic annotation. Source: UniProtKB-KW cellular 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

ATP Potential

Experimental info

Sequence conflict

462 – 464

IFR → YI in AAA85627. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

Q44777 [UniParc].

Last modified December 15, 1998. Version 2.
Checksum: 29038B0C533799BC
Show »

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

« Hide

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. 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
EMBL GenBank DDBJ	AE000783 Genomic DNA. Translation: AAC66644.1. U43739 Genomic DNA. Translation: AAA85627.1.
PIR	H70137.
RefSeq	NP_212438.1. NC_001318.1.
3D structure databases
ProteinModelPortal	Q44777.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBORT00000009056; EBBORP00000008386; EBBORG00000009055.
GeneID	1195141.
GenomeReviews	Gene locus BB_0304 in contig AE000783_GR.
KEGG	bbu:BB0304.
NMPDR	fig\|224326.1.peg.688.
PATRIC	20557226. VBIBorBur75917_0703.
TIGR	BB_0304.
Phylogenomic databases
GeneTree	EBGT00050000006939.
HOGENOM	HBG352886.
OMA	VEGNEEY.
PhylomeDB	Q44777.
ProtClustDB	CLSK507501.
Enzyme and pathway databases
BioCyc	BBUR224326:BB_0304-MONOMER.
Family and domain databases
InterPro	IPR004101. Mur_ligase_C. IPR013221. Mur_ligase_cen. IPR005863. UDP-N-AcMur-pentapeptide_synth. [Graphical view]
Gene3D	G3DSA:3.90.190.20. Mur_ligase_C. 1 hit. G3DSA:3.40.1190.10. Mur_ligase_cen. 1 hit.
KO	K01929.
PANTHER	PTHR23135:SF3. MurF. 1 hit.
Pfam	PF02875. Mur_ligase_C. 1 hit. PF08245. Mur_ligase_M. 1 hit. [Graphical view]
SUPFAM	SSF53244. Mur_ligase_C. 1 hit. SSF53623. Mur_ligase_cen. 1 hit.
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:	January 25, 2012
This is version 88 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents