Q052B5 (DDL_LEPBL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
D-alanine--D-alanine ligase
EC=6.3.2.4

Alternative name(s):
D-Ala-D-Ala ligase
D-alanylalanine synthetase

Gene names

Name:	ddl
Ordered Locus Names:	LBL_1338

Organism

Leptospira borgpetersenii serovar Hardjo-bovis (strain L550) [Complete proteome] [HAMAP]

Taxonomic identifier

355276 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Spirochaetes › Spirochaetia › Spirochaetales › Leptospiraceae › Leptospira › Leptospira borgpetersenii › Leptospira borgpetersenii serovar Hardjo-bovis

Protein attributes

Sequence length	351 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Cell wall formation By similarity.
Catalytic activity	ATP + 2 D-alanine = ADP + phosphate + D-alanyl-D-alanine. HAMAP-Rule MF_00047
Cofactor	Binds 2 magnesium or manganese ions per subunit By similarity.
Pathway	Cell wall biogenesis; peptidoglycan biosynthesis. HAMAP-Rule MF_00047
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the D-alanine--D-alanine ligase family. Contains 1 ATP-grasp domain.

Ontologies

Keywords
Biological process	Cell shape Cell wall biogenesis/degradation Peptidoglycan synthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Magnesium Manganese Metal-binding Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	peptidoglycan biosynthetic process Inferred from electronic annotation. Source: HAMAP regulation of cell shape Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cell wall Inferred from electronic annotation. Source: InterPro cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: HAMAP D-alanine-D-alanine ligase activity Inferred from electronic annotation. Source: HAMAP magnesium ion binding Inferred from electronic annotation. Source: HAMAP manganese ion binding 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 – 351	351	D-alanine--D-alanine ligase HAMAP-Rule MF_00047		PRO_1000030462
Regions
	Domain	135 – 343	209	ATP-grasp
	Nucleotide binding	167 – 222	56	ATP By similarity
Sites
	Metal binding	298	1	Magnesium or manganese 1 By similarity
	Metal binding	310	1	Magnesium or manganese 1 By similarity
	Metal binding	310	1	Magnesium or manganese 2 By similarity
	Metal binding	312	1	Magnesium or manganese 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q052B5 [UniParc]. Last modified November 14, 2006. Version 1. Checksum: B2AF0D10AF638C4A	FASTA	351	38,303
	10 20 30 40 50 60 MAKIAVFFGG SSTEHSISIR TGCFICRTLH TMGHSVKPIL LTQDGGWVVP LQYRISIPYE 70 80 90 100 110 120 AVNSSDLFEE EFQKTNGVSK MDFISNLDAD IVFLGLHGGK GEDGSIQGFL RVLGVPYTGS 130 140 150 160 170 180 GVAASALAMD KTRANQIFLQ SGQKVAPFFE VEKLGYTNSP EETVIKLMSL GFPQFLKPVE 190 200 210 220 230 240 GGSSVSTYKI TNQEQLSRQL ALIFESDSKV MSQSFLAGTE VSCGVLERYR NGKLERIALP 250 260 270 280 290 300 ATEIVPGGEF FDFESKYKQG GSREITPARI SKQEMTRVQE LAIDAHTSLG CRGYSRSDFI 310 320 330 340 350 IVGGEPHILE TNTLPGMTET SLIPQQAKAA GITMEEVFAD LIEIGLKHSI H

References

[1]

"Genome reduction in Leptospira borgpetersenii reflects limited transmission potential." Bulach D.M., Zuerner R.L., Wilson P., Seemann T., McGrath A., Cullen P.A., Davis J., Johnson M., Kuczek E., Alt D.P., Peterson-Burch B., Coppel R.L., Rood J.I., Davies J.K., Adler B. Proc. Natl. Acad. Sci. U.S.A. 103:14560-14565(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: L550.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000348 Genomic DNA. Translation: ABJ78830.1.
RefSeq	YP_797763.1. NC_008508.1.
3D structure databases
ProteinModelPortal	Q052B5.
ModBase	Search...
Protein-protein interaction databases
STRING	355276.LBL_1338.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABJ78830; ABJ78830; LBL_1338.
GeneID	4406262.
KEGG	lbl:LBL_1338.
PATRIC	22366480. VBILepBor75619_1701.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1181.
HOGENOM	HOG000011592.
KO	K01921.
OMA	VEDASCD.
ProtClustDB	PRK14572.
Enzyme and pathway databases
BioCyc	LBOR355276:GHUQ-1612-MONOMER.
UniPathway	UPA00219.
Family and domain databases
Gene3D	3.30.1490.20. 1 hit. 3.30.470.20. 2 hits. 3.40.50.20. 1 hit.
HAMAP	MF_00047. Dala_Dala_lig.
InterPro	IPR011761. ATP-grasp. IPR013815. ATP_grasp_subdomain_1. IPR013816. ATP_grasp_subdomain_2. IPR000291. D-Ala_lig_Van_CS. IPR005905. D_ala_D_ala. IPR011095. Dala_Dala_lig_C. IPR011127. Dala_Dala_lig_N. IPR016185. PreATP-grasp_dom. [Graphical view]
PANTHER	PTHR23132. PTHR23132. 1 hit.
Pfam	PF07478. Dala_Dala_lig_C. 1 hit. PF01820. Dala_Dala_lig_N. 1 hit. [Graphical view]
SUPFAM	SSF52440. PreATP-grasp-like. 1 hit.
TIGRFAMs	TIGR01205. D_ala_D_alaTIGR. 1 hit.
PROSITE	PS50975. ATP_GRASP. 1 hit. PS00843. DALA_DALA_LIGASE_1. 1 hit. PS00844. DALA_DALA_LIGASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DDL_LEPBL

Accession

Primary (citable) accession number: Q052B5

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	November 14, 2006
Last modified:	May 1, 2013
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program