Q0VS00 (DDL_ALCBS) 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:	ABO_0600

Organism

Alcanivorax borkumensis (strain SK2 / ATCC 700651 / DSM 11573) [Complete proteome] [HAMAP]

Taxonomic identifier

393595 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Oceanospirillales › Alcanivoracaceae › Alcanivorax › Alcanivorax borkumensis

Protein attributes

Sequence length	307 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 – 307	307	D-alanine--D-alanine ligase HAMAP-Rule MF_00047		PRO_0000341048
Regions
	Domain	110 – 299	190	ATP-grasp
	Nucleotide binding	136 – 185	50	ATP By similarity
Sites
	Metal binding	253	1	Magnesium or manganese 1 By similarity
	Metal binding	266	1	Magnesium or manganese 1 By similarity
	Metal binding	266	1	Magnesium or manganese 2 By similarity
	Metal binding	268	1	Magnesium or manganese 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q0VS00 [UniParc]. Last modified September 5, 2006. Version 1. Checksum: CDB08412E311061A	FASTA	307	32,851
	10 20 30 40 50 60 MDKRALKERL SRVGRVAVLA GGRSAERAVS LKSGAAVHAG LRNLGLLAEL VDPADKSVDT 70 80 90 100 110 120 LRGFDAAFIA LHGRGGEDGV IQGVLEHLEI PYTGSGVMAS AIGMDKVRTK QLWKGAGLPT 130 140 150 160 170 180 PAFYVAGREE AELGFPVIVK PAHEGSSIGM AKADNTEELG EALVAAEKFD QDVLVEAWVN 190 200 210 220 230 240 GPEYTVAVLG DEALPAIRLQ TPHVFYDFEA KYQSDSTEYL CPAGLDDADE QALRTLALTA 250 260 270 280 290 300 FRVAGCRGWG RVDVMRDEQG QWQLLEVNTV PGMTDHSLVP MAAKATGRDF DVLVGEILLD ALERGRG

References

[1]

"Genome sequence of the ubiquitous hydrocarbon-degrading marine bacterium Alcanivorax borkumensis." Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T., Brecht M., Buhrmester J., Chernikova T.N., Denaro R., Ferrer M., Gertler C., Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N., Lang S., Linke B., McHardy A.C., Meyer F. , Nechitaylo T., Puehler A., Regenhardt D., Rupp O., Sabirova J.S., Selbitschka W., Yakimov M.M., Timmis K.N., Vorhoelter F.-J., Weidner S., Kaiser O., Golyshin P.N. Nat. Biotechnol. 24:997-1004(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: SK2 / ATCC 700651 / DSM 11573.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM286690 Genomic DNA. Translation: CAL16048.1.
RefSeq	YP_692320.1. NC_008260.1.
3D structure databases
ProteinModelPortal	Q0VS00.
SMR	Q0VS00. Positions 14-298.
ModBase	Search...
Protein-protein interaction databases
STRING	393595.ABO_0600.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAL16048; CAL16048; ABO_0600.
GeneID	4212209.
KEGG	abo:ABO_0600.
PATRIC	20838853. VBIAlcBor124741_0627.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1181.
HOGENOM	HOG000011592.
KO	K01921.
OMA	GCRTWGR.
ProtClustDB	PRK01372.
Enzyme and pathway databases
BioCyc	ABOR393595:GHRI-601-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. 2 hits. [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_ALCBS

Accession

Primary (citable) accession number: Q0VS00

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 10, 2008
Last sequence update:	September 5, 2006
Last modified:	May 1, 2013
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program