NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1371/journal.pbio.0040188; PubMed=16729848 [NCBI, ExPASy, EBI, Israel, Japan]
Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L., Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L., Moran N.A., Eisen J.A.;
"Metabolic complementarity and genomics of the dual bacterial symbiosis of sharpshooters.";
PLoS Biol. 4:1079-1092(2006).

Comments

FUNCTION: Cell wall formation (By similarity).
CATALYTIC ACTIVITY: ATP + 2 D-alanine = ADP + phosphate + D-alanyl-D-alanine.
COFACTOR: Binds 2 magnesium or manganese ions per subunit (By similarity).
PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis .
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
SIMILARITY: Contains 1 ATP-grasp domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

CP000238; ABF14027.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_588832.1; -.

3D structure databases

ModBase

Q1LT82.

Ontologies

GO:0005618;	Cellular component: cell wall (inferred from electronic annotation from InterPro).
GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from InterPro).
GO:0008716;	Molecular function: D-alanine-D-alanine ligase activity (inferred from electronic annotation from HAMAP).
GO:0000287;	Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0030145;	Molecular function: manganese ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0009252;	Biological process: peptidoglycan biosynthetic process (inferred from electronic annotation from HAMAP).
GO:0008360;	Biological process: regulation of cell shape (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

HAMAP

MF_00047; -; 1.
PBIL [Tree]

InterPro

IPR011761; ATP-grasp.
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.
IPR013817; Pre-ATP_grasp.
Graphical view of domain structure.

Gene3D

G3DSA:3.30.470.20; ATP_grasp_subdomain_2; 1.
G3DSA:3.40.50.20; Pre-ATP_grasp; 1.

Pfam

PF07478; Dala_Dala_lig_C; 1.
PF01820; Dala_Dala_lig_N; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR01205; D_ala_D_alaTIGR; 1.

PROSITE

PS50975; ATP_GRASP; 1.
PS00843; DALA_DALA_LIGASE_1; 1.
PS00844; DALA_DALA_LIGASE_2; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

Q1LT82.

Genome annotation databases

GeneID

4056458; -.

GenomeReviews

CP000238_GR; BCI_0388.

KEGG

bci:BCI_0388; -.

Phylogenomic databases

HOGENOM

Q1LT82; -.

Genome annotation databases

CMR

Q1LT82; BCI_0388.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

ATP-binding; Cell shape; Cell wall biogenesis/degradation; Complete proteome; Cytoplasm; Ligase; Magnesium; Manganese; Metal-binding; Nucleotide-binding; Peptidoglycan synthesis.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 375`	`375`	`D-alanine--D-alanine ligase.`	`PRO_1000030431`
`DOMAIN`	`145 348`	`204`	`ATP-grasp.`
`NP_BIND`	`175 230`	`56`	`ATP (By similarity).`
`METAL`	`302 302`		`Magnesium or manganese 1 (By similarity).`
`METAL`	`315 315`		`Magnesium or manganese 1 (By similarity).`
`METAL`	`315 315`		`Magnesium or manganese 2 (By similarity).`
`METAL`	`317 317`		`Magnesium or manganese 2 (By similarity).`

Sequence information

Length: 375 AA [This is the length of the unprocessed precursor]

Molecular weight: 41589 Da [This is the MW of the unprocessed precursor]

CRC64: 11B78F1FC8877C53 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAKLRVGIIF GGQSAEHEVS LQSAKNIVET IDENKFEVVL FGIDKEGQWH INNKLNYLIY 

        70         80         90        100        110        120 
GENETYIALN KSNKHIAIIP GRKHDQFIQI DMLEQLVQLD VIFPIVHGTL GEDGNLQGLL 

       130        140        150        160        170        180 
RMANLPFVGS TVLGSAVSMD KDIAKRLLRD ADLEVTPSIT LTRINRENFS YDQIITYLGS 

       190        200        210        220        230        240 
SLFVKPANQG SSVGVSKVIN RISFDQALAL AFCFDDKVLV ESAINGRELE CAVLGNHDPQ 

       250        260        270        280        290        300 
ASLCGEIVLS DNFYSYEKKY LNEHGAVVVV PAAISKEVSN NIQKIAVRAF QALNCTGMAR 

       310        320        330        340        350        360 
VDVFLTTNNK VLVNEVNTSP GFTSISMYPK LWQASGISYP ALITRLIELA IERYYAEQKK 

       370 
ISHRDIYNKI DTGSA

Q1LT82 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools