NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1159/000079829; PubMed=15383718 [NCBI, ExPASy, EBI, Israel, Japan]
Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.;
"The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential.";
J. Mol. Microbiol. Biotechnol. 7:204-211(2004).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1186/gb-2004-5-10-r77; PubMed=15461803 [NCBI, ExPASy, EBI, Israel, Japan]
Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., Bolotin A., Lapidus A., Galleron N., Ehrlich S.D., Berka R.M.;
"Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species.";
Genome Biol. 5:RESEARCH077.1-RESEARCH077.12(2004).

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

CP000002; AAU22144.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AE017333; AAU39499.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_077782.1; -.
YP_090192.1; -.

3D structure databases

ModBase

Q65N65.

Enzyme and pathway databases

BioCyc

BLIC279010:BL02193-MON; -.

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

Q65N65.

Genome annotation databases

GeneID

3030394; -.
3099263; -.

GenomeReviews

CP000002_GR; BL02193.
AE017333_GR; BLi00543.

KEGG

bld:BLi00543; -.
bli:BL02193; -.

NMPDR

fig|279010.5.peg.679; -.

Phylogenomic databases

HOGENOM

Q65N65; -.

Genome annotation databases

CMR

Q65N65; BLi00543.

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`	`1 361`	`361`	`D-alanine--D-alanine ligase.`	`PRO_1000030426`
`DOMAIN`	`140 345`	`206`	`ATP-grasp.`
`NP_BIND`	`173 228`	`56`	`ATP (By similarity).`
`METAL`	`299 299`		`Magnesium or manganese 1 (By similarity).`
`METAL`	`312 312`		`Magnesium or manganese 1 (By similarity).`
`METAL`	`312 312`		`Magnesium or manganese 2 (By similarity).`
`METAL`	`314 314`		`Magnesium or manganese 2 (By similarity).`

Sequence information

Length: 361 AA [This is the length of the unprocessed precursor]

Molecular weight: 40057 Da [This is the MW of the unprocessed precursor]

CRC64: DA83B729D1862A9B [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKTRLGLVYG GKSAEHNVSL QTALAVTKAL DTEKFDIHPI YITEKGEWVR GPQLTEPVSN 

        70         80         90        100        110        120 
VKMLQFEQTG QTFSPAVLNR DMFPGEADAK EDSIDVVFPL LHGPNGEDGT IQGMLELLNV 

       130        140        150        160        170        180 
PYVGNGVLAS SAGMDKVVMK HLFAQAGLDQ AKYVSFLKKT WSQSKEECYA QVEGELGYPC 

       190        200        210        220        230        240 
FVKPANLGSS VGISKCRSRE ELDQAFELAF QYDRKIVVEE GVIGREIELG VLGNDEPVCS 

       250        260        270        280        290        300 
VAGEIAPKKD FYDYKAKYED GDTDLIIPAS LTEDEYETMR SMAVKAFQAI DGSGLVRADF 

       310        320        330        340        350        360 
FLTNEGRVLI NEVNTMPGFT PFSMFPLLWK QSGVEYAELI EKLVALAIER HEEKQQIKHT 


F

Q65N65 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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