NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=USDA 110;
DOI=10.1093/dnares/9.6.189; PubMed=12597275 [NCBI, ExPASy, EBI, Israel, Japan]
Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S., Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M., Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
"Complete genomic sequence of nitrogen-fixing symbiotic bacterium Bradyrhizobium japonicum USDA110.";
DNA Res. 9:189-197(2002).

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

BA000040; BAC48670.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_770045.1; -.

3D structure databases

HSSP

P07862; 1IOW. [HSSP ENTRY / PDB]

ModBase

Q89PS5.

Enzyme and pathway databases

BioCyc

BJAP224911:BLR3405-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).

Genome annotation databases

GeneID

1050703; -.

GenomeReviews

BA000040_GR; blr3405.

KEGG

bja:blr3405; -.

NMPDR

fig|224911.1.peg.3405; -.

Phylogenomic databases

HOGENOM

Q89PS5; -.

Genome annotation databases

CMR

Q89PS5; blr3405.

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`	`1 376`	`376`	`D-alanine--D-alanine ligase B.`	`PRO_0000177793`
`DOMAIN`	`155 361`	`207`	`ATP-grasp.`
`NP_BIND`	`184 239`	`56`	`ATP (By similarity).`
`METAL`	`316 316`		`Magnesium or manganese 1 (By similarity).`
`METAL`	`328 328`		`Magnesium or manganese 1 (By similarity).`
`METAL`	`328 328`		`Magnesium or manganese 2 (By similarity).`
`METAL`	`330 330`		`Magnesium or manganese 2 (By similarity).`

Sequence information

Length: 376 AA [This is the length of the unprocessed precursor]

Molecular weight: 39991 Da [This is the MW of the unprocessed precursor]

CRC64: ADF689A391337460 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTAYGGEMTK ERRKITVGLL FGGRSAEHEV SRASAANILR ALNSDRYDVY LIGISRDGRW 

        70         80         90        100        110        120 
FACDSGNGAG TGSTALTISD EAPEIGLVPG GRGRLVHCDG PTGSDAGSID VAFPILHGPN 

       130        140        150        160        170        180 
GEDGTVQGAL ELADVSFVGS SVTGSAVAMD KEVSKRLMRD AGLPVVPFLT TTASSRIEYA 

       190        200        210        220        230        240 
AAVAALGTPD LFVKPANLGS SVGVSRARSE EEFAASCALA FRYDRKILVE QALNGAREIE 

       250        260        270        280        290        300 
CSVLEESTGD IRASGLGEIV RASEHGFYSY QAKYIDADGA ALHIPADLPL LQARRLQELA 

       310        320        330        340        350        360 
VEVFNVLCCE GMARVDFFVQ GDEVFVNEAN TLPGFTSSSM YPKLWEASGL SQTDLMDKLI 

       370 
AHAFARHERR RALSFG

Q89PS5 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