NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=YCH46;
DOI=10.1073/pnas.0404172101; PubMed=15466707 [NCBI, ExPASy, EBI, Israel, Japan]
Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N., Kuhara S., Hattori M., Hayashi T., Ohnishi Y.;
"Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions regulating cell surface adaptation.";
Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(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

AP006841; BAD47239.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_097773.1; -.

3D structure databases

ModBase

Q64Z37.

Enzyme and pathway databases

BioCyc

BFRA295405:BF0490-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

3081108; -.

AP006841_GR; BF0490.

bfr:BF0490; -.

fig|295405.3.peg.199; -.

Phylogenomic databases

HOGENOM

Q64Z37; -.

Genome annotation databases

CMR

Q64Z37; BF0490.

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`	`1 324`	`324`	`D-alanine--D-alanine ligase.`	`PRO_1000030425`
`DOMAIN`	`121 321`	`201`	`ATP-grasp.`
`NP_BIND`	`149 204`	`56`	`ATP (By similarity).`
`METAL`	`275 275`		`Magnesium or manganese 1 (By similarity).`
`METAL`	`288 288`		`Magnesium or manganese 1 (By similarity).`
`METAL`	`288 288`		`Magnesium or manganese 2 (By similarity).`
`METAL`	`290 290`		`Magnesium or manganese 2 (By similarity).`

Sequence information

Length: 324 AA [This is the length of the unprocessed precursor]

Molecular weight: 36045 Da [This is the MW of the unprocessed precursor]

CRC64: C5E45504FB544DAE [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKRNIAIVAG GDTSEIVVSL RSAQGIYSFI DKEKYNLYIV EMEGRRWEVQ LPDGSKTPVD 

        70         80         90        100        110        120 
RNDFSFINGA EKVVFDFAYI TIHGTPGEDG RLQGYFDMMR IPYSCCGVLA AAITYDKFVC 

       130        140        150        160        170        180 
NQYLKAFGVR ISESLLLRQG QAVSDEDVVE KIGLPCFIKP NLGGSSFGVT KVKTREQIQP 

       190        200        210        220        230        240 
AIAKAFSEAE EVMIEAFMGG TELTCGCYKT KEKSVVFPLT EVVTHNEFFD YDAKYNGQVD 

       250        260        270        280        290        300 
EITPARISEE LTRRVQTLTS AIYDILGCSG IIRVDYIITE GEKINLLEVN TTPGMTATSF 

       310        320 
IPQQVRAAGL DIKDVMTDII ENKF

Q64Z37 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