NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J., Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P.;
"Complete sequence of Anabaena variabilis ATCC 29413.";
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.

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

CP000117; ABA19986.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_320881.1; -.

3D structure databases

ModBase

Q3MGA0.

Enzyme and pathway databases

BioCyc

AVAR240292:AVA_0360-MON; -.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
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

3682734; -.

GenomeReviews

CP000117_GR; Ava_0360.

KEGG

ava:Ava_0360; -.

NMPDR

fig|240292.3.peg.961; -.

Phylogenomic databases

HOGENOM

Q3MGA0; -.

Genome annotation databases

CMR

Q3MGA0; Ava_0360.

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`	`1 367`	`367`	`D-alanine--D-alanine ligase.`	`PRO_1000030423`
`DOMAIN`	`148 357`	`210`	`ATP-grasp.`
`NP_BIND`	`184 239`	`56`	`ATP (By similarity).`
`METAL`	`310 310`		`Magnesium or manganese 1 (By similarity).`
`METAL`	`324 324`		`Magnesium or manganese 1 (By similarity).`
`METAL`	`324 324`		`Magnesium or manganese 2 (By similarity).`
`METAL`	`326 326`		`Magnesium or manganese 2 (By similarity).`

Sequence information

Length: 367 AA [This is the length of the unprocessed precursor]

Molecular weight: 39782 Da [This is the MW of the unprocessed precursor]

CRC64: C7E4A822197A0DC5 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSKLRVGLLF GGRSGEHEVS ISSARAIASA LSAGENASKY EILPFYIHKD GRWLAGEAPQ 

        70         80         90        100        110        120 
QVLKSGAPLL ESSNSSPADN NLVNSQQQTL ERWQSPSQVA EVDVWFPILH GPNGEDGTIQ 

       130        140        150        160        170        180 
GLLTLMQTPF VGSGVLGSAL GMDKIAMKMA FEQAGLPQVK YKAVTRAQIW SNPCVFPKLC 

       190        200        210        220        230        240 
DEIEASLGYP CFVKPANLGS SVGISKVRSR QELEDALDNA ANYDRRIIVE AGVVAREVEC 

       250        260        270        280        290        300 
AVLGNDQPQA STVGEITFNS DFYDYETKYT AGKADLLIPA VIPDEISRQI QDMALQAFAA 

       310        320        330        340        350        360 
VDAAGLARVD FFYVEATGEV LINEINTLPG FTATSMYPQL WAYSGIPFPE LVDKLVQLAI 


ERHNPSH

Q3MGA0 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