Q8KWT3 (BACD2_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Alanine-anticapsin ligase BacD
EC=6.3.2.28

Alternative name(s):
Bacilysin synthetase
L-amino acid ligase

Gene names

Name:

bacD

Organism

Bacillus subtilis

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	472 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the formation of alpha-dipeptides from various L-amino acids in the presence of ATP. Probably catalyzes the ligation of L-alanine and L-anticapsin to produce the final bacilysin antibiotic By similarity.
Catalytic activity	ATP + an L-amino acid + an L-amino acid = ADP + phosphate + L-aminoacyl-L-amino acid.
Cofactor	Magnesium or manganese By similarity.
Pathway	Antibiotic biosynthesis; bacilysin biosynthesis.
Sequence similarities	Contains 1 ATP-grasp domain.

Ontologies

Keywords
Biological process	Antibiotic biosynthesis
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Gene Ontology (GO)
Biological process	antibiotic biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW D-alanine-D-alanine ligase activity Inferred from electronic annotation. Source: InterPro L-amino-acid alpha-ligase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 472	472	Alanine-anticapsin ligase BacD		PRO_0000064802
Regions
	Domain	142 – 355	214	ATP-grasp
	Nucleotide binding	168 – 235	68	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8KWT3 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: D39D317DD624E5FC	FASTA	472	52,166
	10 20 30 40 50 60 MERKTVLVIA DLGGCPPHMF YKSAAEKYNL VSFIPRPFAI TASHAALIEK YSVAVIKDKD 70 80 90 100 110 120 YFKSLADFEH PDSIYWAHED HDKPEEEVVE EIVKVAGMFA VDAITTNNEL FIAPMAKACE 130 140 150 160 170 180 RLGLRGAGVQ AAENARDKNK MRAAFNRAGV KSIKNKRVTT LEDFRAALQE IGTPLILKPT 190 200 210 220 230 240 YLASSIGVTL IKEMETAEAE FNRVNEYLKS INVPKAVTFE APFIAEEFLQ GEYDDWYETS 250 260 270 280 290 300 GYSDYISIEG IMADGEYFPV AIHDKTPQIG FTETSHITPS ILDDDAKRKI VEAAKKANEG 310 320 330 340 350 360 LGLENCATHT EIKLMKNREA GLIESAARFA GWNMIPNIKK VFGVDMAQLL LDVLCFGKEA 370 380 390 400 410 420 DLPKGLLEQE PCYVADCHLY PQHFKENGQL PETAVDFVIE SIDIPDGVLK GDTEIVSFSA 430 440 450 460 470 AEAGTSVDLR LFEAFNSIAA FELKGSNSGD VAESIKQIQQ QAKLTAKYAL PV

References

[1]	"bac genes for recombinant bacilysin and anticapsin production in Bacillus host strains." Steinborn G., Hajirezaei M.-R., Hofemeister J. Arch. Microbiol. 183:71-79(2005) [PubMed: 15609023] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: A1/3.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF396778 Genomic DNA. Translation: AAM90571.1.
3D structure databases
ProteinModelPortal	Q8KWT3.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR011761. ATP-grasp. IPR013815. ATP_grasp_subdomain_1. IPR013816. ATP_grasp_subdomain_2. IPR011095. Dala_Dala_lig_C. [Graphical view]
Gene3D	G3DSA:3.30.1490.20. ATP_grasp_subdomain_1. 1 hit. G3DSA:3.30.470.20. ATP_grasp_subdomain_2. 2 hits.
Pfam	PF07478. Dala_Dala_lig_C. 1 hit. [Graphical view]
PROSITE	PS50975. ATP_GRASP. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

BACD2_BACSU

Accession

Primary (citable) accession number: Q8KWT3

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 30, 2005
Last sequence update:	October 1, 2002
Last modified:	June 28, 2011
This is version 32 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program