Reviewed, UniProtKB/Swiss-Prot O08319 (ARGJ_LACPL)

Names and origin

Protein names

Recommended name:
    Arginine biosynthesis bifunctional protein argJ
Cleaved into the following 2 chains:
    1- Recommended name:
            Arginine biosynthesis bifunctional protein argJ alpha chain
    2- Recommended name:
            Arginine biosynthesis bifunctional protein argJ beta chain
Including the following 2 domains:
    1- Recommended name:
            Glutamate N-acetyltransferase
              EC=2.3.1.35
        Alternative name(s):
            Ornithine acetyltransferase
              Short name=OATase
            Ornithine transacetylase
    2- Recommended name:
            Amino-acid acetyltransferase
              EC=2.3.1.1
        Alternative name(s):
            N-acetylglutamate synthase
              Short name=AGS

Gene names

Name:	argJ
Ordered Locus Names:	lp_0529

Organism

Lactobacillus plantarum [Complete proteome] [HAMAP]

Taxonomic identifier

1590 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Lactobacillaceae › Lactobacillus

Protein attributes

Sequence length	404 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of acetylglutamate from glutamate and acetyl-CoA, and of ornithine by transacetylation between acetylornithine and glutamate. HAMAP MF_01106
Catalytic activity	N(2)-acetyl-L-ornithine + L-glutamate = L-ornithine + N-acetyl-L-glutamate. HAMAP MF_01106 Acetyl-CoA + L-glutamate = CoA + N-acetyl-L-glutamate. HAMAP MF_01106
Pathway	Amino-acid biosynthesis; L-arginine biosynthesis; L-ornithine and N-acetyl-L-glutamate from L-glutamate and N(2)-acetyl-L-ornithine (cyclic): step 1/1. HAMAP MF_01106 Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 1/4. HAMAP MF_01106
Subunit structure	Heterotetramer of two alpha and two beta chains By similarity.
Subcellular location	Cytoplasm Probable.
Miscellaneous	Some bacteria possess a monofunctional argJ, i.e., capable of catalyzing only the fifth step of the arginine biosynthetic pathway. HAMAP MF_01106
Sequence similarities	Belongs to the argJ family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Arginine biosynthesis
Cellular component	Cytoplasm
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	arginine biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	amino-acid N-acetyltransferase activity Inferred from electronic annotation. Source: HAMAP glutamate N-acetyltransferase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 190	190	Arginine biosynthesis bifunctional protein argJ alpha chain By similarity		PRO_0000002177
	Chain	191 – 404	214	Arginine biosynthesis bifunctional protein argJ beta chain By similarity		PRO_0000002178
Sites
	Site	190 – 191	2	Cleavage; by autolysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	O08319-1 [UniParc]. Last modified July 1, 1997. Version 1. Checksum: 1A97F749E4E02580	FASTA	404	43,276
	10 20 30 40 50 60 MQMQVLTNTK FETVAFQWPA GFYSDGIHIG LRRHKKDFGW LFSKVPASAA GTYTTNQFQA 70 80 90 100 110 120 APTKLTKQMI DQGHQLQGLL LNSAIANSCT GEQGWQNALQ EQAWLANKLN VAPNLIGVAS 130 140 150 160 170 180 TGLIGAQLPM DKIKNGLPQL TPTKSDAVTY AVLTTDQHPK TVCVQCELSG QLVTLTGFAK 190 200 210 220 230 240 GSGMIHPKMA TMLGFVTTDA QIDGPVLQDM LSTNVDQTFN QITVDGDTST NDMVVTLANG 250 260 270 280 290 300 LADNPSLQAG TTDYDIFNQA LHYVLGQLAK QIAADGEGAT KLVECNVVHA ATTFDGQQIA 310 320 330 340 350 360 KAIVGSNLVK AAIFGEDPNW GRIISTIGAT DADIDVATVD IEMNGVLLVQ QSLAVDFDMA 370 380 390 400 AVQATLRDNQ IMIDVDLHHG TASGQAWGCD LTYNYVKINA SYHT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Arginine biosynthesis and regulation in Lactobacillus plantarum: the carA gene and the argCJBDF cluster are divergently transcribed." Bringel F., Frey L., Boivin S., Hubert J.-C. J. Bacteriol. 179:2697-2706(1997) [PubMed: 9098069] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 8014 / CCM 1904 / DSM 20205 / NCDO 82 / NCIB 6376.
[2]	"Complete genome sequence of Lactobacillus plantarum WCFS1." Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D., Kuipers O.P., Leer R., Tarchini R., Peters S.A., Sandbrink H.M., Fiers M.W.E.J., Stiekema W., Klein Lankhorst R.M., Bron P.A., Hoffer S.M., Nierop Groot M.N., Kerkhoven R., De Vries M., Ursing B., De Vos W.M., Siezen R.J. Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003) [PubMed: 12566566] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-793 / NCIMB 8826 / WCFS1.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X99978 Genomic DNA. Translation: CAA68240.1. AL935253 Genomic DNA. Translation: CAD63148.1.
RefSeq	NP_784307.1.
3D structure databases
ModBase	Search...
Protein family/group databases
MEROPS	T05.001.
Genome annotation databases
GeneID	1061854.
GenomeReviews	Gene locus lp_0529 in contig AL935263_GR.
KEGG	lpl:lp_0529.
NMPDR	fig|220668.1.peg.441.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	O08319.
OMA	IVNSGNA.
Enzyme and pathway databases
BioCyc	LPLA220668:LP_0529-MON.
BRENDA	2.3.1.1. 593. 2.3.1.35. 593.
Family and domain databases
HAMAP	MF_01106. [Tree]
InterPro	IPR002813. Arg_biosynth_ArgJ. [Graphical view]
PANTHER	PTHR23100. ArgJ. 1 hit.
Pfam	PF01960. ArgJ. 1 hit. [Graphical view]
ProDom	PD004193. ArgJ. 2 hits. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR00120. ArgJ. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ARGJ_LACPL

Accession

Primary (citable) accession number: O08319

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 23, 2003
Last sequence update:	July 1, 1997
Last modified:	November 3, 2009
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)