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P36843 (ARGJ_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Arginine biosynthesis bifunctional protein ArgJ

Cleaved into the following 2 chains:

  1. Arginine biosynthesis bifunctional protein ArgJ alpha chain
  2. Arginine biosynthesis bifunctional protein ArgJ beta chain

Including the following 2 domains:

  1. Glutamate N-acetyltransferase
    EC=2.3.1.35
    Alternative name(s):
    Ornithine acetyltransferase
    Short name=OATase
    Ornithine transacetylase
  2. Amino-acid acetyltransferase
    EC=2.3.1.1
    Alternative name(s):
    N-acetylglutamate synthase
    Short name=AGS
Gene names
Name:argJ
Ordered Locus Names:BSU11200
OrganismBacillus subtilis
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length406 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred 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 By similarity. 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

Enzyme regulation

Feedback inhibition by L-arginine By similarity. 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 HAMAP MF_01106.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 192192Arginine biosynthesis bifunctional protein ArgJ alpha chain By similarity
PRO_0000002121
Chain193 – 406214Arginine biosynthesis bifunctional protein ArgJ beta chain By similarity
PRO_0000002122

Sites

Site192 – 1932Cleavage; by autolysis By similarity

Experimental info

Sequence conflict1811A → R in CAA81544. Ref.1
Sequence conflict2161I → T in CAA81544. Ref.1
Sequence conflict2421G → A in CAA81544. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P36843 [UniParc].

Last modified June 16, 2009. Version 2.
Checksum: 9537998AEF0CAF81

FASTA40643,277
        10         20         30         40         50         60 
MIQLSEDQIV KVTGDVSSPK GFQAKGVHCG LRYSKKDLGV IISETPAVSA AVYTQSHFQA 

        70         80         90        100        110        120 
APIKVTQDSL KHGPTLKAVI VNSAIANACT GEQGLKDAYT MRESFASQLG IEPELVAVSS 

       130        140        150        160        170        180 
TGVIGEHLDM EKIHAGIELL KETPAGSGDF EEAILTTDTV IKQTCYELAI GGKTVTIGGA 

       190        200        210        220        230        240 
AKGSGMIHPN MATMLGFVTT DAAIEEKALQ KALREITDVS FNQITVDGET STNDMVLVMA 

       250        260        270        280        290        300 
NGCAENECLT EDHPDWPVFK KALLLTCEDL AKEIARDGEG ATKLIEAQVQ GAKNNLDANV 

       310        320        330        340        350        360 
IAKKIVGSNL VKTAVYGTDA NWGRIIGAIG HSAAQVTAEE VEVYLGGQCL FKNNEPQPFS 

       370        380        390        400 
ESIAKEYLEG DEITIVIKMA EGDGNGRAWG CDLTYDYIKI NASYRT

« Hide

References

« Hide 'large scale' references
[1]"Sequence and analysis of the citrulline biosynthetic operon argC-F from Bacillus subtilis."
O'Reilly M., Devine K.M.
Microbiology 140:1023-1025(1994) [PubMed: 8025667] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[2]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed: 9384377] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[3]"From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later."
Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.
Microbiology 155:1758-1775(2009) [PubMed: 19383706] [Abstract]
Cited for: SEQUENCE REVISION TO 181; 216 AND 242.
[4]"A 10.3 kbp segment from nprB to argJ at the 102 degrees region of the Bacillus subtilis chromosome."
Levine A., Vannier F., Roche B., Autret S., Mavel D., Seror S.J.
Microbiology 143:175-177(1997) [PubMed: 9025291] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-80.
Strain: 168.
[5]"Sequencing of regions downstream of addA (98 degrees) and citG (289 degrees) in Bacillus subtilis."
Medina N., Vannier F., Roche B., Autret S., Levine A., Seror S.J.
Microbiology 143:3305-3308(1997) [PubMed: 9353931] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-80.
Strain: 168.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Z26919 Genomic DNA. Translation: CAA81544.1.
AL009126 Genomic DNA. Translation: CAB12961.2.
Z79580 Genomic DNA. Translation: CAB01843.1.
Y09476 Genomic DNA. Translation: CAA70639.1.
PIRI40373.
RefSeqNP_389002.2. NC_000964.3.

3D structure databases

ProteinModelPortalP36843.
SMRP36843. Positions 7-406.
ModBaseSearch...

Protein family/group databases

MEROPST05.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000003686; EBBACP00000003686; EBBACG00000003679.
GeneID939800.
GenomeReviewsGene locus BSU11200 in contig AL009126_GR.
KEGGbsu:BSU11200.
NMPDRfig|224308.1.peg.1121.
PATRIC18973950. VBIBacSub10457_1169.

Organism-specific databases

GenoListBSU11200. [Micado]

Phylogenomic databases

GeneTreeEBGT00050000002382.
HOGENOMHBG284202.
PhylomeDBP36843.
ProtClustDBPRK05388.

Enzyme and pathway databases

BioCycBSUB:BSU11200-MONOMER.

Family and domain databases

HAMAPMF_01106. ArgJ.
[Tree]
InterProIPR002813. Arg_biosynth_ArgJ.
IPR016117. Pept_S58_DmpA/Arg_biosyn_ArgJ.
[Graphical view]
KOK00620.
PANTHERPTHR23100. ArgJ. 1 hit.
PfamPF01960. ArgJ. 1 hit.
[Graphical view]
ProDomPD004193. Arg_biosynth_ArgJ. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF56266. Pept_S58_DmpA/Arg_biosyn_ArgJ. 1 hit.
TIGRFAMsTIGR00120. ArgJ. 1 hit.
ProtoNetSearch...

Entry information

Entry nameARGJ_BACSU
AccessionPrimary (citable) accession number: P36843
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 16, 2009
Last modified: January 25, 2012
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents