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UniProtKB/Swiss-Prot entry P36843


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ARGJ_BACSU
Primary accession number P36843
Secondary accession numbers None
Integrated into Swiss-Prot on June 1, 1994
Sequence was last modified on June 1, 1994 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 72)
Name and origin of the protein
Protein name Arginine biosynthesis bifunctional protein argJ
Synonyms None
Includes Glutamate N-acetyltransferase
     (EC 2.3.1.35)
     (Ornithine acetyltransferase)
     (OATase)
     (Ornithine transacetylase)
Amino-acid acetyltransferase
     (EC 2.3.1.1)
     (N-acetylglutamate synthase)
     (AGS)
Contains Arginine biosynthesis bifunctional protein argJ alpha chain
Arginine biosynthesis bifunctional protein argJ beta chain
Gene name
Name: argJ
OrderedLocusNames: BSU11200
From
Bacillus subtilis [TaxID: 1423] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168;
PubMed=8025667 [NCBI, ExPASy, EBI, Israel, Japan]
O'Reilly M., Devine K.M.;
"Sequence and analysis of the citrulline biosynthetic operon argC-F from Bacillus subtilis.";
Microbiology 140:1023-1025(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168;
PubMed=9025291 [NCBI, ExPASy, EBI, Israel, Japan]
Levine A., Vannier F., Roche B., Autret S., Mavel D., Seror S.J.;
"A 10.3 kbp segment from nprB to argJ at the 102 degrees region of the Bacillus subtilis chromosome.";
Microbiology 143:175-177(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=168;
DOI=10.1038/36786; PubMed=9384377 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis.";
Nature 390:249-256(1997).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-80.
STRAIN=168;
PubMed=9353931 [NCBI, ExPASy, EBI, Israel, Japan]
Medina N., Vannier F., Roche B., Autret S., Levine A., Seror S.J.;
"Sequencing of regions downstream of addA (98 degrees) and citG (289 degrees) in Bacillus subtilis.";
Microbiology 143:3305-3308(1997).
Comments
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
Z26919; CAA81544.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z79580; CAB01843.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z99109; CAB12961.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Y09476; CAA70639.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR I40373; I40373.
RefSeq NP_389002.1; -.
3D structure databases
ModBase P36843.
Protein family/group databases
MEROPS T05.001; -.
Enzyme and pathway databases
BioCyc BSUB224308:BSU1121-MON; -.
Organism-specific databases
SubtiList BG10192; argJ. [Micado]
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0004042; Molecular function: amino-acid N-acetyltransferase activity (inferred from electronic annotation from HAMAP).
GO:0004358; Molecular function: glutamate N-acetyltransferase activity (inferred from electronic annotation from HAMAP).
GO:0006526; Biological process: arginine biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_01106; -; 1.
PBIL [Tree]
InterPro IPR002813; Arg_biosynth_ArgJ.
Graphical view of domain structure.
PANTHER PTHR23100; ArgJ; 1.
Pfam PF01960; ArgJ; 1.
Pfam graphical view of domain structure.
ProDom PD004193; ArgJ; 2.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR00120; ArgJ; 1.
ProtoNet P36843.
Genome annotation databases
GeneID 939800; -.
GenomeReviews AL009126_GR; BSU11200.
KEGG bsu:BSU11200; -.
NMPDR fig|224308.1.peg.1121; -.
Phylogenomic databases
HOGENOM P36843; -.
Genome annotation databases
CMR P36843; BSU11200.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acyltransferase; Amino-acid biosynthesis; Arginine biosynthesis; Complete proteome; Cytoplasm; Multifunctional enzyme; Transferase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   192  192     Arginine biosynthesis bifunctional protein argJ alpha chain (By similarity). PRO_0000002121
CHAIN   193   406  214     Arginine biosynthesis bifunctional protein argJ beta chain (By similarity). PRO_0000002122
SITE   192   193  2     Cleavage; by autolysis (By similarity). 
Sequence information
Length: 406 AA [This is the length of the unprocessed precursor] Molecular weight: 43364 Da [This is the MW of the unprocessed precursor] CRC64: D49C9192055D0571 [This is a checksum on the sequence]
        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 
RKGSGMIHPN MATMLGFVTT DAAIEEKALQ KALRETTDVS FNQITVDGET STNDMVLVMA 

       250        260        270        280        290        300 
NACAENECLT 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 

P36843 in FASTA format

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View entry in raw text format (no links)
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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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