ID   ARGB_EHRRW              Reviewed;         322 AA.
AC   Q5HB82; Q5FEK2;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 2.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Acetylglutamate kinase {ECO:0000255|HAMAP-Rule:MF_00082};
DE            EC=2.7.2.8 {ECO:0000255|HAMAP-Rule:MF_00082};
DE   AltName: Full=N-acetyl-L-glutamate 5-phosphotransferase {ECO:0000255|HAMAP-Rule:MF_00082};
DE   AltName: Full=NAG kinase {ECO:0000255|HAMAP-Rule:MF_00082};
DE            Short=NAGK {ECO:0000255|HAMAP-Rule:MF_00082};
GN   Name=argB {ECO:0000255|HAMAP-Rule:MF_00082};
GN   OrderedLocusNames=Erum4480, ERWE_CDS_04700;
OS   Ehrlichia ruminantium (strain Welgevonden).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Ehrlichia.
OX   NCBI_TaxID=254945;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Welgevonden;
RX   PubMed=15637156; DOI=10.1073/pnas.0406633102;
RA   Collins N.E., Liebenberg J., de Villiers E.P., Brayton K.A., Louw E.,
RA   Pretorius A., Faber F.E., van Heerden H., Josemans A., van Kleef M.,
RA   Steyn H.C., van Strijp M.F., Zweygarth E., Jongejan F., Maillard J.C.,
RA   Berthier D., Botha M., Joubert F., Corton C.H., Thomson N.R., Allsopp M.T.,
RA   Allsopp B.A.;
RT   "The genome of the heartwater agent Ehrlichia ruminantium contains multiple
RT   tandem repeats of actively variable copy number.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:838-843(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Welgevonden;
RX   PubMed=16547041; DOI=10.1128/jb.188.7.2533-2542.2006;
RA   Frutos R., Viari A., Ferraz C., Morgat A., Eychenie S., Kandassamy Y.,
RA   Chantal I., Bensaid A., Coissac E., Vachiery N., Demaille J., Martinez D.;
RT   "Comparative genomic analysis of three strains of Ehrlichia ruminantium
RT   reveals an active process of genome size plasticity.";
RL   J. Bacteriol. 188:2533-2542(2006).
CC   -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-
CC       glutamate. {ECO:0000255|HAMAP-Rule:MF_00082}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-
CC         phosphate; Xref=Rhea:RHEA:14629, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:44337, ChEBI:CHEBI:57936, ChEBI:CHEBI:456216; EC=2.7.2.8;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00082};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC       L-ornithine from L-glutamate: step 2/4. {ECO:0000255|HAMAP-
CC       Rule:MF_00082}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00082}.
CC   -!- SIMILARITY: Belongs to the acetylglutamate kinase family. ArgB
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00082}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAH58176.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=CAI26964.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CR767821; CAH58176.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CR925678; CAI26964.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_011256090.1; NC_006832.1.
DR   AlphaFoldDB; Q5HB82; -.
DR   SMR; Q5HB82; -.
DR   STRING; 254945.Erum4480; -.
DR   EnsemblBacteria; CAI26964; CAI26964; ERWE_CDS_04700.
DR   KEGG; eru:Erum4480; -.
DR   KEGG; erw:ERWE_CDS_04700; -.
DR   eggNOG; COG0548; Bacteria.
DR   HOGENOM; CLU_053680_0_0_5; -.
DR   BioCyc; ERUM254945:ERUM_RS02460-MON; -.
DR   UniPathway; UPA00068; UER00107.
DR   Proteomes; UP000001021; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003991; F:acetylglutamate kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0042450; P:arginine biosynthetic process via ornithine; IEA:UniProtKB-UniRule.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd04250; AAK_NAGK-C; 1.
DR   Gene3D; 3.40.1160.10; -; 1.
DR   HAMAP; MF_00082; ArgB; 1.
DR   InterPro; IPR036393; AceGlu_kinase-like_sf.
DR   InterPro; IPR004662; AcgluKinase_fam.
DR   InterPro; IPR037528; ArgB.
DR   InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR   InterPro; IPR041727; NAGK-C.
DR   Pfam; PF00696; AA_kinase; 1.
DR   PIRSF; PIRSF000728; NAGK; 1.
DR   SUPFAM; SSF53633; SSF53633; 1.
DR   TIGRFAMs; TIGR00761; argB; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding; Cytoplasm;
KW   Kinase; Nucleotide-binding; Transferase.
FT   CHAIN           1..322
FT                   /note="Acetylglutamate kinase"
FT                   /id="PRO_0000264705"
FT   BINDING         89..90
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT   BINDING         111
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT   BINDING         217
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT   SITE            54
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT   SITE            277
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
SQ   SEQUENCE   322 AA;  34878 MW;  25E8643CEE9C4324 CRC64;
     MKLRNVSKNN LNKEDTKLSI EQFGGNVEWF NITKTLSESL PYIQQFSGET FIIKYGGAAM
     TDKKLAESFA HDVVLLKQLG INPIVVHGGG NKINEFLEKI NKKSTFINGL RITDAETLEI
     VEMVLCGLVN KNITQLINNA GGNAIGLCGK DANLIEAKKI CYTYKENQSN NVEKILDMGF
     VGEPHDINTD LLFFMEESDF IPVIAPVCSG ENNLTYNVNA DLVAGALANA MAAAKLIILT
     NVSGVTDSNG NLISELSVSH AENLIDNGTA HTGMIPKLQT CVRVVKEGYG SAHIIDGRIP
     HVLLLELFTI HGTGTMVVNS GV