ID   ARGB_PROMH              Reviewed;         257 AA.
AC   B4F1G7;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 86.
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}; OrderedLocusNames=PMI3238;
OS   Proteus mirabilis (strain HI4320).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Proteus.
OX   NCBI_TaxID=529507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HI4320;
RX   PubMed=18375554; DOI=10.1128/jb.01981-07;
RA   Pearson M.M., Sebaihia M., Churcher C., Quail M.A., Seshasayee A.S.,
RA   Luscombe N.M., Abdellah Z., Arrosmith C., Atkin B., Chillingworth T.,
RA   Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA   Rabbinowitsch E., Walker D., Whithead S., Thomson N.R., Rather P.N.,
RA   Parkhill J., Mobley H.L.T.;
RT   "Complete genome sequence of uropathogenic Proteus mirabilis, a master of
RT   both adherence and motility.";
RL   J. Bacteriol. 190:4027-4037(2008).
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   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-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}.
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DR   EMBL; AM942759; CAR46340.1; -; Genomic_DNA.
DR   RefSeq; WP_012368683.1; NC_010554.1.
DR   AlphaFoldDB; B4F1G7; -.
DR   SMR; B4F1G7; -.
DR   STRING; 529507.PMI3238; -.
DR   EnsemblBacteria; CAR46340; CAR46340; PMI3238.
DR   GeneID; 6803007; -.
DR   KEGG; pmr:PMI3238; -.
DR   PATRIC; fig|529507.6.peg.3165; -.
DR   eggNOG; COG0548; Bacteria.
DR   HOGENOM; CLU_053680_1_1_6; -.
DR   OMA; EGLYEDW; -.
DR   UniPathway; UPA00068; UER00107.
DR   Proteomes; UP000008319; 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; cd04249; AAK_NAGK-NC; 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; IPR041731; NAGK-NC.
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; Reference proteome; Transferase.
FT   CHAIN           1..257
FT                   /note="Acetylglutamate kinase"
FT                   /id="PRO_1000092872"
FT   BINDING         43..44
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT   BINDING         65
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT   BINDING         157
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT   BINDING         180..185
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT   BINDING         208..210
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT   SITE            7
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT   SITE            216
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
SQ   SEQUENCE   257 AA;  27117 MW;  9318CD81D96B5EBB CRC64;
     MEPLIIKLGG VLLDNEKALT RFFTALQEYR TSHSRPLVIV HGGGCLVDSL MKKLQLPVVK
     KQGLRVTPAD QIDIITGALA GSANKTLLSW ATRFGLNGVG LCLGDGQLAK VTKISDELGH
     VGNAEPGSPE LLNLLLNAGY LPIISSIGVS IQGELMNVNA DQAATAIAET LGADLVLLSD
     VSGILDGKGQ KLTEISATKA QALIDQGIIT DGMIVKVNAA LEAARTLRRP VEIASWRHAE
     KLTDLFNGMV IGTRILA