ID   AMGK_NEIMB              Reviewed;         334 AA.
AC   Q9K188;
DT   30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=N-acetylmuramate/N-acetylglucosamine kinase {ECO:0000250|UniProtKB:Q88QT3};
DE            Short=MurNAc/GlcNAc kinase {ECO:0000250|UniProtKB:Q88QT3};
DE            EC=2.7.1.221 {ECO:0000250|UniProtKB:Q88QT3};
GN   Name=amgK {ECO:0000250|UniProtKB:Q88QT3};
GN   OrderedLocusNames=NMB0279 {ECO:0000312|EMBL:AAF40733.1};
OS   Neisseria meningitidis serogroup B (strain MC58).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=122586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC58;
RX   PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA   Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA   Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA   Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA   Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA   Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA   Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA   Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA   Moxon E.R., Rappuoli R., Venter J.C.;
RT   "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT   MC58.";
RL   Science 287:1809-1815(2000).
RN   [2]
RP   FUNCTION, AND PATHWAY.
RC   STRAIN=MC58;
RX   PubMed=23831760; DOI=10.1038/nchembio.1289;
RA   Gisin J., Schneider A., Naegele B., Borisova M., Mayer C.;
RT   "A cell wall recycling shortcut that bypasses peptidoglycan de novo
RT   biosynthesis.";
RL   Nat. Chem. Biol. 9:491-493(2013).
CC   -!- FUNCTION: Sugar kinase that catalyzes the ATP-dependent phosphorylation
CC       of N-acetylmuramate (MurNAc) and N-acetylglucosamine (GlcNAc) at its C1
CC       hydroxyl group, leading to MurNAc alpha-1P and GlcNAc alpha-1P,
CC       respectively (By similarity). Is likely involved in peptidoglycan
CC       recycling as part of a cell wall recycling pathway that bypasses de
CC       novo biosynthesis of the peptidoglycan precursor UDP-MurNAc
CC       (PubMed:23831760). Is able to complement the fosfomycin sensitivity
CC       phenotype of a P.putida mutant lacking amgK (PubMed:23831760).
CC       {ECO:0000250|UniProtKB:Q88QT3, ECO:0000269|PubMed:23831760}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + N-acetyl-D-muramate = ADP + H(+) + N-acetyl-alpha-D-
CC         muramate 1-phosphate; Xref=Rhea:RHEA:53720, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:28881, ChEBI:CHEBI:30616, ChEBI:CHEBI:137594,
CC         ChEBI:CHEBI:456216; EC=2.7.1.221;
CC         Evidence={ECO:0000250|UniProtKB:Q88QT3};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + N-acetyl-D-glucosamine = ADP + H(+) + N-acetyl-alpha-D-
CC         glucosamine 1-phosphate; Xref=Rhea:RHEA:53724, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:57776, ChEBI:CHEBI:456216,
CC         ChEBI:CHEBI:506227; Evidence={ECO:0000250|UniProtKB:Q88QT3};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan recycling.
CC       {ECO:0000305|PubMed:23831760}.
CC   -!- SIMILARITY: Belongs to the kinase AmgK family. {ECO:0000305}.
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DR   EMBL; AE002098; AAF40733.1; -; Genomic_DNA.
DR   PIR; D81217; D81217.
DR   RefSeq; NP_273335.1; NC_003112.2.
DR   RefSeq; WP_002224845.1; NC_003112.2.
DR   AlphaFoldDB; Q9K188; -.
DR   SMR; Q9K188; -.
DR   STRING; 122586.NMB0279; -.
DR   PaxDb; Q9K188; -.
DR   EnsemblBacteria; AAF40733; AAF40733; NMB0279.
DR   KEGG; nme:NMB0279; -.
DR   PATRIC; fig|122586.8.peg.348; -.
DR   HOGENOM; CLU_021467_1_0_4; -.
DR   OMA; HSRNLMV; -.
DR   UniPathway; UPA00544; -.
DR   Proteomes; UP000000425; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009254; P:peptidoglycan turnover; IEA:UniProtKB-UniPathway.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   InterPro; IPR002575; Aminoglycoside_PTrfase.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   Pfam; PF01636; APH; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Carbohydrate metabolism; Cell shape;
KW   Cell wall biogenesis/degradation; Kinase; Nucleotide-binding;
KW   Peptidoglycan synthesis; Reference proteome; Transferase.
FT   CHAIN           1..334
FT                   /note="N-acetylmuramate/N-acetylglucosamine kinase"
FT                   /id="PRO_0000441267"
SQ   SEQUENCE   334 AA;  39099 MW;  4AAB563963B0239B CRC64;
     MQRQIKLKNW LQTVYPERDF DLTFAAADAD FRRYFRATFS DGSSVVCMDA PPDKMSVAPY
     LKVQKLFDMV NVPQVLHADT DLGFVVLNDL GNTTFLTAML QEQGETAHKA LLLEAIGELV
     ELQKASREGV LPEYDRETML REINLFPEWF VAKELGRELT FKQRQLWQQT VDTLLPPLLA
     QPKVYVHRDF IVRNLMLTRG RPGVLDFQDA LYGPISYDLV SLLRDAFIEW EEEFVLDLVI
     RYWEKARAAG LPVPEAFDEF YRWFEWMGVQ RHLKVAGIFA RLYYRDGKDK YRPEIPRFLN
     YLRRVSRRYA ELAPLYALLV ELVGDEELET GFTF