AMGK_CAUVC
ID AMGK_CAUVC Reviewed; 363 AA.
AC Q9A2M2;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 106.
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=CC_3535 {ECO:0000312|EMBL:AAK25497.1};
OS Caulobacter vibrioides (strain ATCC 19089 / CB15) (Caulobacter crescentus).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=190650;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19089 / CB15;
RX PubMed=11259647; DOI=10.1073/pnas.061029298;
RA Nierman W.C., Feldblyum T.V., Laub M.T., Paulsen I.T., Nelson K.E.,
RA Eisen J.A., Heidelberg J.F., Alley M.R.K., Ohta N., Maddock J.R.,
RA Potocka I., Nelson W.C., Newton A., Stephens C., Phadke N.D., Ely B.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H., Kolonay J.F.,
RA Smit J., Craven M.B., Khouri H.M., Shetty J., Berry K.J., Utterback T.R.,
RA Tran K., Wolf A.M., Vamathevan J.J., Ermolaeva M.D., White O.,
RA Salzberg S.L., Venter J.C., Shapiro L., Fraser C.M.;
RT "Complete genome sequence of Caulobacter crescentus.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4136-4141(2001).
RN [2]
RP FUNCTION, AND PATHWAY.
RC STRAIN=ATCC 19089 / CB15;
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; AE005673; AAK25497.1; -; Genomic_DNA.
DR PIR; E87687; E87687.
DR RefSeq; NP_422329.1; NC_002696.2.
DR RefSeq; WP_010921364.1; NC_002696.2.
DR AlphaFoldDB; Q9A2M2; -.
DR SMR; Q9A2M2; -.
DR STRING; 190650.CC_3535; -.
DR EnsemblBacteria; AAK25497; AAK25497; CC_3535.
DR KEGG; ccr:CC_3535; -.
DR PATRIC; fig|190650.5.peg.3541; -.
DR eggNOG; COG3178; Bacteria.
DR HOGENOM; CLU_021467_2_0_5; -.
DR OMA; SPNIIWR; -.
DR BioCyc; CAULO:CC3535-MON; -.
DR UniPathway; UPA00544; -.
DR Proteomes; UP000001816; 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..363
FT /note="N-acetylmuramate/N-acetylglucosamine kinase"
FT /id="PRO_0000441268"
SQ SEQUENCE 363 AA; 39979 MW; 4DCF182AA6A2622C CRC64;
MTLSSEREAA KAAFLSANGF GDVRRESLGG DASTRAYERL HRGEQSYIFM DQPPSLETAP
CPPDASPAER AALGYNALAR LAAGRVDAFV ACAGWLNAQG LSAPKVLAAD PAAGLAVLED
LGDDLYARLI EAGTDEAPLY DAAIDGLLAI HAAPTPKVLR YDGSTWPLLT YDDLALKTAH
DIFVEWQPRF RDISFDAAAL AEWEAIWAPI RAKGEADATV FCHRDYHAEN LIWLPERDGA
ARVGMLDFQD AVLAHPAWDL SMLLHDARRT VSPEREAACL DRYLAARPEL DRTAFLAGYH
ALGALNIIRI LGIFARLVTR DGKPRYADFI PRLWVYLDVC FADPALAELK AWFDRYVPVE
TRR
