AMGK_PSEAE
ID AMGK_PSEAE Reviewed; 338 AA.
AC Q9I5U1;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 112.
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};
DE AltName: Full=Anomeric sugar kinase {ECO:0000303|PubMed:24819062};
GN Name=amgK {ECO:0000303|PubMed:24819062};
GN OrderedLocusNames=PA0596 {ECO:0000312|EMBL:AAG03985.1};
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=24819062; DOI=10.1089/mdr.2014.0036;
RA Borisova M., Gisin J., Mayer C.;
RT "Blocking peptidoglycan recycling in Pseudomonas aeruginosa attenuates
RT intrinsic resistance to fosfomycin.";
RL Microb. Drug Resist. 20:231-237(2014).
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 involved in peptidoglycan recycling as
CC part of a cell wall recycling pathway that bypasses de novo
CC biosynthesis of the peptidoglycan precursor UDP-MurNAc
CC (PubMed:24819062). Plays a role in intrinsic resistance to fosfomycin,
CC which targets the de novo synthesis of UDP-MurNAc (PubMed:24819062).
CC {ECO:0000250|UniProtKB:Q88QT3, ECO:0000269|PubMed:24819062}.
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:0000269|PubMed:24819062}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene accumulate MurNAc.
CC Deletion of this gene increases fosfomycin sensitivity. Growth rate is
CC not affected. {ECO:0000269|PubMed:24819062}.
CC -!- SIMILARITY: Belongs to the kinase AmgK family. {ECO:0000305}.
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DR EMBL; AE004091; AAG03985.1; -; Genomic_DNA.
DR PIR; C83570; C83570.
DR RefSeq; NP_249287.1; NC_002516.2.
DR RefSeq; WP_003113208.1; NZ_QZGE01000010.1.
DR AlphaFoldDB; Q9I5U1; -.
DR SMR; Q9I5U1; -.
DR STRING; 287.DR97_3565; -.
DR PaxDb; Q9I5U1; -.
DR PRIDE; Q9I5U1; -.
DR DNASU; 882000; -.
DR EnsemblBacteria; AAG03985; AAG03985; PA0596.
DR GeneID; 882000; -.
DR KEGG; pae:PA0596; -.
DR PATRIC; fig|208964.12.peg.632; -.
DR PseudoCAP; PA0596; -.
DR HOGENOM; CLU_021467_1_0_6; -.
DR InParanoid; Q9I5U1; -.
DR OMA; HSRNLMV; -.
DR PhylomeDB; Q9I5U1; -.
DR BioCyc; PAER208964:G1FZ6-603-MON; -.
DR UniPathway; UPA00544; -.
DR Proteomes; UP000002438; 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 GO; GO:0046677; P:response to antibiotic; 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 Antibiotic resistance; ATP-binding; Carbohydrate metabolism; Cell shape;
KW Cell wall biogenesis/degradation; Kinase; Nucleotide-binding;
KW Peptidoglycan synthesis; Reference proteome; Transferase.
FT CHAIN 1..338
FT /note="N-acetylmuramate/N-acetylglucosamine kinase"
FT /id="PRO_0000441266"
SQ SEQUENCE 338 AA; 38186 MW; BA70559C06CD7C66 CRC64;
MSDDARFQQL NCWLDSCLPE LFVAEGWGEV PPAELIPASS DASFRRYFRW QGGDRSLVVM
DAPPPQEDCR PFVKVAGLLA GAGVHVPRIL AQDLENGFLL LSDLGRQTYL DVLHPGNADE
LFEPALDALI AFQKVDVAGV LPAYDEAVLR RELQLFPDWY LARHLGVELE GETLARWKRI
CDLLVRSALE QPRVFVHRDY MPRNLMLSEP NPGVLDFQDA LHGPVTYDVT CLYKDAFVSW
PEPRVHAALN RYWKKATWAG IPLPPSFEDF LRASDLMGVQ RHLKVIGIFA RICHRDGKPR
YLGDVPRFFR YLETAVARRP ELAELGELLA SLPQGAEA
