ID A0A0R1Z9Y3_9LACO Unreviewed; 188 AA.
AC A0A0R1Z9Y3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=UDP-N-acetylglucosamine kinase {ECO:0000256|ARBA:ARBA00011963};
DE EC=2.7.1.176 {ECO:0000256|ARBA:ARBA00011963};
DE AltName: Full=UDP-N-acetylglucosamine kinase {ECO:0000256|ARBA:ARBA00032897};
GN ORFNames=FC64_GL000915 {ECO:0000313|EMBL:KRM51728.1};
OS Ligilactobacillus araffinosus DSM 20653.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Ligilactobacillus.
OX NCBI_TaxID=1423820 {ECO:0000313|EMBL:KRM51728.1, ECO:0000313|Proteomes:UP000051291};
RN [1] {ECO:0000313|EMBL:KRM51728.1, ECO:0000313|Proteomes:UP000051291}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20653 {ECO:0000313|EMBL:KRM51728.1,
RC ECO:0000313|Proteomes:UP000051291};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + UDP-N-acetyl-alpha-D-glucosamine = ADP + H(+) + UDP-N-
CC acetyl-alpha-D-glucosamine 3'-phosphate; Xref=Rhea:RHEA:32671,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57705,
CC ChEBI:CHEBI:64353, ChEBI:CHEBI:456216; EC=2.7.1.176;
CC Evidence={ECO:0000256|ARBA:ARBA00000912};
CC -!- SIMILARITY: Belongs to the zeta toxin family.
CC {ECO:0000256|ARBA:ARBA00009104}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRM51728.1}.
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DR EMBL; AYYZ01000029; KRM51728.1; -; Genomic_DNA.
DR RefSeq; WP_057906785.1; NZ_AYYZ01000029.1.
DR AlphaFoldDB; A0A0R1Z9Y3; -.
DR STRING; 1423820.FC64_GL000915; -.
DR PATRIC; fig|1423820.4.peg.937; -.
DR Proteomes; UP000051291; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:InterPro.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR010488; Zeta_toxin_domain.
DR PANTHER; PTHR39206; SLL8004 PROTEIN; 1.
DR PANTHER; PTHR39206:SF1; SLL8004 PROTEIN; 1.
DR Pfam; PF06414; Zeta_toxin; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000051291};
KW Toxin-antitoxin system {ECO:0000256|ARBA:ARBA00022649}.
FT DOMAIN 3..159
FT /note="Zeta toxin"
FT /evidence="ECO:0000259|Pfam:PF06414"
SQ SEQUENCE 188 AA; 21840 MW; 5485499102DC0A23 CRC64;
MAKKLVLLMG INGAGKTTLR NSQQLKADDA QTIDSDEFLQ AAKGNWRRKD DRIKAILQAD
QKLNLLIEKN VDIIWELEAV GSLHNELNII TKAKDQRYDV ELVWVTLDRP ELALKRVLSR
FREGGIGGSQ IDVPQRYRRV NDNFIKLEML ADQVVIYDNT FEMKKVYEKQ DNKEVLNKLI
DYPWIKIK
//