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Database: UniProt
Entry: W4AE81_9BACL
LinkDB: W4AE81_9BACL
Original site: W4AE81_9BACL 
ID   W4AE81_9BACL            Unreviewed;       190 AA.
AC   W4AE81;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 27.
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=C161_29248 {ECO:0000313|EMBL:ETT29669.1};
OS   Paenibacillus sp. FSL R5-192.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1226754 {ECO:0000313|EMBL:ETT29669.1, ECO:0000313|Proteomes:UP000019041};
RN   [1] {ECO:0000313|EMBL:ETT29669.1, ECO:0000313|Proteomes:UP000019041}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSL R5-192 {ECO:0000313|EMBL:ETT29669.1,
RC   ECO:0000313|Proteomes:UP000019041};
RX   PubMed=24422886; DOI=10.1186/1471-2164-15-26;
RA   Moreno Switt A.I., Andrus A.D., Ranieri M.L., Orsi R.H., Ivy R.,
RA   den Bakker H.C., Martin N.H., Wiedmann M., Boor K.J.;
RT   "Genomic comparison of sporeforming bacilli isolated from milk.";
RL   BMC Genomics 15:26-26(2014).
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:ETT29669.1}.
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DR   EMBL; ASPR01000078; ETT29669.1; -; Genomic_DNA.
DR   RefSeq; WP_036674731.1; NZ_ASPR01000078.1.
DR   AlphaFoldDB; W4AE81; -.
DR   PATRIC; fig|1226754.4.peg.5887; -.
DR   Proteomes; UP000019041; 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   Toxin-antitoxin system {ECO:0000256|ARBA:ARBA00022649}.
FT   DOMAIN          3..156
FT                   /note="Zeta toxin"
FT                   /evidence="ECO:0000259|Pfam:PF06414"
SQ   SEQUENCE   190 AA;  21280 MW;  8599F561BCD31611 CRC64;
     MSEIRPVMTV FAGTNGAGKS TLSMQMREWL GELVDPDQIA RELKPENPRS ADLSAGREAV
     KRIRSLIKSG VNFAIETTLS GSFVLKHMEI AKENSYEIVV YYIGLEDVQM HIDRVASRVE
     QGGHWIAEED IRYRYGQSLK NLKPALSIAD RVIIIDNTYE PLIVAEIIQG DLIYCVESIP
     AWANPVLVGY
//
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