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Database: UniProt
Entry: T0V2L2_9STRE
LinkDB: T0V2L2_9STRE
Original site: T0V2L2_9STRE 
ID   T0V2L2_9STRE            Unreviewed;       252 AA.
AC   T0V2L2;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 30.
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=HSISM1_2168 {ECO:0000313|EMBL:EQC76094.1};
OS   Streptococcus sp. HSISM1.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1316408 {ECO:0000313|EMBL:EQC76094.1};
RN   [1] {ECO:0000313|EMBL:EQC76094.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HSISM1 {ECO:0000313|EMBL:EQC76094.1};
RA   Van den Bogert B., Boekhorst J., Herrmann R., Smid E.J., Zoetendal E.G.,
RA   Kleerebezem M.;
RT   "Comparative Genomics Analysis of Streptococcus Isolates from the Human
RT   Small Intestine Reveals their Adaptation to a Highly Dynamic Ecosystem.";
RL   PLoS ONE 8:E83418-E83418(2013).
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:EQC76094.1}.
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DR   EMBL; ASKI01000076; EQC76094.1; -; Genomic_DNA.
DR   AlphaFoldDB; T0V2L2; -.
DR   PATRIC; fig|1316408.3.peg.1744; -.
DR   eggNOG; COG4185; Bacteria.
DR   HOGENOM; CLU_064262_2_0_9; -.
DR   Proteomes; UP000015933; Chromosome.
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; IPR048180; PezT.
DR   InterPro; IPR010488; Zeta_toxin_domain.
DR   NCBIfam; NF041574; antitoxPezT_Strep; 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          26..215
FT                   /note="Zeta toxin"
FT                   /evidence="ECO:0000259|Pfam:PF06414"
SQ   SEQUENCE   252 AA;  28846 MW;  D9EE1DA8123AE7CC CRC64;
     MKLEEFSQDD FERASRRLVR SLTRGKTTSS QPKAILLGGQ SGAGKTTIHR IKQREFQGNI
     IIIDGDSYRS FHPNYLGLQK KYGKDSVDYT KVFAGKMVEY LVDELSKQGY HLLIEGTLRT
     TEVPRKTAQL LAIRGYQVSL ALIATKPELS YLSTLIRYEE LYAINPSQAR ATPKAHHDGI
     VEHLVDNLRE LENDKIFNQI QIYQRDQSCV YDSEVDQISA AEVLQECLFG KWNKVEKEML
     KMGKERLKEL GE
//
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