HMUDK_BPS10
ID HMUDK_BPS10 Reviewed; 637 AA.
AC F8WQ30;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 03-AUG-2022, entry version 25.
DE RecName: Full=5-hmdU DNA kinase {ECO:0000303|PubMed:34522950};
DE AltName: Full=5-hydroxymethyluracil DNA kinase {ECO:0000303|PubMed:34522950};
DE AltName: Full=P-loop kinase {ECO:0000303|PubMed:34522950};
DE AltName: Full=gp186;
OS Bacillus phage SP10 (Bacillus phage SP-10).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Herelleviridae; Spounavirinae; unclassified Spounavirinae.
OX NCBI_TaxID=941058;
OH NCBI_TaxID=1423; Bacillus subtilis.
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND FUNCTION.
RX PubMed=21597187; DOI=10.1271/bbb.100921;
RA Yee L.M., Matsumoto T., Yano K., Matsuoka S., Sadaie Y., Yoshikawa H.,
RA Asai K.;
RT "The genome of Bacillus subtilis phage SP10: a comparative analysis with
RT phage SPO1.";
RL Biosci. Biotechnol. Biochem. 75:944-952(2011).
RN [2]
RP FUNCTION.
RC STRAIN=Mutant hmd1, and Mutant hmd2;
RX PubMed=6792371; DOI=10.1128/jvi.39.2.536-547.1981;
RA Witmer H.;
RT "Synthesis of deoxythymidylate and the unusual deoxynucleotide in mature
RT DNA of Bacillus subtilis bacteriophage SP10 occurs by postreplicational
RT modification of 5-hydroxymethyldeoxyuridylate.";
RL J. Virol. 39:536-547(1981).
RN [3]
RP FUNCTION.
RC STRAIN=Mutant hmd1, and Mutant hmd2;
RX PubMed=16789224; DOI=10.1128/jvi.42.2.636-648.1982;
RA Witmer H., Franks M.;
RT "DNA Synthesis and Gene Expression in Bacillus subtilis Infected with Wild-
RT Type and Hypermodification-Defective Bacteriophage SP10.";
RL J. Virol. 42:636-648(1982).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND DOMAIN.
RX PubMed=34522950; DOI=10.1093/nar/gkab781;
RA Lee Y.J., Dai N., Mueller S.I., Guan C., Parker M.J., Fraser M.E.,
RA Walsh S.E., Sridar J., Mulholland A., Nayak K., Sun Z., Lin Y.C.,
RA Comb D.G., Marks K., Gonzalez R., Dowling D.P., Bandarian V., Saleh L.,
RA Correa I.R., Weigele P.R.;
RT "Pathways of thymidine hypermodification.";
RL Nucleic Acids Res. 0:0-0(2021).
CC -!- FUNCTION: Phosphorylates 5-hydroxymethyluracil (5hmdU) into 5-
CC phosphomethyl-2'-deoxyuridine (5- PmdU) on DNA as a step in the pathway
CC leading to thymidine hypermodifications in the viral genome
CC (PubMed:34522950). The phosphate is added internally to the DNA polymer
CC (PubMed:34522950). As a final result of the pathway of
CC hypermodification, alpha-glutamylthymidine (YdTMP) substitutes for
CC about 20% of the thymidines in the viral DNA, the 80% left are dTMP
CC (PubMed:34522950, PubMed:6792371, PubMed:16789224). These modifications
CC probably prevent degradation of viral genome by the host restriction-
CC modification antiviral defense system (PubMed:34522950,
CC PubMed:21597187). {ECO:0000269|PubMed:16789224,
CC ECO:0000269|PubMed:21597187, ECO:0000269|PubMed:34522950,
CC ECO:0000269|PubMed:6792371}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-hydroxymethyl-dUMP in DNA + ATP = 5-phosphomethyl-dUMP in
CC DNA + ADP + H(+); Xref=Rhea:RHEA:71543, Rhea:RHEA-COMP:18039,
CC Rhea:RHEA-COMP:18041, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:190917, ChEBI:CHEBI:190918, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:34522950};
CC -!- DOMAIN: The N-terminus contains the 5-hmdU DNA kinase activity.
CC {ECO:0000269|PubMed:34522950}.
CC -!- MISCELLANEOUS: Mutants hmdl and hmd2 are heat-sensitive mutants
CC defective in thymidine hypermodifications with accumulation of 5- PPmdU
CC and 5hmdU, respectively. {ECO:0000269|PubMed:6792371}.
CC -!- SIMILARITY: Belongs to the thymidylate kinase family. 5-hmdU DNA kinase
CC subfamily. {ECO:0000305}.
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DR EMBL; AB605730; BAK52998.1; -; Genomic_DNA.
DR RefSeq; YP_007003443.1; NC_019487.1.
DR GeneID; 14007383; -.
DR KEGG; vg:14007383; -.
DR Proteomes; UP000207621; Genome.
DR InterPro; IPR040684; Alpha_GPT-Pplase1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR040924; Ploopntkinase1.
DR Pfam; PF18723; aGPT-Pplase1; 1.
DR Pfam; PF18748; Ploopntkinase1; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW Host-virus interaction; Multifunctional enzyme; Reference proteome;
KW Restriction-modification system evasion by virus.
FT CHAIN 1..637
FT /note="5-hmdU DNA kinase"
FT /id="PRO_0000456266"
SQ SEQUENCE 637 AA; 73960 MW; C027418B0A1A914D CRC64;
MKTKEEFHRI EISKFTEDLR EAFGYKIQYR QDLVLVNIRG CNGAGKSTVP MQMLQTDPGA
FMLTLDGKDK ATVFPSYGFV AMGRYFSKTG GLDGFKNNEE TLKVLKLLWE LPFSIIMEGV
ISSTIFSTYC DLFKELEQRN NPKRAVGVLN LLPPFEVCLE RIKKRTPEKF DSIKKDQIEG
KWRTVNRNAQ KFRDAGVTSW DEDNSVIDIN DTVSWFFSSI KNNLQPEFTG LRLGVRFPTE
EPVKALKKAE KGVKRGKKGR KTSPVAKTLD DNGDGAFLRS LKREIRPHWD PKYLNTPDDN
VRLRRDPETG QTLWDMYFIN LVERQNIWYR RVIQGKSKPW TDDPVMSTYH FTNVDRRLDR
VTLHYIDKVL CNLEDSYESK KFLLLNTFIY RLFVRPETTD AMGYIFPETF EEDWERAKAA
LRARRESGEP VFTDAYFVND LKSANPDRAN SSNKTENAIH LIQFIIDHLD ELAEFTFNPK
NSMEEVIEKF TMIPAVGNFN AYEVALDLGI VKEMTGIDFV DWTPDHYANV GPGCKKGIEY
VFEDLGNMSH LDIVFFITSV YKGELERLGL EYKYQEGCKE LDLRALEGWC CEMSKYFNYY
ATERGYDWAK GKRPKKKMNL RTDDVSYLNP RISNLVK
