MUTT4_MYCTU
ID MUTT4_MYCTU Reviewed; 248 AA.
AC P9WIX7; L0TFL7; O05437; Q8VIR0;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 35.
DE RecName: Full=Putative mutator protein MutT4;
DE EC=3.6.1.-;
GN Name=mutT4; OrderedLocusNames=Rv3908;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP INDUCTION BY HYPOXIA.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=11416222; DOI=10.1073/pnas.121172498;
RA Sherman D.R., Voskuil M., Schnappinger D., Liao R., Harrell M.I.,
RA Schoolnik G.K.;
RT "Regulation of the Mycobacterium tuberculosis hypoxic response gene
RT encoding alpha -crystallin.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7534-7539(2001).
RN [3]
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=16585780; DOI=10.1128/jb.188.8.3159-3161.2006;
RA Dos Vultos T., Blazquez J., Rauzier J., Matic I., Gicquel B.;
RT "Identification of Nudix hydrolase family members with an antimutator role
RT in Mycobacterium tuberculosis and Mycobacterium smegmatis.";
RL J. Bacteriol. 188:3159-3161(2006).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC -!- FUNCTION: May be involved in the GO system responsible for removing an
CC oxidatively damaged form of guanine (7,8-dihydro-8-oxoguanine, 8-oxo-
CC dGTP) from DNA and the nucleotide pool (By similarity). In vitro has
CC dATPase rather than 8-oxo-dGTPase activity. {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- INDUCTION: A possible member of the dormancy regulon. Induced in
CC response to reduced oxygen tension (hypoxia). It is hoped that this
CC regulon will give insight into the latent, or dormant phase of
CC infection. {ECO:0000269|PubMed:11416222}.
CC -!- DISRUPTION PHENOTYPE: None observed. {ECO:0000269|PubMed:16585780}.
CC -!- MISCELLANEOUS: There are 4 mutT paralogs in M.tuberculosis; the exact
CC function of each is unknown.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. {ECO:0000305}.
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DR EMBL; AL123456; CCP46737.1; -; Genomic_DNA.
DR PIR; E70600; E70600.
DR RefSeq; NP_218425.1; NC_000962.3.
DR RefSeq; WP_003400124.1; NZ_NVQJ01000005.1.
DR AlphaFoldDB; P9WIX7; -.
DR SMR; P9WIX7; -.
DR STRING; 83332.Rv3908; -.
DR PaxDb; P9WIX7; -.
DR DNASU; 886242; -.
DR GeneID; 45427908; -.
DR GeneID; 886242; -.
DR KEGG; mtu:Rv3908; -.
DR TubercuList; Rv3908; -.
DR eggNOG; COG0494; Bacteria.
DR OMA; NGCGQGP; -.
DR PhylomeDB; P9WIX7; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR020476; Nudix_hydrolase.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR020084; NUDIX_hydrolase_CS.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR Pfam; PF00293; NUDIX; 1.
DR PRINTS; PR00502; NUDIXFAMILY.
DR SUPFAM; SSF55811; SSF55811; 1.
DR PROSITE; PS51462; NUDIX; 1.
DR PROSITE; PS00893; NUDIX_BOX; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Magnesium; Manganese; Metal-binding; Mutator protein;
KW Reference proteome.
FT CHAIN 1..248
FT /note="Putative mutator protein MutT4"
FT /id="PRO_0000392934"
FT DOMAIN 62..198
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 103..124
FT /note="Nudix box"
FT BINDING 103
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 118
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT BINDING 121
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 122
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
SQ SEQUENCE 248 AA; 27171 MW; 270A5193861EADD3 CRC64;
MSDGEQAKSR RRRGRRRGRR AAATAENHMD AQPAGDATPT PATAKRSRSR SPRRGSTRMR
TVHETSAGGL VIDGIDGPRD AQVAALIGRV DRRGRLLWSL PKGHIELGET AEQTAIREVA
EETGIRGSVL AALGRIDYWF VTDGRRVHKT VHHYLMRFLG GELSDEDLEV AEVAWVPIRE
LPSRLAYADE RRLAEVADEL IDKLQSDGPA ALPPLPPSSP RRRPQTHSRA RHADDSAPGQ
HNGPGPGP
