ID   Y0571_MYCTU             Reviewed;         443 AA.
AC   P9WHK1; L0T5R8; O53768; Q7D9M2;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 37.
DE   RecName: Full=Putative phosphoribosyl transferase Rv0571c;
GN   OrderedLocusNames=Rv0571c;
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 NITRIC OXIDE (NO) AND BY HYPOXIA, AND DORMANCY REGULON.
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=12953092; DOI=10.1084/jem.20030205;
RA   Voskuil M.I., Schnappinger D., Visconti K.C., Harrell M.I., Dolganov G.M.,
RA   Sherman D.R., Schoolnik G.K.;
RT   "Inhibition of respiration by nitric oxide induces a Mycobacterium
RT   tuberculosis dormancy program.";
RL   J. Exp. Med. 198:705-713(2003).
RN   [3]
RP   INDUCTION BY CARBON MONOXIDE (CO), AND DORMANCY REGULON.
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=18400743; DOI=10.1074/jbc.m802274200;
RA   Kumar A., Deshane J.S., Crossman D.K., Bolisetty S., Yan B.S., Kramnik I.,
RA   Agarwal A., Steyn A.J.;
RT   "Heme oxygenase-1-derived carbon monoxide induces the Mycobacterium
RT   tuberculosis dormancy regulon.";
RL   J. Biol. Chem. 283:18032-18039(2008).
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   -!- INDUCTION: A member of the dormancy regulon. Induced in response to
CC       reduced oxygen tension (hypoxia), low levels of nitric oxide (NO) and
CC       carbon monoxide (CO). It is hoped that this regulon will give insight
CC       into the latent, or dormant phase of infection.
CC       {ECO:0000269|PubMed:12953092, ECO:0000269|PubMed:18400743}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the purine/pyrimidine
CC       phosphoribosyltransferase family. {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the dienelactone
CC       hydrolase family. {ECO:0000305}.
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DR   EMBL; AL123456; CCP43309.1; -; Genomic_DNA.
DR   PIR; B70933; B70933.
DR   RefSeq; NP_215085.1; NC_000962.3.
DR   RefSeq; WP_003403001.1; NZ_NVQJ01000036.1.
DR   AlphaFoldDB; P9WHK1; -.
DR   SMR; P9WHK1; -.
DR   STRING; 83332.Rv0571c; -.
DR   ESTHER; myctu-y0571; DLH-S.
DR   PaxDb; P9WHK1; -.
DR   DNASU; 887710; -.
DR   GeneID; 887710; -.
DR   KEGG; mtu:Rv0571c; -.
DR   TubercuList; Rv0571c; -.
DR   eggNOG; COG1073; Bacteria.
DR   eggNOG; COG1926; Bacteria.
DR   OMA; LARDWFT; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005829; C:cytosol; HDA:MTBBASE.
DR   GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR   GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   CDD; cd06223; PRTases_typeI; 1.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   Gene3D; 3.40.50.2020; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR002925; Dienelactn_hydro.
DR   InterPro; IPR000836; PRibTrfase_dom.
DR   InterPro; IPR029057; PRTase-like.
DR   Pfam; PF01738; DLH; 1.
DR   Pfam; PF00156; Pribosyltran; 1.
DR   SUPFAM; SSF53271; SSF53271; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   1: Evidence at protein level;
KW   Reference proteome; Transferase.
FT   CHAIN           1..443
FT                   /note="Putative phosphoribosyl transferase Rv0571c"
FT                   /id="PRO_0000392688"
SQ   SEQUENCE   443 AA;  46655 MW;  CC64EF0CE8C598A8 CRC64;
     MKLFDDRGDA GRQLAQRLAQ LSGKAVVVLG LPRGGVPVAF EVAKSLQAPL DVLVVRKLGV
     PFQPELAFGA IGEDGVRVLN DDVVRGTHLD AAAMDAVERK QLIELQRRAE RFRRGRDRIP
     LTGRIAVIVD DGIATGATAK AACQVARAHG ADKVVLAVPI GPDDIVARFA GYADEVVCLA
     TPALFFAVGQ GYRNFTQTSD DEVVAFLDRA HRDFAEAGAI DAAADPPLRD EEVQVVAGPV
     PVAGHLTVPE KPRGIVVFAH GSGSSRHSIR NRYVAEVLTG AGFATLLFDL LTPEEERNRA
     NVFDIELLAS RLIDVTGWLA TQPDTASLPV GYFGASTGAG AALVAAADPR VNVRAVVSRG
     GRPDLAGDSL GSVVAPTLLI VGGRDQVVLE LNQRAQAVIP GKCQLTVVPG ATHLFEEPGT
     LEQVAKLACD WFIDHLCGPG PSG