ID   Y2030_MYCTU             Reviewed;         681 AA.
AC   P9WLM1; L0T8K6; O53475; Q7D7L3;
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=Uncharacterized protein Rv2030c;
GN   OrderedLocusNames=Rv2030c;
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   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   [4]
RP   INDUCTION BY CARBON MONOXIDE (CO).
RC   STRAIN=ATCC 35801 / TMC 107 / Erdman;
RX   PubMed=18474359; DOI=10.1016/j.chom.2008.03.007;
RA   Shiloh M.U., Manzanillo P., Cox J.S.;
RT   "Mycobacterium tuberculosis senses host-derived carbon monoxide during
RT   macrophage infection.";
RL   Cell Host Microbe 3:323-330(2008).
RN   [5]
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   [6]
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:11416222, ECO:0000269|PubMed:12953092,
CC       ECO:0000269|PubMed:18400743, ECO:0000269|PubMed:18474359}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the purine/pyrimidine
CC       phosphoribosyltransferase family. {ECO:0000305}.
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DR   EMBL; AL123456; CCP44803.1; -; Genomic_DNA.
DR   PIR; E70942; E70942.
DR   RefSeq; NP_216546.1; NC_000962.3.
DR   RefSeq; WP_003410178.1; NZ_NVQJ01000046.1.
DR   AlphaFoldDB; P9WLM1; -.
DR   SMR; P9WLM1; -.
DR   STRING; 83332.Rv2030c; -.
DR   PaxDb; P9WLM1; -.
DR   PRIDE; P9WLM1; -.
DR   GeneID; 887536; -.
DR   KEGG; mtu:Rv2030c; -.
DR   PATRIC; fig|83332.111.peg.2263; -.
DR   TubercuList; Rv2030c; -.
DR   eggNOG; COG1926; Bacteria.
DR   eggNOG; COG2312; Bacteria.
DR   OMA; SHYYHVR; -.
DR   PhylomeDB; P9WLM1; -.
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:0005886; C:plasma membrane; HDA:MTBBASE.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046677; P:response to antibiotic; IEA:InterPro.
DR   CDD; cd14728; Ere-like; 1.
DR   CDD; cd06223; PRTases_typeI; 1.
DR   Gene3D; 3.40.50.2020; -; 1.
DR   InterPro; IPR007815; Emycin_Estase.
DR   InterPro; IPR000836; PRibTrfase_dom.
DR   InterPro; IPR029057; PRTase-like.
DR   Pfam; PF05139; Erythro_esteras; 1.
DR   Pfam; PF00156; Pribosyltran; 1.
DR   SUPFAM; SSF53271; SSF53271; 1.
PE   1: Evidence at protein level;
KW   Reference proteome; Transferase.
FT   CHAIN           1..681
FT                   /note="Uncharacterized protein Rv2030c"
FT                   /id="PRO_0000392909"
SQ   SEQUENCE   681 AA;  74930 MW;  82DAC6ACC5550947 CRC64;
     MLMTAAADVT RRSPRRVFRD RREAGRVLAE LLAAYRDQPD VIVLGLARGG LPVAWEVAAA
     LHAPLDAFVV RKLGAPGHDE FAVGALASGG RVVVNDDVVR GLRITPQQLR DIAEREGREL
     LRRESAYRGE RPPTDITGKT VIVVDDGLAT GASMFAAVQA LRDAQPAQIV IAVPAAPEST
     CREFAGLVDD VVCATMPTPF LAVGESFWDF RQVTDEEVRR LLATPTAGPS LRRPAASTAA
     DVLRRVAIDA PGGVPTHEVL AELVGDARIV LIGESSHGTH EFYQARAAMT QWLIEEKGFG
     AVAAEADWPD AYRVNRYVRG LGEDTNADEA LSGFERFPAW MWRNTVVRDF VEWLRTRNQR
     YESGALRQAG FYGLDLYSLH RSIQEVISYL DKVDPRAAAR ARARYACFDH ACADDGQAYG
     FAAAFGAGPS CEREAVEQLV DVQRNALAYA RQDGLLAEDE LFYAQQNAQT VRDAEVYYRA
     MFSGRVTSWN LRDQHMAQTL GSLLTHLDRH LDAPPARIVV WAHNSHVGDA RATEVWADGQ
     LTLGQIVRER YGDESRSIGF STYTGTVTAA SEWGGIAQRK AVRPALHGSV EELFHQTADS
     FLVSARLSRD AEAPLDVVRL GRAIGVVYLP ATERQSHYLH VRPADQFDAM IHIDQTRALE
     PLEVTSRWIA GENPETYPTG L