ID   Y2006_MYCTU             Reviewed;        1327 AA.
AC   P9WN15; L0T8I0; Q10850;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 40.
DE   RecName: Full=Uncharacterized glycosyl hydrolase Rv2006;
DE            EC=3.2.1.-;
GN   OrderedLocusNames=Rv2006; ORFNames=MTCY39.11c;
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   LACK OF FUNCTION AS A TREHALOSE-PHOSPHATE PHOSPHATASE.
RX   PubMed=15703182; DOI=10.1074/jbc.m414232200;
RA   Murphy H.N., Stewart G.R., Mischenko V.V., Apt A.S., Harris R.,
RA   McAlister M.S.B., Driscoll P.C., Young D.B., Robertson B.D.;
RT   "The OtsAB pathway is essential for trehalose biosynthesis in Mycobacterium
RT   tuberculosis.";
RL   J. Biol. Chem. 280:14524-14529(2005).
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   BIOTECHNOLOGY.
RX   PubMed=19553548; DOI=10.1128/cvi.00111-09;
RA   Black G.F., Thiel B.A., Ota M.O., Parida S.K., Adegbola R., Boom W.H.,
RA   Dockrell H.M., Franken K.L., Friggen A.H., Hill P.C., Klein M.R.,
RA   Lalor M.K., Mayanja H., Schoolnik G., Stanley K., Weldingh K.,
RA   Kaufmann S.H., Walzl G., Ottenhoff T.H.;
RT   "Immunogenicity of novel DosR regulon-encoded candidate antigens of
RT   Mycobacterium tuberculosis in three high-burden populations in Africa.";
RL   Clin. Vaccine Immunol. 16:1203-1212(2009).
RN   [7]
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       ECO:0000269|PubMed:18474359}.
CC   -!- BIOTECHNOLOGY: This protein serves as an immunogenic antigen, inducing
CC       gamma-interferon responses in whole-blood cultures from M.tuberculosis-
CC       exposed adults in Uganda, The Gambia and South Africa, indicating this
CC       might be a good vaccine candidate. {ECO:0000269|PubMed:19553548}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the trehalose
CC       phosphatase family. {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the glycosyl
CC       hydrolase 65 family. {ECO:0000305}.
CC   -!- CAUTION: Despite its similarity with the trehalose-phosphate
CC       phosphatase enzymes, it does not display trehalose-phosphate
CC       phosphatase activity. {ECO:0000305}.
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DR   EMBL; AL123456; CCP44778.1; -; Genomic_DNA.
DR   PIR; D70759; D70759.
DR   RefSeq; WP_003410063.1; NZ_NVQJ01000043.1.
DR   RefSeq; YP_177855.1; NC_000962.3.
DR   AlphaFoldDB; P9WN15; -.
DR   SMR; P9WN15; -.
DR   STRING; 83332.Rv2006; -.
DR   PaxDb; P9WN15; -.
DR   PRIDE; P9WN15; -.
DR   GeneID; 888943; -.
DR   KEGG; mtu:Rv2006; -.
DR   TubercuList; Rv2006; -.
DR   eggNOG; COG0561; Bacteria.
DR   eggNOG; COG0637; Bacteria.
DR   eggNOG; COG1554; Bacteria.
DR   OMA; WIPDNSR; -.
DR   PhylomeDB; P9WN15; -.
DR   BioCyc; MetaCyc:G185E-6208-MON; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005576; C:extracellular region; 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:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProt.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IBA:GO_Central.
DR   GO; GO:0016791; F:phosphatase activity; IEA:UniProt.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IBA:GO_Central.
DR   GO; GO:0005992; P:trehalose biosynthetic process; IEA:InterPro.
DR   Gene3D; 1.10.150.240; -; 1.
DR   Gene3D; 1.50.10.10; -; 1.
DR   Gene3D; 2.70.98.40; -; 1.
DR   Gene3D; 3.40.50.1000; -; 2.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR005194; Glyco_hydro_65_C.
DR   InterPro; IPR005195; Glyco_hydro_65_M.
DR   InterPro; IPR005196; Glyco_hydro_65_N.
DR   InterPro; IPR037018; Glyco_hydro_65_N_sf.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR006379; HAD-SF_hydro_IIB.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR023198; PGP-like_dom2.
DR   InterPro; IPR003337; Trehalose_PPase.
DR   Pfam; PF03633; Glyco_hydro_65C; 1.
DR   Pfam; PF03632; Glyco_hydro_65m; 1.
DR   Pfam; PF03636; Glyco_hydro_65N; 1.
DR   Pfam; PF02358; Trehalose_PPase; 1.
DR   SUPFAM; SSF48208; SSF48208; 1.
DR   SUPFAM; SSF56784; SSF56784; 2.
DR   SUPFAM; SSF74650; SSF74650; 1.
DR   TIGRFAMs; TIGR01484; HAD-SF-IIB; 1.
DR   TIGRFAMs; TIGR00685; T6PP; 1.
PE   1: Evidence at protein level;
KW   Glycosidase; Hydrolase; Reference proteome.
FT   CHAIN           1..1327
FT                   /note="Uncharacterized glycosyl hydrolase Rv2006"
FT                   /id="PRO_0000108019"
FT   ACT_SITE        1023
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:D6XZ22"
FT   BINDING         884..885
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:D6XZ22"
FT   BINDING         1143..1144
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:D6XZ22"
SQ   SEQUENCE   1327 AA;  145784 MW;  21F3BBC2F4CF9D91 CRC64;
     MRCGIVVNVT GPPPTIDRRY HDAVIVGLDN VVDKATRVHA AAWTKFLDDY LTRRPQRTGE
     DHCPLTHDDY RRFLAGKPDG VADFLAARGI RLPPGSPTDL TDDTVYGLQN LERQTFLQLL
     NTGVPEGKSI ASFARRLQVA GVRVAAHTSH RNYGHTLDAT GLAEVFAVFV DGAVTAELGL
     PAEPNPAGLI ETAKRLGANP GRCVVIDSCQ TGLRAGRNGG FALVIAVDAH GDAENLLSSG
     ADAVVADLAA VTVGSGDAAI STIPDALQVY SQLKRLLTGR RPAVFLDFDG TLSDIVERPE
     AATLVDGAAE ALRALAAQCP VAVISGRDLA DVRNRVKVDG LWLAGSHGFE LVAPDGSHHQ
     NAAATAAIDG LAEAAAQLAD ALREIAGAVV EHKRFAVAVH YRNVADDSVD NLIAAVRRLG
     HAAGLRVTTG RKVVELRPDI AWDKGKALDW IGERLGPAEV GPDLRLPIYI GDDLTDEDAF
     DAVRFTGVGI VVRHNEHGDR RSAATFRLEC PYTVCQFLSQ LACDLQEAVQ HDDPWTLVFH
     GYDPGQERLR EALCAVGNGY LGSRGCAPES AESEAHYPGT YVAGVYNQLT DHIEGCTVDN
     ESLVNLPNWL SLTFRIDGGA WFNVDTVELL SYRQTFDLRR ATLTRSLRFR DAGGRVTTMT
     QERFASMNRP NLVALQTRIE SENWSGTVDF RSLVDGGVHN TLVDRYRQLS SQHLTTAEIE
     VLADSVLLRT QTSQSGIAIA VAARSTLWRD GQRVDAQYRV ARDTNRGGHD IQVTLSAGQS
     VTLEKVATIF TSRDAATLTA AISAQRCLGE AGRYAELCQQ HVRAWARLWE RCAIDLTGNT
     EELRLVRLHL LHLLQTISPH TAELDAGVPA RGLNGEAYRG HVFWDALFVA PVLSLRMPKV
     ARSLLDYRYR RLPAARRAAH RAGHLGAMYP WQSGSDGSEV SQQLHLNPRS GRWTPDPSDR
     AHHVGLAVAY NAWHYYQVTG DRQYLVDCGA ELLVEIARFW VGLAKLDDSR GRYLIRGVIG
     PDEFHSGYPG NEYDGIDNNA YTNVMAVWVI LRAMEALDLL PLTDRRHLIE KLGLTTQERD
     QWDDVSRRMF VPFHDGVISQ FEGYSELAEL DWDHYRHRYG NIQRLDRILE AEGDSVNNYQ
     ASKQADALML LYLLSSDELI GLLARLGYRF APTQIPGTVD YYLARTSDGS TLSAVVHAWV
     LARANRSNAM EYFRQVLRSD IADVQGGTTQ EGIHLAAMAG SIDLLQRCYS GLELRDDRLV
     LSPQWPEALG PLEFPFVYRR HQLSLRISGR SATLTAESGD AEPIEVECRG HVQRLRCGHT
     IEVGCSR