ID   GLYTR_MYCTU             Reviewed;         342 AA.
AC   P9WMX5; L0T716; P71781; Q7D8C9;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 37.
DE   RecName: Full=Putative glycosyltransferases;
DE            EC=2.4.-.-;
GN   Name=pimF; OrderedLocusNames=Rv1500;
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   NOMENCLATURE.
RX   PubMed=14960574; DOI=10.1074/jbc.m400791200;
RA   Alexander D.C., Jones J.R., Tan T., Chen J.M., Liu J.;
RT   "PimF, a mannosyltransferase of mycobacteria, is involved in the
RT   biosynthesis of phosphatidylinositol mannosides and lipoarabinomannan.";
RL   J. Biol. Chem. 279:18824-18833(2004).
RN   [3]
RP   IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
RX   PubMed=19099550; DOI=10.1186/1752-0509-2-109;
RA   Raman K., Yeturu K., Chandra N.;
RT   "targetTB: a target identification pipeline for Mycobacterium tuberculosis
RT   through an interactome, reactome and genome-scale structural analysis.";
RL   BMC Syst. Biol. 2:109-109(2008).
RN   [4]
RP   FUNCTION AS A GLYCOSYLTRANSFERASE, AND LACK OF FUNCTION AS A
RP   MANNOSYLTRANSFERASE.
RX   PubMed=18585090; DOI=10.1016/j.ijmm.2008.03.010;
RA   Malm S., Walter K., Engel R., Maass S., Pfau S., Hubner G., Lindner B.,
RA   Holst O., Ehlers S., Bange F.C.;
RT   "In vitro and in vivo characterization of a Mycobacterium tuberculosis
RT   mutant deficient in glycosyltransferase Rv1500.";
RL   Int. J. Med. Microbiol. 298:645-655(2008).
RN   [5]
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 play only a redundant role in maintaining cell wall
CC       viability and bacterial virulence. {ECO:0000269|PubMed:18585090}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- MISCELLANEOUS: Was identified as a high-confidence drug target.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
CC   -!- CAUTION: Was originally thought (PubMed:14960574) to be a
CC       mannosyltransferase involved in the biosynthesis of
CC       phosphatidylinositol mannosides (PIMs), but further in vivo and in
CC       vitro characterizations (PubMed:18585090) clearly show that
CC       inactivation of Rv1500 does not affect the expression pattern of PIMs.
CC       {ECO:0000305|PubMed:14960574, ECO:0000305|PubMed:18585090}.
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DR   EMBL; AL123456; CCP44262.1; -; Genomic_DNA.
DR   PIR; G70712; G70712.
DR   RefSeq; NP_216016.1; NC_000962.3.
DR   RefSeq; WP_003407612.1; NZ_NVQJ01000004.1.
DR   AlphaFoldDB; P9WMX5; -.
DR   SMR; P9WMX5; -.
DR   STRING; 83332.Rv1500; -.
DR   PaxDb; P9WMX5; -.
DR   DNASU; 886492; -.
DR   GeneID; 45425480; -.
DR   GeneID; 886492; -.
DR   KEGG; mtu:Rv1500; -.
DR   TubercuList; Rv1500; -.
DR   eggNOG; COG1216; Bacteria.
DR   OMA; PLRMWTY; -.
DR   PhylomeDB; P9WMX5; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR001173; Glyco_trans_2-like.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   Pfam; PF00535; Glycos_transf_2; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Glycosyltransferase; Membrane; Reference proteome;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..342
FT                   /note="Putative glycosyltransferases"
FT                   /id="PRO_0000393107"
FT   TRANSMEM        227..247
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        262..282
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   342 AA;  38095 MW;  69373418DD844255 CRC64;
     MRLSIVTTMY MSEPYVLEFY RRARAAADKI TPDVEIIFVD DGSPDAALQQ AVSLLDSDPC
     VRVIQLSRNF GHHKAMMTGL AHATGDLVFL IDSDLEEDPA LLEPFYEKLI STGADVVFGC
     HARRPGGWLR NFGPKIHYRA SALLCDPPLH ENTLTVRLMT ADYVRSLVQH QERELSIAGL
     WQITGFYQVP MSVNKAWKGT TTYTFRRKVA TLVDNVTSFS NKPLVFIFYL GAAIFIISSS
     AAGYLIIDRI FFRALQAGWA SVIVSIWMLG GVTIFCIGLV GIYVSKVFIE TKQRPYTIIR
     RIYGSDLTTR EPSSLKTAFP AAHLSNGKRV TSEPEGLATG NR