GLYTR_MYCTO
ID GLYTR_MYCTO Reviewed; 342 AA.
AC P9WMX4; 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 34.
DE RecName: Full=Putative glycosyltransferases;
DE EC=2.4.-.-;
GN Name=pimF; OrderedLocusNames=MT1549;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
CC -!- FUNCTION: May play only a redundant role in maintaining cell wall
CC viability and bacterial virulence. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
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DR EMBL; AE000516; AAK45815.1; -; Genomic_DNA.
DR PIR; G70712; G70712.
DR RefSeq; WP_003407612.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WMX4; -.
DR SMR; P9WMX4; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR EnsemblBacteria; AAK45815; AAK45815; MT1549.
DR GeneID; 45425480; -.
DR KEGG; mtc:MT1549; -.
DR PATRIC; fig|83331.31.peg.1666; -.
DR HOGENOM; CLU_033536_0_1_11; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 3: Inferred from homology;
KW Cell membrane; Glycosyltransferase; Membrane; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..342
FT /note="Putative glycosyltransferases"
FT /id="PRO_0000427226"
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