MPTB_CORGL
ID MPTB_CORGL Reviewed; 602 AA.
AC Q8NQ73; Q6M526;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 2.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Alpha-(1->6)-mannopyranosyltransferase B;
DE Short=MptB;
DE EC=2.4.1.-;
DE AltName: Full=Polyprenyl-1-monophosphorylmannose dependent alpha-(1->6)mannopyranosyltransferase;
DE Short=PPM-dependent alpha-(1->6)mannopyranosyltransferase;
GN Name=mptB; OrderedLocusNames=Cgl1566, cg1766;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
RN [3]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND NOMENCLATURE.
RX PubMed=18452585; DOI=10.1111/j.1365-2958.2008.06265.x;
RA Mishra A.K., Alderwick L.J., Rittmann D., Wang C., Bhatt A.,
RA Jacobs W.R. Jr., Takayama K., Eggeling L., Besra G.S.;
RT "Identification of a novel alpha(1-->6) mannopyranosyltransferase MptB from
RT Corynebacterium glutamicum by deletion of a conserved gene, NCgl1505,
RT affords a lipomannan- and lipoarabinomannan-deficient mutant.";
RL Mol. Microbiol. 68:1595-1613(2008).
CC -!- FUNCTION: Involved in the initiation of core alpha-(1->6) mannan
CC biosynthesis of lipomannan (LM-A) and multi-mannosylated polymer (LM-
CC B), extending triacylatedphosphatidyl-myo-inositol dimannoside
CC (Ac1PIM2) and mannosylated glycolipid, 1,2-di-O-C16/C18:1-(alpha-D-
CC mannopyranosyl)-(1->4)-(alpha-D-glucopyranosyluronic acid)-(1->3)-
CC glycerol (Man1GlcAGroAc2), respectively. Catalyzes the addition of
CC alpha-(1->6)-mannose residue. {ECO:0000269|PubMed:18452585}.
CC -!- PATHWAY: Cell wall biogenesis; cell wall polysaccharide biosynthesis.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305|PubMed:18452585}; Multi-
CC pass membrane protein {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are unable to synthesize
CC lipoglycans (LM-A, LM-B and lipoarabinomannan (LAM)).
CC {ECO:0000269|PubMed:18452585}.
CC -!- SIMILARITY: Belongs to the MptA/B family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB98959.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BA000036; BAB98959.1; ALT_INIT; Genomic_DNA.
DR EMBL; BX927152; CAF21575.1; -; Genomic_DNA.
DR RefSeq; NP_600781.1; NC_003450.3.
DR AlphaFoldDB; Q8NQ73; -.
DR STRING; 196627.cg1766; -.
DR TCDB; 9.B.225.1.1; the mannosyl transferase (mptb) family.
DR KEGG; cgb:cg1766; -.
DR KEGG; cgl:Cgl1566; -.
DR PATRIC; fig|196627.13.peg.1528; -.
DR eggNOG; ENOG502Z9GU; Bacteria.
DR HOGENOM; CLU_023913_0_0_11; -.
DR UniPathway; UPA00963; -.
DR Proteomes; UP000000582; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0045227; P:capsule polysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
PE 3: Inferred from homology;
KW Cell wall biogenesis/degradation; Glycosyltransferase; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..602
FT /note="Alpha-(1->6)-mannopyranosyltransferase B"
FT /id="PRO_0000420593"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 244..264
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 274..294
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 320..340
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 368..388
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 404..424
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 448..468
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 472..492
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 503..523
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 546..566
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 571..591
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 602 AA; 64199 MW; 5748C090D7EA0FA5 CRC64;
MFSAPLRRMM RVTKDEQIQP NSNAPENRKW FPRAPRPLRQ FLDTLPRIGT AGSRSATLHV
EDEQSPLGAT LFDVATGASS INDRDTDASG LEPEKIRRFA WLRLIGTMGA LMIAFGALGA
GALPVVNNPY VDFPGGNFMS RMLQTSSMIV LIGVGFLVLA WVLMAPLVGI PFKRSGNRTA
SVSLSMLRRT FGAWVAPIML TAPLFTQDIY SYLAQGSVTA QGMDAYAGGP LELLGPDNHL
ARSVPFIWAQ SPSPYGPVAL SIAASISVIT NDSIVGGVLA HRIASLLGVV AAGWAITMLA
RRCRVSEEAS FYLGVLNPLL ILHLIGGIHN ESILLGFLLV GLELGLRGTD RIQTGLWGPA
WTYIALSGVL ISCAGLVKVT GFIGLGFVGM ALARAFHARG HRHVVAIGVA GLVQVAALVI
TVVVLSVITG ISLGWITGQG GAATIRSWMS MTTNIGVISG FIGMNLGLGD HTAAMLVVTR
AAGIAVAAAF MVRMLFATYR GHIHAVGGLG VATFVLVILF PVVHPWYMLW AIVPLASWAN
RLFFQLGVIA YSTAFSFFVL PRGLALPVGT VFSIYFGAAL GFSILLLVGW WSLRRNPTFG
LH
