PMT_CORGL
ID PMT_CORGL Reviewed; 520 AA.
AC Q8NRZ6; Q6M6Q4;
DT 06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Probable dolichyl-phosphate-mannose--protein mannosyltransferase;
DE EC=2.4.1.109;
GN Name=pmt; OrderedLocusNames=Cgl0890, cg1014;
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 DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=16734784; DOI=10.1111/j.1574-6968.2006.00269.x;
RA Mahne M., Tauch A., Puhler A., Kalinowski J.;
RT "The Corynebacterium glutamicum gene pmt encoding a glycosyltransferase
RT related to eukaryotic protein-O-mannosyltransferases is essential for
RT glycosylation of the resuscitation promoting factor (Rpf2) and other
RT secreted proteins.";
RL FEMS Microbiol. Lett. 259:226-233(2006).
CC -!- FUNCTION: Transfers mannose from Dol-P-mannose to Ser or Thr residues
CC on proteins. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl beta-D-mannosyl phosphate + L-seryl-[protein] = 3-
CC O-(alpha-D-mannosyl)-L-seryl-[protein] + a dolichyl phosphate + H(+);
CC Xref=Rhea:RHEA:17377, Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9527,
CC Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:13546, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29999, ChEBI:CHEBI:57683, ChEBI:CHEBI:58211,
CC ChEBI:CHEBI:137321; EC=2.4.1.109;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl beta-D-mannosyl phosphate + L-threonyl-[protein] =
CC 3-O-(alpha-D-mannosyl)-L-threonyl-[protein] + a dolichyl phosphate +
CC H(+); Xref=Rhea:RHEA:53396, Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9527,
CC Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:13547, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30013, ChEBI:CHEBI:57683, ChEBI:CHEBI:58211,
CC ChEBI:CHEBI:137323; EC=2.4.1.109;
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Loss of protein glycosylation.
CC {ECO:0000269|PubMed:16734784}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 39 family.
CC {ECO:0000305}.
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DR EMBL; BA000036; BAB98283.1; -; Genomic_DNA.
DR EMBL; BX927150; CAF19596.1; -; Genomic_DNA.
DR RefSeq; NP_600117.1; NC_003450.3.
DR RefSeq; WP_011013949.1; NC_006958.1.
DR AlphaFoldDB; Q8NRZ6; -.
DR SMR; Q8NRZ6; -.
DR STRING; 196627.cg1014; -.
DR CAZy; GT39; Glycosyltransferase Family 39.
DR DNASU; 1018883; -.
DR KEGG; cgb:cg1014; -.
DR KEGG; cgl:Cgl0890; -.
DR PATRIC; fig|196627.13.peg.873; -.
DR eggNOG; COG1928; Bacteria.
DR HOGENOM; CLU_021079_1_0_11; -.
DR OMA; AGNHHPW; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000000582; 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:0004169; F:dolichyl-phosphate-mannose-protein mannosyltransferase activity; IEA:UniProtKB-EC.
DR InterPro; IPR027005; GlyclTrfase_39-like.
DR InterPro; IPR003342; Glyco_trans_39/83.
DR InterPro; IPR032421; PMT_4TMC.
DR PANTHER; PTHR10050; PTHR10050; 2.
DR Pfam; PF02366; PMT; 1.
DR Pfam; PF16192; PMT_4TMC; 1.
PE 3: Inferred from homology;
KW Cell membrane; Glycosyltransferase; Membrane; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..520
FT /note="Probable dolichyl-phosphate-mannose--protein
FT mannosyltransferase"
FT /id="PRO_0000421157"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 145..165
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 274..294
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 388..408
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 418..438
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 441..461
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 485..505
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 520 AA; 58734 MW; 9F6C21ED4B20788D CRC64;
MSQALPVRDQ GRDQGIFAGT LPPAPPKFKW TRLDTYTWAI IAVFALVTRF TGLSSATASG
TPVFDEKHYV PQAWDMVRSW INPITGGIES NPGYGLVVHP PLAKQLEALG EWVFGYTPLG
WRIMVAIFGT LTIFAIMAIA RRLSGSTMVT FIAGILALAD GVLLVSSRFG MLDIFLVFFI
TAAAWALIRD HQQMHQRLND LLLTNGQITK DFGPRFGFRW WRFTTGVFLG LALSVKWSGL
YYIAFFGLTS VFLDLWLRKR YGVRRYVTGT LKNDVIPALG SLVIIPALLY IWSWRAWFAS
ETSVYRHAKT DGTITEDSIL QLFPESIAGW IHYHISVLEF HGSLTTSSGH SHPWDSKPWA
WLVSGRPILY FSSTDISCDV GGTCRRMIYL FGTPAIWWLT VPVILWALWS FFARRSRGYV
VPLVAFAAGF LPWLAAYDRQ MYFFYATALV PFTIIMLALA CGELWGRGKM TPTGLTRGSM
AVVTYISLVV MMFLAFSPLF YGFVIPDYVY ESLMWFPSWR
