ID A0A1R1SN47_9ACTN Unreviewed; 589 AA.
AC A0A1R1SN47;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Dolichyl-phosphate-mannose--protein mannosyltransferase {ECO:0000256|ARBA:ARBA00012839, ECO:0000256|RuleBase:RU367007};
DE EC=2.4.1.109 {ECO:0000256|ARBA:ARBA00012839, ECO:0000256|RuleBase:RU367007};
DE Flags: Fragment;
GN ORFNames=SPAR_09478 {ECO:0000313|EMBL:OMI39724.1};
OS Streptomyces sparsogenes DSM 40356.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1331668 {ECO:0000313|EMBL:OMI39724.1, ECO:0000313|Proteomes:UP000186168};
RN [1] {ECO:0000313|EMBL:OMI39724.1, ECO:0000313|Proteomes:UP000186168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40356 {ECO:0000313|EMBL:OMI39724.1,
RC ECO:0000313|Proteomes:UP000186168};
RA Coyne S., Seebeck F.P.;
RT "Genome sequence of Streptomyces sparsogenes DSM 40356.";
RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Transfers mannose from Dol-P-mannose to Ser or Thr residues
CC on proteins. {ECO:0000256|RuleBase:RU367007}.
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 Evidence={ECO:0000256|ARBA:ARBA00034032,
CC ECO:0000256|RuleBase:RU367007};
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 Evidence={ECO:0000256|ARBA:ARBA00033990,
CC ECO:0000256|RuleBase:RU367007};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|ARBA:ARBA00004922, ECO:0000256|RuleBase:RU367007}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU367007}.
CC Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 39 family.
CC {ECO:0000256|ARBA:ARBA00007222, ECO:0000256|RuleBase:RU367007}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OMI39724.1}.
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DR EMBL; ASQP01000140; OMI39724.1; -; Genomic_DNA.
DR RefSeq; WP_076970814.1; NZ_ASQP01000140.1.
DR AlphaFoldDB; A0A1R1SN47; -.
DR STRING; 67365.GCA_001704635_07180; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000186168; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004169; F:dolichyl-phosphate-mannose-protein mannosyltransferase activity; IEA:UniProtKB-UniRule.
DR InterPro; IPR027005; GlyclTrfase_39-like.
DR InterPro; IPR003342; Glyco_trans_39/83.
DR InterPro; IPR032421; PMT_4TMC.
DR PANTHER; PTHR10050; DOLICHYL-PHOSPHATE-MANNOSE--PROTEIN MANNOSYLTRANSFERASE; 1.
DR PANTHER; PTHR10050:SF51; PROTEIN O-MANNOSYL-TRANSFERASE 1; 1.
DR Pfam; PF02366; PMT; 1.
DR Pfam; PF16192; PMT_4TMC; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|RuleBase:RU367007};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000256|RuleBase:RU367007};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU367007};
KW Reference proteome {ECO:0000313|Proteomes:UP000186168};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU367007};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU367007};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU367007}.
FT TRANSMEM 68..87
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 164..181
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 188..209
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 215..234
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 290..307
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 328..348
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 464..482
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 489..505
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 511..533
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 545..566
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT DOMAIN 77..302
FT /note="Glycosyl transferase family 39/83"
FT /evidence="ECO:0000259|Pfam:PF02366"
FT DOMAIN 394..588
FT /note="Protein O-mannosyl-transferase C-terminal four TM"
FT /evidence="ECO:0000259|Pfam:PF16192"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OMI39724.1"
SQ SEQUENCE 589 AA; 65738 MW; 2BFD5D81A80C801D CRC64;
DTATHAQPGR AAGQHPPAWQ RRLRRFGYAG RPRSDVRERL VPPYPEPGTR LWEALGAAPP
AAARIARWTG WGGPLLVALF AGLLRFWRLD SPHKVIFDET YYAKDAWALL QLGYEGTWPK
NANAKIMADP QQIPLSDAAG YVVHPPVGKW VIAVGEQLFG LTPFGWRFMV ALLGTASVLM
LCRIGRRLFR STFLGCLAGA LLAVDGLHYV MSRTALLDIV VMFFVLAAFG CLLVDRDQAR
ARLAAALPLA PDGTARPDAE VAARLKLGAR PWRIAAGVML GLATGTKWNG LYVLAAFGVM
TVLWDIGARR TAGARRPFLS VLRRDTPWAF LSTVPVALVT YLATWWGWFA NSGSYSPRTG
WTHSGYFRHW AETPTSQGGG GYSDHGPLAW LNPLRSLWHY EHEVYKFHVG LNDPHIYQSN
PWSWIIQSRP VSYFYESPSP GEAGCPKDAT EKCAREVLAL GTPLLWWAAC FAVAYLLFRW
ALRRDWRAGA ILCGLAAGYL PWFLYQERTI FNFYAVVFVP FLCLAVAMMV GAIVGPPGAR
ENRRVVGTVA AGVLVLLIFW NFIYFFPLYT GQTLPMDQWR ARIWLDTWI
//
