ID A0A2T0N0J4_9ACTN Unreviewed; 528 AA.
AC A0A2T0N0J4;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
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};
GN ORFNames=B0I32_10794 {ECO:0000313|EMBL:PRX65334.1};
OS Nonomuraea fuscirosea.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Nonomuraea.
OX NCBI_TaxID=1291556 {ECO:0000313|EMBL:PRX65334.1, ECO:0000313|Proteomes:UP000238312};
RN [1] {ECO:0000313|EMBL:PRX65334.1, ECO:0000313|Proteomes:UP000238312}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.7104 {ECO:0000313|EMBL:PRX65334.1,
RC ECO:0000313|Proteomes:UP000238312};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (MAR-2018) 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:PRX65334.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; PVNG01000007; PRX65334.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T0N0J4; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000238312; 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:UP000238312};
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 20..39
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 126..147
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 154..172
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 178..196
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 228..258
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 395..413
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 420..439
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 445..467
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 479..500
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT DOMAIN 29..260
FT /note="Glycosyl transferase family 39/83"
FT /evidence="ECO:0000259|Pfam:PF02366"
FT DOMAIN 330..522
FT /note="Protein O-mannosyl-transferase C-terminal four TM"
FT /evidence="ECO:0000259|Pfam:PF16192"
SQ SEQUENCE 528 AA; 57819 MW; 0F6621AA8A37AF70 CRC64;
MSNWGVSARR LVPPMQGSAL VGWLGPIAVA IFGGLLRFIR LGEPKAVVFD ETYYVKDAYS
LMLHGVERTM LGDAKNPVAD RRLIAGNLDI FQQCPQPSDC ASFVAHPPLG KWMIAAGEWL
FGMNPFGWRA VAALAGTLSI LVLARVARRM TRSTLLGCLG GLLLALDGLH LVLSRTALLD
VFLMFWVLAG FACLVADRDQ ARAKLVSWYE RSPVTALGPR LGPRPWRLAA GICLGAACAV
KWSGIFFLLA FAVMSVLWDM GARRAVGLRE PYRGALTYDL PGAAGAMALA PAVTFMASWT
GWFVTAGGYG RNWDQATSSG PLFFVVDSVR SWLRYQQQVL GYHSGLEDYH PYMSEPWQWP
VLLRPVSFHY PTNLPPSACG ADKCAQAVLG VGTPALWYAA ALALVGLVAW YVATRDWRAG
AVLLAYGVGW LPWFYYAIAD NRTMYLFYMI PVVPFMVLAL VLMAGLIMGP RDAPAARRAI
GAAVVGAYAL IVLVNFWWLY PVLAAETITQ AQWWSRMLLS SWVTAAPK
//
