ID A0A192D700_9SPHN Unreviewed; 444 AA.
AC A0A192D700;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Dolichyl-phosphate-mannose--protein mannosyltransferase {ECO:0000256|RuleBase:RU367007};
DE EC=2.4.1.109 {ECO:0000256|RuleBase:RU367007};
GN ORFNames=A9D12_13960 {ECO:0000313|EMBL:ANK13880.1};
OS Erythrobacter neustonensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX NCBI_TaxID=1112 {ECO:0000313|EMBL:ANK13880.1, ECO:0000313|Proteomes:UP000078263};
RN [1] {ECO:0000313|EMBL:ANK13880.1, ECO:0000313|Proteomes:UP000078263}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 9434 {ECO:0000313|EMBL:ANK13880.1,
RC ECO:0000313|Proteomes:UP000078263};
RA Shi X.-L., Wu Y.-H., Cheng H., Xu L., Zhang X.-Q., Wang C.-S., Xu X.-W.;
RT "Compelete Genome Sequence of Bacteriochlorophyll-Synthesizing Bacterium
RT Porphyrobacter neustonensis DSM 9434.";
RL Submitted (MAY-2016) 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|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|RuleBase:RU367007};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|RuleBase:RU367007}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU367007}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 39 family.
CC {ECO:0000256|RuleBase:RU367007}.
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DR EMBL; CP016033; ANK13880.1; -; Genomic_DNA.
DR RefSeq; WP_068352971.1; NZ_CP016033.1.
DR AlphaFoldDB; A0A192D700; -.
DR STRING; 1112.A9D12_13960; -.
DR KEGG; pns:A9D12_13960; -.
DR OrthoDB; 9776737at2; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000078263; Chromosome.
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; IPR032421; PMT_4TMC.
DR InterPro; IPR038731; RgtA/B/C-like.
DR PANTHER; PTHR10050; DOLICHYL-PHOSPHATE-MANNOSE--PROTEIN MANNOSYLTRANSFERASE; 1.
DR PANTHER; PTHR10050:SF51; PROTEIN O-MANNOSYL-TRANSFERASE 1; 1.
DR Pfam; PF13231; PMT_2; 1.
DR Pfam; PF16192; PMT_4TMC; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|RuleBase:RU367007};
KW Glycosyltransferase {ECO:0000256|RuleBase:RU367007};
KW Membrane {ECO:0000256|RuleBase:RU367007};
KW Reference proteome {ECO:0000313|Proteomes:UP000078263};
KW Transferase {ECO:0000256|RuleBase:RU367007};
KW Transmembrane {ECO:0000256|RuleBase:RU367007};
KW Transmembrane helix {ECO:0000256|RuleBase:RU367007}.
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 100..118
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 125..142
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 199..214
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 235..256
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 326..344
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 351..367
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 373..391
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 403..429
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT DOMAIN 76..219
FT /note="Glycosyltransferase RgtA/B/C/D-like"
FT /evidence="ECO:0000259|Pfam:PF13231"
FT DOMAIN 271..443
FT /note="Protein O-mannosyl-transferase C-terminal four TM"
FT /evidence="ECO:0000259|Pfam:PF16192"
SQ SEQUENCE 444 AA; 48845 MW; 6D0A4209D1BF7F1B CRC64;
MAHIEAPAAP AAVPALRPRD PLGWCLLLTG LFALLTGWRL AIPSQPYFDE IHYLPAAREL
LELLRTGQGT YLNREHPLLA KELIAVGMAL FGDNPLGWRI MPWLAGVIAY GAMLRAMWHA
SHDRYATLAF AVLLATGFHL FIHARIAMLD IVMASALAVA AWQFAVAIAR PEQGRLRLAL
TGIAIGCALA AKWNAIPLAV MPGLIFLAAR AFAGRRRLLL SRRGAPVPGV TLIEAFVWLG
LLPLAVYAAT FIPGYWLSEP LHPSPLAERG LIGLHQHIYE LQSQLKVPHR YMSQWPQWVL
DTRGIWYLYQ EVDGAQRGVL LIGNPLSMWL GLPALVWCLV AGLFQRSGVR LAAALGYAVS
LGLWVIAPKP VQFYYHYLVP SFFLLAALAL TCSDLRRLPK GDWLAGGVLA GAVAVFAVFF
PIIAALPLLG PDAYLEWMWL SSWK
//
