ID A0A3T0Y3A8_9MICC Unreviewed; 426 AA.
AC A0A3T0Y3A8;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Dolichyl-phosphate-mannose--protein mannosyltransferase {ECO:0000256|RuleBase:RU367007};
DE EC=2.4.1.109 {ECO:0000256|RuleBase:RU367007};
GN ORFNames=MN0502_09830 {ECO:0000313|EMBL:BBE22100.1};
OS Arthrobacter sp. MN05-02.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1571833 {ECO:0000313|EMBL:BBE22100.1, ECO:0000313|Proteomes:UP000283134};
RN [1] {ECO:0000313|EMBL:BBE22100.1, ECO:0000313|Proteomes:UP000283134}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MN05-02 {ECO:0000313|EMBL:BBE22100.1,
RC ECO:0000313|Proteomes:UP000283134};
RA Ii KM., Kono N., Paulino-Lima IG., Tomita M., Rothschild LJ., Arakawa K.;
RT "Complete genome sequence of Arthrobacter sp. Strain MN05-02, a UV-
RT resistant bacteria from Sonoran Desert.";
RL Submitted (MAY-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|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; AP018697; BBE22100.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3T0Y3A8; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000283134; 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 ECO:0000313|EMBL:BBE22100.1}; Membrane {ECO:0000256|RuleBase:RU367007};
KW Reference proteome {ECO:0000313|Proteomes:UP000283134};
KW Transferase {ECO:0000256|RuleBase:RU367007, ECO:0000313|EMBL:BBE22100.1};
KW Transmembrane {ECO:0000256|RuleBase:RU367007};
KW Transmembrane helix {ECO:0000256|RuleBase:RU367007}.
FT TRANSMEM 24..45
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 52..70
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 76..94
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 190..213
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 301..318
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 325..342
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 348..372
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 384..403
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT DOMAIN 3..92
FT /note="Glycosyltransferase RgtA/B/C/D-like"
FT /evidence="ECO:0000259|Pfam:PF13231"
FT DOMAIN 239..425
FT /note="Protein O-mannosyl-transferase C-terminal four TM"
FT /evidence="ECO:0000259|Pfam:PF16192"
SQ SEQUENCE 426 AA; 47041 MW; B484A2AF8BDCAD87 CRC64;
MVHPPVGKWM IAFGMLLFGS DNAFGWRFSA AAVGTLSVLL LAVVARRMFG SALLGAAAGL
LLAVDGHHLV ESRTSLLDIF LSFWLLAAFA ALLLDRDDGR RRLARRLASI AGRNDDGVPT
RAQLSWGPFL GLRPWRLIAG VCLGLALGTK WSALPYIAAF GLMTVAWDMS ARRIAGVHHW
ALGGAVKDGL LAFACLVPVA ALTYLGTWTG WFLSDDAYDR TWAERNPSEQ WGWVPDALRS
LAEYHRSAFT FHQGLGSDHP YEASAWSWLV MGRPTSFFYE KPAGCGEDAC SQAVTVLGNP
LIWWTAALSL LVLVFFWLGR RDWRAAAILT GVAAGYLPWF LYPERTTFYF YAVAFEPYLV
LGLVYCLGLV LGSPAADAAR RRRGIVLVGV FLAAAVALSA YFLPVWTAEI IPYDQWRMRM
WLPSWI
//
