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Database: UniProt
Entry: E3H5S9_ROTDC
LinkDB: E3H5S9_ROTDC
Original site: E3H5S9_ROTDC 
ID   E3H5S9_ROTDC            Unreviewed;       534 AA.
AC   E3H5S9;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   24-JAN-2024, entry version 61.
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   OrderedLocusNames=HMPREF0733_11402 {ECO:0000313|EMBL:ADP40859.1};
OS   Rothia dentocariosa (strain ATCC 17931 / CDC X599 / XDIA).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Rothia.
OX   NCBI_TaxID=762948 {ECO:0000313|EMBL:ADP40859.1, ECO:0000313|Proteomes:UP000000387};
RN   [1] {ECO:0000313|Proteomes:UP000000387}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17931 / CDC X599 / XDIA
RC   {ECO:0000313|Proteomes:UP000000387};
RA   Muzny D., Qin X., Buhay C., Dugan-Rocha S., Ding Y., Chen G., Hawes A.,
RA   Holder M., Jhangiani S., Johnson A., Khan Z., Li Z., Liu W., Liu X.,
RA   Perez L., Shen H., Wang Q., Watt J., Xi L., Xin Y., Zhou J., Deng J.,
RA   Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Villasana D., Johnson A.,
RA   Liu J., Liyanage D., Lorensuhewa L., Robinson T., Song A., Song B.-B.,
RA   Dinh H., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M.,
RA   Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N.,
RA   Okwuonu G., Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W.,
RA   Jakkamsetti A., Pham P., Ruth R., San Lucas F., Warren J., Zhang J.,
RA   Zhao Z., Zhou C., Zhu D., Lee S., Bess C., Blankenburg K., Forbes L.,
RA   Fu Q., Gubbala S., Hirani K., Jayaseelan J.C., Lara F., Munidasa M.,
RA   Palculict T., Patil S., Pu L.-L., Saada N., Tang L., Weissenberger G.,
RA   Zhu Y., Hemphill L., Shang Y., Youmans B., Ayvaz T., Ross M.,
RA   Santibanez J., Aqrawi P., Gross S., Joshi V., Fowler G., Nazareth L.,
RA   Reid J., Worley K., Petrosino J., Highlander S., Gibbs R.;
RT   "The complete genome of Rothia dentocariosa ATCC 17931.";
RL   Submitted (OCT-2010) 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}.
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DR   EMBL; CP002280; ADP40859.1; -; Genomic_DNA.
DR   AlphaFoldDB; E3H5S9; -.
DR   CAZy; GT39; Glycosyltransferase Family 39.
DR   KEGG; rdn:HMPREF0733_11402; -.
DR   eggNOG; COG1928; Bacteria.
DR   HOGENOM; CLU_021079_0_0_11; -.
DR   OMA; AGNHHPW; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000000387; 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; IPR003342; Glyco_trans_39/83.
DR   InterPro; IPR032421; PMT_4TMC.
DR   PANTHER; PTHR10050:SF53; -; 1.
DR   PANTHER; PTHR10050; DOLICHYL-PHOSPHATE-MANNOSE--PROTEIN MANNOSYLTRANSFERASE; 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   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        34..52
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367007"
FT   TRANSMEM        129..149
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367007"
FT   TRANSMEM        180..199
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367007"
FT   TRANSMEM        235..251
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367007"
FT   TRANSMEM        257..274
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367007"
FT   TRANSMEM        295..315
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367007"
FT   TRANSMEM        409..426
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367007"
FT   TRANSMEM        433..450
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367007"
FT   TRANSMEM        456..479
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367007"
FT   TRANSMEM        491..511
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367007"
FT   DOMAIN          42..200
FT                   /note="Glycosyl transferase family 39/83"
FT                   /evidence="ECO:0000259|Pfam:PF02366"
FT   DOMAIN          345..533
FT                   /note="Protein O-mannosyl-transferase C-terminal four TM"
FT                   /evidence="ECO:0000259|Pfam:PF16192"
SQ   SEQUENCE   534 AA;  60012 MW;  972D23166E542192 CRC64;
     MLTASLSFTK SRVQYSLSNL FEALGVARVS LPRWGWLAPT LIVLLAGVLR FYNLAHPNAI
     VFDETYYAKD AYSYLHYGYE VSWSSGVDHA FASGDFSGIL PNSPEYVVHP PLGKWMIAWG
     MAIFGENAFG WRVSAAIIGT LSVALLAVAG WLMFRSVTVA SIAALLGAVD GLMFVESRLA
     LLDIFQMFWI LATFVCLLLD RQAARRRLAA NVMKIVDAHG ESGLQKIVFG PGSGLHLWRL
     AAGICAGAAV AVKWNSLFFI AAMGVLTVFW DMNARRILGL KNWGIVALIR EGIPAFIQMI
     GVGLIVYLTT WIGWFKSSNA FYRHWSNQFP DSGAVKWLPE DLRLLWEYHT SAFKFHSGLS
     SEHRYASQAW QWLILGHPTS YYYEAPKFGE KGCTALNCSQ AILNIGNPLI WWVFIPAIIL
     ALVIFILKRD WRFGALLLVF AAGYLPWFLY PNRTMFFFYA LSFEPFLLIL LAGCLGVLLG
     NRTSSVRRVR VGVLCVGIYL TAVLLVSAYF WPLWTGQVIP YEQWYGHMWI PTWI
//
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