ID C8X6U6_NAKMY Unreviewed; 559 AA.
AC C8X6U6;
DT 03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 03-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 68.
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=Namu_4565 {ECO:0000313|EMBL:ACV80844.1};
OS Nakamurella multipartita (strain ATCC 700099 / DSM 44233 / CIP 104796 / JCM
OS 9543 / NBRC 105858 / Y-104) (Microsphaera multipartita).
OC Bacteria; Actinomycetota; Actinomycetes; Nakamurellales; Nakamurellaceae;
OC Nakamurella.
OX NCBI_TaxID=479431 {ECO:0000313|EMBL:ACV80844.1, ECO:0000313|Proteomes:UP000002218};
RN [1] {ECO:0000313|Proteomes:UP000002218}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700099 / DSM 44233 / CIP 104796 / JCM 9543 / NBRC 105858 /
RC Y-104 {ECO:0000313|Proteomes:UP000002218};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA Ovchinnikova G., Sims D., Meincke L., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Nakamurella multipartita DSM 44233.";
RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACV80844.1, ECO:0000313|Proteomes:UP000002218}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700099 / DSM 44233 / CIP 104796 / JCM 9543 / NBRC 105858 /
RC Y-104 {ECO:0000313|Proteomes:UP000002218};
RX PubMed=21304699;
RA Tice H., Mayilraj S., Sims D., Lapidus A., Nolan M., Lucas S.,
RA Glavina Del Rio T., Copeland A., Cheng J.F., Meincke L., Bruce D.,
RA Goodwin L., Pitluck S., Ivanova N., Mavromatis K., Ovchinnikova G.,
RA Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Detter J.C., Brettin T., Rohde M., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA Chen F.;
RT "Complete genome sequence of Nakamurella multipartita type strain (Y-
RT 104).";
RL Stand. Genomic Sci. 2:168-175(2010).
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; CP001737; ACV80844.1; -; Genomic_DNA.
DR RefSeq; WP_015749659.1; NC_013235.1.
DR AlphaFoldDB; C8X6U6; -.
DR STRING; 479431.Namu_4565; -.
DR CAZy; GT39; Glycosyltransferase Family 39.
DR KEGG; nml:Namu_4565; -.
DR eggNOG; COG1928; Bacteria.
DR HOGENOM; CLU_021079_1_0_11; -.
DR InParanoid; C8X6U6; -.
DR OrthoDB; 9776737at2; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000002218; 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; 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:UP000002218};
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 151..170
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 177..195
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 201..219
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 264..284
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 305..327
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 427..448
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 455..474
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 480..503
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 515..536
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT DOMAIN 149..321
FT /note="Glycosyl transferase family 39/83"
FT /evidence="ECO:0000259|Pfam:PF02366"
FT DOMAIN 364..558
FT /note="Protein O-mannosyl-transferase C-terminal four TM"
FT /evidence="ECO:0000259|Pfam:PF16192"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 559 AA; 61442 MW; 85504689B9EBFEF0 CRC64;
MSAPPSLADP ATEDDIAAAR SAGATAPDTE PERPDPAGTV VAIGEVPALT RPVRPARTLR
PAPPTDRARG WVVTGVVTLI AAMVRLVNLG SATDGGTPLF DEKYYAIQAW EMLRNGGVED
NQAFGVVVHP PLGKQLIAIG EWLLGYNATG WRLASAVAGI VSVLLIVRVT RRMTGSTLLG
GIAGVLLICD GVSHVQSRSA LLDIFQAVFV LGAFACLIAD RDQVRARLAL AVADGSLTGT
KAGPPMGARW WRFGAGVLLG LTTAVKWSGA YWILAFVALS LIWDMQARRE AGVRRPVRAG
LRRDLLPSIW SLAVVPVLVY VGSWWAWFAS ETSWPRHTLV AEPSNRSDWK SGFLYDVASA
WSNSLWQWTW KMLDFHAHLL TPTDPSKRHP WESKPWTWPL GTRPVLYYSP ADAPCPADPA
TECVRRIFLI GTPALWWISL FVLIWALWKA IGRLDWRYAA VLVAYGAGYL PWFTNLDRQM
YFFYATPLAP FLVIGITLVL GDILGRRGAG IERRLTSIAV VAMYVGLVVA NFIWLWPILN
GEPITHERLI METWLPSWG
//
