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Database: UniProt
Entry: H5USI7_9MICO
LinkDB: H5USI7_9MICO
Original site: H5USI7_9MICO 
ID   H5USI7_9MICO            Unreviewed;       525 AA.
AC   H5USI7;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   24-JAN-2024, entry version 33.
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   Name=pmt {ECO:0000313|EMBL:GAB48695.1};
GN   ORFNames=MOPEL_078_00840 {ECO:0000313|EMBL:GAB48695.1};
OS   Mobilicoccus pelagius NBRC 104925.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermatophilaceae;
OC   Mobilicoccus.
OX   NCBI_TaxID=1089455 {ECO:0000313|EMBL:GAB48695.1, ECO:0000313|Proteomes:UP000004367};
RN   [1] {ECO:0000313|EMBL:GAB48695.1, ECO:0000313|Proteomes:UP000004367}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 104925 {ECO:0000313|EMBL:GAB48695.1,
RC   ECO:0000313|Proteomes:UP000004367};
RA   Yoshida Y., Hosoyama A., Tsuchikane K., Katsumata H., Yamazaki S.,
RA   Fujita N.;
RT   "Whole genome shotgun sequence of Mobilicoccus pelagius NBRC 104925.";
RL   Submitted (FEB-2012) 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:GAB48695.1}.
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DR   EMBL; BAFE01000056; GAB48695.1; -; Genomic_DNA.
DR   RefSeq; WP_009482593.1; NZ_BAFE01000056.1.
DR   AlphaFoldDB; H5USI7; -.
DR   STRING; 1089455.MOPEL_078_00840; -.
DR   eggNOG; COG4346; Bacteria.
DR   OrthoDB; 9776737at2; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000004367; 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:UP000004367};
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        121..138
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367007"
FT   TRANSMEM        144..160
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367007"
FT   TRANSMEM        172..190
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367007"
FT   TRANSMEM        247..265
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367007"
FT   TRANSMEM        286..307
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367007"
FT   TRANSMEM        400..418
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367007"
FT   TRANSMEM        425..441
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367007"
FT   TRANSMEM        447..470
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367007"
FT   TRANSMEM        482..505
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367007"
FT   DOMAIN          29..189
FT                   /note="Glycosyl transferase family 39/83"
FT                   /evidence="ECO:0000259|Pfam:PF02366"
FT   DOMAIN          334..524
FT                   /note="Protein O-mannosyl-transferase C-terminal four TM"
FT                   /evidence="ECO:0000259|Pfam:PF16192"
SQ   SEQUENCE   525 AA;  58324 MW;  7F597BE78E960F2F CRC64;
     MSETDRLRAR LLGHRPTDTL AGWLGALLVA VFGGVLRFWR LGQPNTLVFD ETYYVKQGWS
     LLTHGYEAKV RPEVADGVDR LWAAGTPDVF GTAADFVVHP PVGKWVIAAG ERLLGVQDPT
     SWRLGVAALG TLSILMLALA ARRLFGSTVL GLSAGLLLAV DGQHLVHSRT GLLDMSVMFF
     ALGGFCALLL DRDRSREILA RQVGGHLDAG GSPYAPVLRY GPWLGLHPWR WVAAVSLGLC
     IGTKWSGLYF LAVFGLMTVF WDMGARRAAG IREWWRGAML RDAPQAALTL VGGAIATYVA
     TWAGWFATSG GWNRQWAATH PATGLARLVP DPLRSLVDYH ERMWVFHVGL STPHTYQSNP
     WSWMLQTRPT SFFYEGPKAG QQGCTVTECS RAILDLGNPA IWWTATLALP VLLFMWAVAR
     DWRAGAILSG FAAGYLPWFL YQQRTIFTFY SVAFVPWVVL AVVYLLSLVL GRPDDSARRH
     RLGLLGWAAF LVLAIAVFAF FWPIYVGDVI PRDDWSMRMW FRSWI
//
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