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
//