ID A0A0A0BSW8_9CELL Unreviewed; 574 AA.
AC A0A0A0BSW8;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
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 ORFNames=N868_12380 {ECO:0000313|EMBL:KGM11056.1};
OS Cellulomonas carbonis T26.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=947969 {ECO:0000313|EMBL:KGM11056.1, ECO:0000313|Proteomes:UP000029839};
RN [1] {ECO:0000313|EMBL:KGM11056.1, ECO:0000313|Proteomes:UP000029839}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T26 {ECO:0000313|EMBL:KGM11056.1,
RC ECO:0000313|Proteomes:UP000029839};
RA Chen F., Li Y., Wang G.;
RT "Genome sequencing of Cellulomonas carbonis T26.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KGM11056.1, ECO:0000313|Proteomes:UP000029839}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T26 {ECO:0000313|EMBL:KGM11056.1,
RC ECO:0000313|Proteomes:UP000029839};
RX PubMed=26587181;
RA Zhuang W., Zhang S., Xia X., Wang G.;
RT "Draft genome sequence of Cellulomonas carbonis T26(T) and comparative
RT analysis of six Cellulomonas genomes.";
RL Stand. Genomic Sci. 10:104-104(2015).
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:KGM11056.1}.
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DR EMBL; AXCY01000031; KGM11056.1; -; Genomic_DNA.
DR RefSeq; WP_052426127.1; NZ_AXCY01000031.1.
DR AlphaFoldDB; A0A0A0BSW8; -.
DR OrthoDB; 9776737at2; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000029839; 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:UP000029839};
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 163..183
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 215..233
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 280..299
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 320..340
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 434..451
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 458..475
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 481..500
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 534..554
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT DOMAIN 163..294
FT /note="Glycosyl transferase family 39/83"
FT /evidence="ECO:0000259|Pfam:PF02366"
FT DOMAIN 368..573
FT /note="Protein O-mannosyl-transferase C-terminal four TM"
FT /evidence="ECO:0000259|Pfam:PF16192"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 574 AA; 60884 MW; BC3481624718E85A CRC64;
MASTGEHTSP LDPVQEAASA GHAPQGAPAG STETAEVAPS PRHAVAGPAT TWLASLVPPH
GSAADRRLAL PLTALVGALA AALRLPGLDR PGVLVFDETY YVKDAWSLVS LGYEGEWPDG
ADAAFEAGDV DGFDERGSYV VHPPVGKLLI GAGMRLVGAG TPIGWRLATA VAGVVAVLVL
VRVGRRLLRS TWAGAAAALL LAVDGSAIAH SRTALLDGLL MTLLLGAFAA LVADRDAAAA
LLARRTGPPR APTTLGPGLG VRPWRLVAGL LLGLAVGTKW SALFFVAALG LLSVGWDALA
RRRAGVRSWW AGALVRDAPV AFASLVGLAA VVYVASWTGW LRTTGGYGRT WAGDHPGEGV
TWLPEGLRSL WKYHQDMWGF HTGLTAEHPY AAHPAGWLLQ LRPTTFFYES PEPAQQWCAA
DRCSQTVTSL GNPVLWWLAA AAVLVCAWWV VRRRDEVALA ALAGIAAGWL PWFAYAHRTI
FTFYAVVVLP WLVLCLVHVA REATRARGPA DGPLGARTAH VTHADADPPL VRRAVVVGLL
VVVLGVSAWF LPLWTGQVVP FRFWQLHMWL PGWV
//
