ID A0A1B8W9P5_9BACI Unreviewed; 1268 AA.
AC A0A1B8W9P5;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=dolichyl-phosphate-mannose--protein mannosyltransferase {ECO:0000256|ARBA:ARBA00012839};
DE EC=2.4.1.109 {ECO:0000256|ARBA:ARBA00012839};
GN ORFNames=A7975_10900 {ECO:0000313|EMBL:OBZ13355.1};
OS Bacillus sp. FJAT-26390.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1743142 {ECO:0000313|EMBL:OBZ13355.1, ECO:0000313|Proteomes:UP000092623};
RN [1] {ECO:0000313|EMBL:OBZ13355.1, ECO:0000313|Proteomes:UP000092623}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FJAT-26390 {ECO:0000313|EMBL:OBZ13355.1,
RC ECO:0000313|Proteomes:UP000092623};
RA Liu X., Pan Z., Shi H., Ge C., Che J., Lan J., Chen Z., Chen Q., Liu B.,
RA Zhu Y., Wang J., Liu G.;
RT "Bacillus sp. FJAT-26390.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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 -!- 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 -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|ARBA:ARBA00004922}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 39 family.
CC {ECO:0000256|ARBA:ARBA00007222}.
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:OBZ13355.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MAQX01000011; OBZ13355.1; -; Genomic_DNA.
DR RefSeq; WP_065385520.1; NZ_MAQX01000011.1.
DR AlphaFoldDB; A0A1B8W9P5; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000092623; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004169; F:dolichyl-phosphate-mannose-protein mannosyltransferase activity; IEA:UniProtKB-EC.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR008979; Galactose-bd-like_sf.
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.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS50022; FA58C_3; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000092623};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:OBZ13355.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..1268
FT /note="dolichyl-phosphate-mannose--protein
FT mannosyltransferase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008618302"
FT TRANSMEM 207..228
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 248..266
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 305..324
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 331..349
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 355..375
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 387..404
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 410..434
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 446..470
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 505..528
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 540..557
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 563..579
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 584..602
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 614..636
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 686..704
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 894..915
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 922..938
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 944..961
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 973..991
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 997..1015
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1052..1074
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1149..1166
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1173..1190
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1196..1217
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1229..1246
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 712..808
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
SQ SEQUENCE 1268 AA; 142848 MW; F6AF6CD4808D933E CRC64;
MFKLSFRSMA IVLLLALLWP AVMGHAATNL LKNASFENVT AGAPADWNHD AYLKEDNVTA
YSVSSDESHT GTYSAVLENK GANHSRWTQV VNVKPKTTYK LSGYVKTEQI GPDATGAHFF
VDGVAVTYPE VKDTNGKWAY VHFYAKTGKD QKSITFAASL GGYGAINTGK AYFDDVSVEK
VSKAPSGAEV FSLVPTETGQ GADATGAGVS VLPLILFGAL FCLLFAAVYK KLFRDRGWLD
EKPHLHKVIL VFVLLGALAL RFWIAIASKG YANDIALFMA WADHAVKQGL SGFYHTDMFV
DYPPGYIYIL YVLGAVKSML ALDASSNAAM LLFKLPAILA DLAAAYFIFK AANKKAGYSV
ALGLSLLYVF NPAIIVDSAA WGQVDSIFAL ALVLSIYGIA ENKIERASVW FAIAALIKPQ
AFIFMPVLLV WFVYRKAWRK IPVSAFYGFT TFILLALPFF WGNGGLAGLI NLYRGTLSSY
PYATLNAFNF YTLTNDNWKP ITDTWLLFSF QTWGMIFILA AVALAAYFSF KKLDGDSSKR
AFYVGMVLIV VVFMGVTKMH ERYLFPVLLL AVFAFIQSLD RRMLMLYLGF SLTSFINITY
VLDYSKVSTN VPFNGIVLLC SLANIGLLLY LLYIGYDKYV RGKVKPVSPL LEEELQQSDE
NVLAPFKAGA VSRLNQENNR LERKDWIWMG AVTLIYAIVA LYQLGEMKGP VTVWQPAEAN
QSFIVDLGGV KQLDRINSFG GVGTGKFKYE FSQNGTDWDN VMEMDSSHVA VFTWTSQPAA
LQARYVKLTT VQSGFSMHEI AIYEQSNKIP LPIVGINDEQ AKNAKRGSVP QLFDEQSLAK
YDATYMNGSY FDEIYHARTA YEHLEHIVAY ENTHPPLGKI IIALGIKLFG LNPFGWRVMG
TLFGIAMLPL MYLFARRLFK SRLYAGLAAA LFAADFMHFT QTRIATIDVY GVFFIMLMFY
FMHKYYSLNF YRVKLSVTLL PLFLAGLFFG IGVASKWIVL YGGAGLAIML AISLFERYKE
YAAAKRVLRN DKAESAFSLD KLQHIVNVFP RYTIITLAVC LVFYIVIPLS IYALSYIPVL
TVMDEGYTLK SLIDYQKHMF SYHSHLVSTH PFSSSWWEWP FMKRPVWYYS GDNMAPGMKS
TIVAMGNPLI WWAGIFAMAA TIWLSIKRRD RAMYTVWIAF LAQYVPWMLV TRLTFLYHYF
AMVPFIILSL VYIFKVIEEK EPSFKRVRNI FLVVSILLFI VYYPALSGMT VPTWYVEHVL
RWFPSWLF
//
