ID A0A2Z2KRT9_9BACL Unreviewed; 1268 AA.
AC A0A2Z2KRT9;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, 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=B9T62_35460 {ECO:0000313|EMBL:ASA25569.1};
OS Paenibacillus donghaensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=414771 {ECO:0000313|EMBL:ASA25569.1, ECO:0000313|Proteomes:UP000249890};
RN [1] {ECO:0000313|EMBL:ASA25569.1, ECO:0000313|Proteomes:UP000249890}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 13049 {ECO:0000313|EMBL:ASA25569.1,
RC ECO:0000313|Proteomes:UP000249890};
RA Jung B.K., Hong S.-J., Shin J.-H.;
RT "Complete genome sequence of Paenibacillus donghaensis KCTC 13049T isolated
RT from East Sea sediment, South Korea.";
RL Submitted (JUN-2017) 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}.
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DR EMBL; CP021780; ASA25569.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Z2KRT9; -.
DR KEGG; pdh:B9T62_35460; -.
DR OrthoDB; 9776737at2; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000249890; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000030; F:mannosyltransferase activity; IEA:InterPro.
DR GO; GO:0006493; P:protein O-linked glycosylation; IEA:InterPro.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
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.
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:UP000249890};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ASA25569.1};
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..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..1268
FT /note="dolichyl-phosphate-mannose--protein
FT mannosyltransferase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016343735"
FT TRANSMEM 216..235
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 247..268
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 307..325
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 337..354
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 386..402
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 408..431
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 443..463
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 512..532
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 539..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..604
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 616..637
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 684..703
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 893..914
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 921..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..990
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 996..1014
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1052..1073
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..1256
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 845..1078
FT /note="Glycosyl transferase family 39/83"
FT /evidence="ECO:0000259|Pfam:PF02366"
FT DOMAIN 1088..1266
FT /note="Protein O-mannosyl-transferase C-terminal four TM"
FT /evidence="ECO:0000259|Pfam:PF16192"
SQ SEQUENCE 1268 AA; 141400 MW; 4C33A4772C6EE5D5 CRC64;
MIKKMRAAAI IIMLLLIFML PVTSIHAEDN LLQNPGFENE ENGVPSGWIE DRWVAGDGSG
LISLQGDDVR SGGKAAVIEN IEPNHLKWVQ NLTVSPDSYY KISGWTKVIS ITGEGMGANL
FVVGVGGGYP STKDTAGDWQ YLEFIGQTGP EQTEIGVGAA LGGYASLIQG KAYFDDLSVE
KLEAAPEGAA VVSLVSGTTV QEGAAETPHK VSPTRLLLIS ALFSIFFAIL YHKAFRSDRL
LKQPEMIYTR WMVVVFGAAL ILRVWIGLTA QGYQNDMNTF IAWGQRLVDL GPGKFYEEGY
FADYPPGYLY ILYMLGLVRG VFGFAQGSGG ESLLFKLPAI LSDLVLGYLI YQFGRKKLGQ
GIAFGLMLLF LFNPAVLINS SAWGQADSFF LIFLLLAIKG AADKTLVRAA IFFALATLIK
PQALIFTPVL LFAFYHQRAW KQLAVGALYG LGIFGVLAAP FFWNNGGFAG VINLYKATLS
SYPYSTVNAF NLYALTDPMW AALDNTWLGI TYRVWGFVFI LVAVATSVFY SFKRDRQNLA
KSYFIGMVLI VIVFVLGTKM HERYMYPALL LALFAYIESR DRRFLTLFLG FSLTQFINVG
YTLAFLNIQS NPPNDGIVLL TAITNLLLLC YMLYIGYDLY IRGRHKLLPQ PLTGQEKYSR
DLQTAEELRP LAEETKLKLQ RKDWIAMLAI TAVYAAIALF NLGSDKAPET LWEPAAGGES
FYVDLGQSRQ LERVNVFGGT GTGKFKLEFS QSPDAWSSPL TVNEEVGNVF VWKSQPLNVA
ARYVKLTVDS PGFTLNEMAF YEQGGGRTPL PVAAVTPDAA AAPKRGEPAN LFDEQTLIPE
YSGFTNGTYF DEIYHARTAY EYTHGIVPYE NTHPPLGKLL IAVGMELFGV NPFGWRIIGT
LFGIAMLPLI YLMAQRLFRS TTYAALATGL FALDFMHFTQ TRISTIDVYG VFFIMLMFYF
MQRYTTRSFY RQPLAKTLLP LFLSGLFFGI GVASKWIVAY GGVGLAIMLA LSLFQRYKES
QAAGRVLAEG KLKDGELTAA CRVAARSFWK NTIITLASCV VFFVIIPALI YSLSFWPALS
ASSEGFTFKG LIDAQKNMYN YHSQLVATHP FASSWWEWPF MKRPVWFYSG GEGLPAGKVS
SIVTMGNPLI WWTGIFAMLG TLWLTLKRKD KNLYMIWIAF FSQYVPWMLV PRETFLYHYF
AMVPFMILGI VYVMQLLEGK YAKAKTLRYV YVAVAALLFV AFYPVLSGMV VSGSYVTTLL
RWFPSWVF
//
