ID A0A1E7MYZ5_KITAU Unreviewed; 592 AA.
AC A0A1E7MYZ5;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 38.
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=HS99_0038535 {ECO:0000313|EMBL:OEV33656.1};
OS Kitasatospora aureofaciens (Streptomyces aureofaciens).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Kitasatospora.
OX NCBI_TaxID=1894 {ECO:0000313|EMBL:OEV33656.1, ECO:0000313|Proteomes:UP000037395};
RN [1] {ECO:0000313|EMBL:OEV33656.1, ECO:0000313|Proteomes:UP000037395}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10762 / DSM 40127 / CCM 3239 / JCM 4008 / LMG 5968 / NBRC
RC 12843 / NCIMB 8234 / A-377 {ECO:0000313|Proteomes:UP000037395};
RA Zhang J.E., Yang H., Guo J., Deng Z., Luo H., Luo M., Zhao B.;
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000037395}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10762 / DSM 40127 / CCM 3239 / JCM 4008 / LMG 5968 / NBRC
RC 12843 / NCIMB 8234 / A-377 {ECO:0000313|Proteomes:UP000037395};
RA Gradnigo J.S., Johnson N., Somerville G.A.;
RT "Sequencing, assembly and comparative genomics of S. aureofaciens ATCC
RT 10762.";
RL Submitted (AUG-2016) 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:OEV33656.1}.
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DR EMBL; JPRF03000063; OEV33656.1; -; Genomic_DNA.
DR RefSeq; WP_030286430.1; NZ_LBHA01000395.1.
DR AlphaFoldDB; A0A1E7MYZ5; -.
DR GeneID; 33981424; -.
DR OrthoDB; 9776737at2; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000037395; 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:UP000037395};
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 88..111
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 191..212
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 219..237
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 243..261
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 347..369
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 467..484
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 491..508
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 514..536
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 548..569
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT DOMAIN 104..323
FT /note="Glycosyl transferase family 39/83"
FT /evidence="ECO:0000259|Pfam:PF02366"
FT DOMAIN 401..591
FT /note="Protein O-mannosyl-transferase C-terminal four TM"
FT /evidence="ECO:0000259|Pfam:PF16192"
SQ SEQUENCE 592 AA; 65539 MW; 8C8CC2E5D5CB1571 CRC64;
MNGDTAAQAP TGTDHSAQGG AGLPSPRSPG SPLSWRERLA RHGYRARPTG TLTERLVPPM
PDGPGVTEPG VPQSPVLLRL GITLPQGLWY FLCRWSGWLG PIAVAVFAGL LRFTNLGQPH
AIIFDETYYA KDAYALWQGG YEINWPEDAN TTIMTPGAAV PYRSTASYVV HPPVGKWIIG
AGEQLFGMNP FGWRFAVALL GTLSVLMLAR IARRMFRSTL LGCVAGLLLS VDGLHLVLSR
TALLDLVVMF WMLAAFGFLL LDRDHTRGRL AARLGGVADP ARAQRLNLGW RPYRIAAGVC
VGLTCATKWS GLYVAAAFGV LTVLWDVGAR RLAGAPRPYL AVLARDVVPA FVSVVVVSVT
VYLASWWGWF ASSNAPGRGG WGRDWAVGRS TDYPWIPEGL RALWHYHSTV YEFHTHLTDP
HTYQSNPWSW LVLGRPVSFY YESPKFGQDG CTVSDCAREV LGIGTPLLWW TAVLALVYCL
WRWAFRRDWR AGALLCGLAA GYLPWFLYQQ RTIFLFYAVV FVPFLVLAVT MLIGALIGPA
GASRDRRIIG SATAGLLVLL IMWNFLYFFP LFTGQTIPLE DWRARMWFNS WI
//
