ID   Q9CD61_MYCLE            Unreviewed;       510 AA.
AC   Q9CD61;
DT   01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2001, sequence version 1.
DT   04-NOV-2026, entry version 105.
DE   RecName: Full=Polyprenol-phosphate-mannose--protein mannosyltransferase {ECO:0000256|ARBA:ARBA00093617, ECO:0000256|RuleBase:RU367007};
DE            EC=2.4.1.- {ECO:0000256|RuleBase:RU367007};
GN   OrderedLocusNames=ML0192 {ECO:0000313|EMBL:CAC29700.1};
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Mycobacteriaceae; Mycobacterium.
OX   NCBI_TaxID=272631 {ECO:0000313|EMBL:CAC29700.1, ECO:0000313|Proteomes:UP000000806};
RN   [1] {ECO:0000313|EMBL:CAC29700.1, ECO:0000313|Proteomes:UP000000806}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN {ECO:0000313|EMBL:CAC29700.1,
RC   ECO:0000313|Proteomes:UP000000806};
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
CC   -!- FUNCTION: Protein O-mannosyltransferase that catalyzes the transfer of
CC       a single mannose residue from a polyprenol phospho-mannosyl lipidic
CC       donor to the hydroxyl group of selected serine and threonine residues
CC       in acceptor proteins. {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}.
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DR   EMBL; AL583917; CAC29700.1; -; Genomic_DNA.
DR   PIR; H86932; H86932.
DR   AlphaFoldDB; Q9CD61; -.
DR   STRING; 272631.gene:17574008; -.
DR   KEGG; mle:ML0192; -.
DR   PATRIC; fig|272631.5.peg.305; -.
DR   Leproma; ML0192; -.
DR   eggNOG; COG4346; Bacteria.
DR   HOGENOM; CLU_021079_1_0_11; -.
DR   OrthoDB; 9776737at2; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000000806; Chromosome.
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; IPR003342; ArnT-like_N.
DR   InterPro; IPR027005; PMT-like.
DR   InterPro; IPR032421; PMT_4TMC.
DR   PANTHER; PTHR10050; DOLICHYL-PHOSPHATE-MANNOSE--PROTEIN MANNOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR10050:SF46; PROTEIN O-MANNOSYL-TRANSFERASE 2; 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:UP000000806};
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        100..121
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367007"
FT   TRANSMEM        128..146
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367007"
FT   TRANSMEM        152..170
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367007"
FT   TRANSMEM        197..215
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367007"
FT   TRANSMEM        259..280
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367007"
FT   TRANSMEM        375..392
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367007"
FT   TRANSMEM        399..415
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367007"
FT   TRANSMEM        421..446
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367007"
FT   TRANSMEM        467..487
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367007"
FT   DOMAIN          81..230
FT                   /note="ArnT-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02366"
FT   DOMAIN          307..509
FT                   /note="Protein O-mannosyl-transferase C-terminal four TM"
FT                   /evidence="ECO:0000259|Pfam:PF16192"
SQ   SEQUENCE   510 AA;  57115 MW;  9094A9AB84B9F099 CRC64;
     MISPGPLVPV EDFGPTDDVR GWIATGVITV LATGTRFINL SSPTDAGTPI FDEKHYAPQA
     WQLLHNHGVE DNPGFGLVVH PPIGKQLIAI GEAIFGYNGV GWRFTGALLG VIMVALVMRI
     VRRITRSTLI GTIAGLLVIC DGVSFVTART ALLDGFLTFF VVATFGALIV DRDQVRQRMH
     TAITEGRSTE TVWGPRLGVR WWRFLGGILL GLACATKWSG LYFVLFFGVM SLAFDVSSRR
     QYQVLNPWRG VLRRDVIPTV YALGLISFLV YITSYAPWFA SETAIDRHQV GQTIGRHGMI
     PLPDAVRSLW YYHAKTLQFH AGLTNSAGNY HPWESKPWSW PMSLRPVLYA IDQQDVPGCG
     AQSCVKAEML VGTPAMWWLA VPVLVYATWR TVIQRDWRYA AVLVGYCAGW LPWFADIDRQ
     MYLFYAATMA PFLVMGIALI LGDILYPPWH DSSPRSPSTH STERRTLRLI AVSCYVALVI
     TNFVWLYPVL TGLPISHQTW NMEIWLPSWR
//