ID   C3PF34_CORA7            Unreviewed;       537 AA.
AC   C3PF34;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   02-SEP-2026, entry version 81.
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=cauri_0841 {ECO:0000313|EMBL:ACP32438.1};
OS   Corynebacterium aurimucosum (strain ATCC 700975 / DSM 44827 / CIP 107346 /
OS   CN-1) (Corynebacterium nigricans).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=548476 {ECO:0000313|EMBL:ACP32438.1, ECO:0000313|Proteomes:UP000002077};
RN   [1] {ECO:0000313|EMBL:ACP32438.1, ECO:0000313|Proteomes:UP000002077}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700975 / DSM 44827 / CIP 107346 / CN-1
RC   {ECO:0000313|Proteomes:UP000002077};
RX   PubMed=20137072; DOI=10.1186/1471-2164-11-91;
RA   Trost E., Gotker S., Schneider J., Schneiker-Bekel S., Szczepanowski R.,
RA   Tilker A., Viehoever P., Arnold W., Bekel T., Blom J., Gartemann K.H.,
RA   Linke B., Goesmann A., Puhler A., Shukla S.K., Tauch A.;
RT   "Complete genome sequence and lifestyle of black-pigmented Corynebacterium
RT   aurimucosum ATCC 700975 (formerly C. nigricans CN-1) isolated from a
RT   vaginal swab of a woman with spontaneous abortion.";
RL   BMC Genomics 11:91-91(2010).
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; CP001601; ACP32438.1; -; Genomic_DNA.
DR   AlphaFoldDB; C3PF34; -.
DR   STRING; 548476.cauri_0841; -.
DR   KEGG; car:cauri_0841; -.
DR   eggNOG; COG4346; Bacteria.
DR   HOGENOM; CLU_021079_1_0_11; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000002077; 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:UP000002077};
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        44..65
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367007"
FT   TRANSMEM        127..148
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367007"
FT   TRANSMEM        155..173
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367007"
FT   TRANSMEM        179..196
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367007"
FT   TRANSMEM        285..305
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367007"
FT   TRANSMEM        403..420
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367007"
FT   TRANSMEM        427..444
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367007"
FT   TRANSMEM        450..473
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367007"
FT   TRANSMEM        494..521
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367007"
FT   DOMAIN          128..298
FT                   /note="ArnT-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02366"
FT   DOMAIN          336..536
FT                   /note="Protein O-mannosyl-transferase C-terminal four TM"
FT                   /evidence="ECO:0000259|Pfam:PF16192"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   537 AA;  59907 MW;  0E4E9FFED8A692CA CRC64;
     MSIATPTDRS GRRKRTRLSA ARGAHTRPAP PAPRPYTWTR ADTISTAIIG VLAFLTRFIG
     LTAPVSEGTP VFDEKHYVPQ AWDMVTSWHN LFLGGIESNP GYGLVVHPPL AKQIIAISEA
     LFGYTPLGWR AMAALFGVGT VMLTMALARR LSGSWQVGFL AGLLAVCDGV LLVASKFGML
     DIFQVFFVVA AAWALARDHQ QMRERLQAAF VSGTMGDSDF GPRFGFRWWR FTAGVFLGLT
     LSVKWSGLYY IMFFGLMSVF SDLALRRLYG VRRYIVGTLV RDTPAALASI VAVPVALYTW
     SWRAWFADET AVYRHAKVDG TIEEGSWLLH LPEPLAGWFY YHSSVLEFHA SLTTSGGHSH
     PWDSKPWAWL VAARPILYYS ATDISCGDGG SCRKMLYLFG TPAIWWLVIP AVLWGLWSLL
     VRRNRAFLIP LVGAAAGFLP WLAVFDRQMY FFYATAFIPF VIVLISLTLG QMIGRGRVLQ
     WRWLTGLFGS AMPLGTFLTV CYAALVVAMF AYFSPILYGY LIPDSWNSSM MWLPSWS
//