ID   B2GLL7_KOCRD            Unreviewed;       566 AA.
AC   B2GLL7;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   02-SEP-2026, entry version 83.
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   Name=pmt {ECO:0000313|EMBL:BAG30091.1};
GN   OrderedLocusNames=KRH_17440 {ECO:0000313|EMBL:BAG30091.1};
OS   Kocuria rhizophila (strain ATCC 9341 / DSM 348 / NBRC 103217 / DC2201).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
OC   Micrococcaceae; Kocuria.
OX   NCBI_TaxID=378753 {ECO:0000313|EMBL:BAG30091.1, ECO:0000313|Proteomes:UP000008838};
RN   [1] {ECO:0000313|EMBL:BAG30091.1, ECO:0000313|Proteomes:UP000008838}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9341 / DSM 348 / NBRC 103217 / DC2201
RC   {ECO:0000313|Proteomes:UP000008838};
RX   PubMed=18408034; DOI=10.1128/JB.01853-07;
RA   Takarada H., Sekine M., Kosugi H., Matsuo Y., Fujisawa T., Omata S.,
RA   Kishi E., Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Complete genome sequence of the soil actinomycete Kocuria rhizophila.";
RL   J. Bacteriol. 190:4139-4146(2008).
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; AP009152; BAG30091.1; -; Genomic_DNA.
DR   AlphaFoldDB; B2GLL7; -.
DR   STRING; 378753.KRH_17440; -.
DR   KEGG; krh:KRH_17440; -.
DR   eggNOG; COG1928; Bacteria.
DR   HOGENOM; CLU_021079_0_0_11; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000008838; 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:UP000008838};
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        60..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367007"
FT   TRANSMEM        155..176
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367007"
FT   TRANSMEM        183..201
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367007"
FT   TRANSMEM        207..225
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367007"
FT   TRANSMEM        270..287
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367007"
FT   TRANSMEM        308..328
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367007"
FT   TRANSMEM        422..439
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367007"
FT   TRANSMEM        446..463
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367007"
FT   TRANSMEM        469..491
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367007"
FT   TRANSMEM        524..546
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367007"
FT   DOMAIN          135..297
FT                   /note="ArnT-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02366"
FT   DOMAIN          355..565
FT                   /note="Protein O-mannosyl-transferase C-terminal four TM"
FT                   /evidence="ECO:0000259|Pfam:PF16192"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..12
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   566 AA;  62045 MW;  53404906C7C336A4 CRC64;
     MAGGAVAAGR GATPDPPGLG PYHGSVPSTV FSPAALRHPD GSPASPRELL LPAVTRLPRW
     WWVPLVLVTV LGGVLRFVGL ASPHAVVFDE TYYLKDAYSL LLHGTEQQWP SGADEGFVSG
     AVPDVQDQPS FVVHPPLGKW LIAVGLWLFG PEDPFGWRFS AAVVGTLSIA LIWWAGWLLF
     RSVSLATIAG LLTALDGLHL VESRLALLDI FLMFFLLLAF VLALLDRDDG RRRLAARLGG
     SPLGPWLGVR WWRIAAGAAC GAAAAVKWNA LFSIAALGIL VVLWDMNARR VAGVRHWFTG
     AVLKDGPWGF LTVIGTGLVT YVLMWSGWLA TSGGYDRTWA QLNPGQGPPW LPPALRSLWE
     YHVAAYSFHT GLDFHHTYMA GPATWPFMLR PTSYYYESPG AGTDGCTVDA CSQAILNVGN
     PAVWWVGILA VLLGVWLWAG RRDWRFGALV GVCAAGYLPW FLYPDRTMFF FYALSYFPAV
     ALLIAGAVGV LTGRLAVPRH GATAGTPVAA AHEHRITGVW AQRWRAVTVC YLLLAVALAV
     FFWPVWTAQT IPYEHWRWRM WFRSWI
//