PMT_MYCSE
ID PMT_MYCSE Reviewed; 516 AA.
AC L8F4Z2; A0A2U9PX03;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2013, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Probable dolichyl-phosphate-mannose--protein mannosyltransferase {ECO:0000305};
DE EC=2.4.1.109 {ECO:0000250|UniProtKB:P9WN05};
GN Name=pmt;
GN ORFNames=5447 {ECO:0000303|PubMed:18554329},
GN D806_053290 {ECO:0000312|EMBL:AWT56277.1}, D806_5507;
OS Mycolicibacterium smegmatis (strain MKD8) (Mycobacterium smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=1214915;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MKD8;
RX PubMed=23618714; DOI=10.1128/genomea.00148-13;
RA Gray T.A., Palumbo M.J., Derbyshire K.M.;
RT "Draft genome sequence of MKD8, a conjugal recipient Mycobacterium
RT smegmatis strain.";
RL Genome Announc. 1:E0014813-E0014813(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MKD8;
RA Derbyshire K., Gray T.A., Champion M.;
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=MKD8;
RX PubMed=18554329; DOI=10.1111/j.1365-2958.2008.06299.x;
RA Coros A., Callahan B., Battaglioli E., Derbyshire K.M.;
RT "The specialized secretory apparatus ESX-1 is essential for DNA transfer in
RT Mycobacterium smegmatis.";
RL Mol. Microbiol. 69:794-808(2008).
CC -!- FUNCTION: Transfers mannose from Dol-P-mannose to Ser or Thr residues
CC on proteins (By similarity). Involved in DNA conjugation, in at least
CC the recipient strain (PubMed:18554329). {ECO:0000250|UniProtKB:P9WN05,
CC ECO:0000269|PubMed:18554329}.
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:0000250|UniProtKB:P9WN05};
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:0000250|UniProtKB:P9WN05};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Loss of DNA conjugation when disrupted in
CC recipient strain, strain does not secrete EsxB (PubMed:18554329).
CC {ECO:0000269|PubMed:18554329}.
CC -!- MISCELLANEOUS: DNA conjugation in M.smegmatis is unidirectional with
CC distinct donor and recipient strains; mc(2)155 is a donor strain while
CC MKD8 is a recipient strain. Mutations in a donor strain that alter DNA
CC transfer do not always alter DNA transfer in a recipient strain.
CC {ECO:0000305|PubMed:18554329}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 39 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AWT56277.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP027541; AWT56277.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_003896844.1; NZ_CP027541.1.
DR AlphaFoldDB; L8F4Z2; -.
DR SMR; L8F4Z2; -.
DR EnsemblBacteria; AWT56277; AWT56277; D806_053290.
DR PATRIC; fig|1214915.3.peg.5534; -.
DR HOGENOM; CLU_021079_1_0_11; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000011200; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004169; F:dolichyl-phosphate-mannose-protein mannosyltransferase activity; IEA:UniProtKB-EC.
DR InterPro; IPR027005; GlyclTrfase_39-like.
DR InterPro; IPR003342; Glyco_trans_39/83.
DR InterPro; IPR032421; PMT_4TMC.
DR PANTHER; PTHR10050; PTHR10050; 2.
DR Pfam; PF02366; PMT; 1.
DR Pfam; PF16192; PMT_4TMC; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Glycosyltransferase; Membrane;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..516
FT /note="Probable dolichyl-phosphate-mannose--protein
FT mannosyltransferase"
FT /id="PRO_0000438349"
FT TRANSMEM 113..133
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 166..186
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 234..254
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 275..295
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 384..404
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 413..433
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 437..457
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 473..493
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 516 AA; 57566 MW; E8A7B0E29E965C90 CRC64;
MTALDTDTPT AGRSAPLISP GPVIPPPDFG PLDRAQGWAM TAIITALAAI TRFLNLGSPT
DAGTPIFDEK HYAPQAWQVL HNDGVEDNPG YGLVVHPPVG KQLIAIGEWL FGYNGLGWRF
SGAVCGVIIV MLVTRIARRI SRSTLVGAIA GLLIIADGVS FVSSRTALLD VFLVMFAVAA
FACLMVDRDQ VRERMYHAFL DGRIAETRWG PRLGVRWWRF GAGVLLGLAC ATKWSGLYFV
LFFGVMTLVF DAIARKQYHV PHPWRGMLRR DLGPAAYVFG LIPFAVYLAS YAPWFASETA
VNRYEVGRSI GPDSILPIPD ALRSLWHYTH AAYRFHSNLT NADGNHHPWE SKPWTWPMSL
RPVLYAIDNQ DVPGCGAQSC VKAVMLVGTP AMWFIAVPVL GWALWRTVVR RDWRYGAVLV
GYMAGFLPWF ADIDRQMYFF YATVMAPFLV LAIALILGDI LYKPNQNPER RTLGLLTVCF
YVALVITNFA WMYPILTGLP ISQTTWNLQI WLPSWR
