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O05586 (PMT_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Probable dolichyl-phosphate-mannose--protein mannosyltransferase
EC=2.4.1.109
Gene names
Name:pmt
Ordered Locus Names:Rv1002c, MT1031
ORF Names:MTCI237.17c
OrganismMycobacterium tuberculosis [Reference proteome] [HAMAP]
Taxonomic identifier1773 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length503 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins Probable. Mannosylates an artificial substrate, probably on a Thr residue, upon expression in M.smegmatis. Glycosylation probably requires the Sec-translocation system. Ref.3

Catalytic activity

Dolichyl phosphate D-mannose + protein = dolichyl phosphate + O-D-mannosylprotein.

Pathway

Protein modification; protein glycosylation.

Subcellular location

Cell membrane; Multi-pass membrane protein Probable Ref.3.

Sequence similarities

Belongs to the glycosyltransferase 39 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 503503Probable dolichyl-phosphate-mannose--protein mannosyltransferase
PRO_0000121517

Regions

Topological domain1 – 2323Cytoplasmic Potential
Transmembrane24 – 4421Helical; Potential
Topological domain45 – 10056Extracellular Potential
Transmembrane101 – 12121Helical; Potential
Topological domain122 – 1309Cytoplasmic Potential
Transmembrane131 – 15121Helical; Potential
Topological domain1521Extracellular Potential
Transmembrane153 – 17321Helical; Potential
Topological domain174 – 22047Cytoplasmic Potential
Transmembrane221 – 24121Helical; Potential
Topological domain242 – 26221Extracellular Potential
Transmembrane263 – 28321Helical; Potential
Topological domain284 – 37188Cytoplasmic Potential
Transmembrane372 – 39221Helical; Potential
Topological domain393 – 3997Extracellular Potential
Transmembrane400 – 42021Helical; Potential
Topological domain421 – 4233Cytoplasmic Potential
Transmembrane424 – 44421Helical; Potential
Topological domain445 – 45915Extracellular Potential
Transmembrane460 – 48021Helical; Potential
Topological domain481 – 50323Cytoplasmic Potential

Experimental info

Mutagenesis55 – 562DE → AA: Loss of protein mannosyltransferase. Ref.3
Mutagenesis551D → A: Loss of protein mannosyltransferase. Ref.3
Mutagenesis561E → A: Loss of protein mannosyltransferase. Ref.3

Sequences

Sequence LengthMass (Da)Tools
O05586 [UniParc].

Last modified August 1, 1998. Version 2.
Checksum: EB6226AA8F1442C6

FASTA50355,531
        10         20         30         40         50         60 
MVPVVSPGPL VPVADFGPLD RLRGWIVTGL ITLLATVTRF LNLGSLTDAG TPIFDEKHYA 

        70         80         90        100        110        120 
PQAWQVLNNH GVEDNPGYGL VVHPPVGKQL IAIGEAIFGY NGFGWRFTGA LLGVVLVALV 

       130        140        150        160        170        180 
VRIVRRISRS TLVGAIAGVL LICDGVSFVT ARTALLDGFL TFFVVAAFGA LIVDRDQVRE 

       190        200        210        220        230        240 
RMHIALLAGR SAATVWGPRV GVRWWRFGAG VLLGLACATK WSGVYFVLFF GAMALAFDVA 

       250        260        270        280        290        300 
ARRQYQVQRP WLGTVRRDVL PSGYALGLIP FAVYLATYAP WFASETAIDR HAVGQAVGRN 

       310        320        330        340        350        360 
SVVPLPDAVR SLWHYTAKAF HFHAGLTNSA GNYHPWESKP WTWPMSLRPV LYAIDQQDVA 

       370        380        390        400        410        420 
GCGAQSCVKA EMLVGTPAMW WLAVPVLAYA GWRMFVRRDW RYAVVLVGYC AGWLPWFADI 

       430        440        450        460        470        480 
DRQMYFFYAA TMAPFLVMGI SLVLGDILYH PGQGSERRTL GLIVVCCYVA LVVTNFAWLY 

       490        500 
PVLTGLPISQ QTWNLEIWLP SWR

« Hide

References

« Hide 'large scale' references
[1]"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence."
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. expand/collapse author list , Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G.
Nature 393:537-544(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25618 / H37Rv.
[2]"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains."
Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. expand/collapse author list , Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.
J. Bacteriol. 184:5479-5490(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CDC 1551 / Oshkosh.
[3]"Export-mediated assembly of mycobacterial glycoproteins parallels eukaryotic pathways."
VanderVen B.C., Harder J.D., Crick D.C., Belisle J.T.
Science 309:941-943(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-55 AND GLU-56.
Strain: ATCC 25618 / H37Rv.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BX842575 Genomic DNA. Translation: CAB08157.1.
AE000516 Genomic DNA. Translation: AAK45281.1.
AL123456 Genomic DNA. Translation: CCP43752.1.
PIRE70602.
RefSeqNP_215518.1. NC_000962.3.
NP_335467.1. NC_002755.2.
YP_006514363.1. NC_018143.1.

3D structure databases

ProteinModelPortalO05586.
ModBaseSearch...

Protein-protein interaction databases

STRING83332.Rv1002c.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK45281; AAK45281; MT1031.
GeneID13319564.
887882.
925170.
KEGGmtc:MT1031.
mtu:Rv1002c.
mtv:RVBD_1002c.
PATRIC18124012. VBIMycTub22151_1128.

Organism-specific databases

TubercuListRv1002c.

Phylogenomic databases

eggNOGCOG1928.
HOGENOMHOG000097888.
OMAKHYVPQA.
ProtClustDBCLSK790886.

Enzyme and pathway databases

UniPathwayUPA00378.

Family and domain databases

InterProIPR003342. Glyco_trans_39.
[Graphical view]
PfamPF02366. PMT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePMT_MYCTU
AccessionPrimary (citable) accession number: O05586
Secondary accession number(s): L0T8C2
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2002
Last sequence update: August 1, 1998
Last modified: May 1, 2013
This is version 82 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh

Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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