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P68585 (MTBP_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phi-3T prophage-derived modification methylase Phi3TI

Short name=M.Phi3TI
EC=2.1.1.37
Alternative name(s):
Cytosine-specific methyltransferase Phi3TI
Gene names
Name:mtbP
Ordered Locus Names:BSU20250
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length443 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

This enzyme methylates the first cytosine within the sequences GGCC and GCNGC By similarity.

Catalytic activity

S-adenosyl-L-methionine + DNA = S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine.

Sequence similarities

Belongs to the class I-like SAM-binding methyltransferase superfamily. C5-methyltransferase family.

Contains 1 SAM-dependent MTase C5-type domain.

Ontologies

Keywords
   Biological processRestriction system
   LigandS-adenosyl-L-methionine
   Molecular functionMethyltransferase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA restriction-modification system

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionDNA (cytosine-5-)-methyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

DNA binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 443443Phi-3T prophage-derived modification methylase Phi3TI
PRO_0000087865

Regions

Domain4 – 440437SAM-dependent MTase C5-type

Sites

Active site781 By similarity

Sequences

Sequence LengthMass (Da)Tools
P68585 [UniParc].

Last modified December 7, 2004. Version 1.
Checksum: 2BF02005159E9879

FASTA44350,510
        10         20         30         40         50         60 
MSKLRVMSLF SGIGAFEAAL RNIGVDYELI GFSEIDKYAI KSYCAIHNVS ETLNVGDISK 

        70         80         90        100        110        120 
AKKDNIPYFD LLTSGFPCPT FSVAGGRDGM EYKCSNCSHE HLITYEDYKK GVKCPKCEAV 

       130        140        150        160        170        180 
SKAKDERGTL FFETALLAEE KKPKFVILEN VKGLINSGNG QVLRIISETM NNIGYRIDLE 

       190        200        210        220        230        240 
LLNSKFFNVP QNRERVYIIG IREDLVENEQ WVVGQKRNDV LSKGKKRLQE INIKSFNFKW 

       250        260        270        280        290        300 
PLQDTVTKRL REILEDFVDE KYYLNEEKTK KLVEQLGTAP LQKQEVREPL MVGHVDLKGH 

       310        320        330        340        350        360 
DAIKRVYSPE GLSPTLTTMG GGHREPKIAE KQKEVRAVLT PEREEKRQNG RRFKENGEPA 

       370        380        390        400        410        420 
FTVNTIDRHG VAIGEYPKYK IRKLSPLECW RLQAFDDEDF EKAFAAGISN SQLYKQAGNS 

       430        440 
ITVSVLESIF QELIHTYVNK ESE 

« Hide

References

[1]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL009126 Genomic DNA. Translation: CAB13917.1.
RefSeqNP_389907.1. NC_000964.3.

3D structure databases

ProteinModelPortalP68585.
SMRP68585. Positions 1-441.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224308.BSU20250.

Protein family/group databases

REBASE3140. M.BsuMIIP.

Proteomic databases

PaxDbP68585.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB13917; CAB13917; BSU20250.
GeneID939532.
KEGGbsu:BSU20250.
PATRIC18975891. VBIBacSub10457_2136.

Organism-specific databases

GenoListBSU20250. [Micado]

Phylogenomic databases

eggNOGCOG0270.
HOGENOMHOG000225505.
KOK00558.
OMACEKDKFA.
OrthoDBEOG6PZXGV.
ProtClustDBCLSK887444.

Enzyme and pathway databases

BioCycBSUB:BSU20250-MONOMER.

Family and domain databases

InterProIPR018117. C5_DNA_meth_AS.
IPR001525. C5_MeTfrase.
[Graphical view]
PANTHERPTHR10629. PTHR10629. 1 hit.
PfamPF00145. DNA_methylase. 2 hits.
[Graphical view]
PRINTSPR00105. C5METTRFRASE.
TIGRFAMsTIGR00675. dcm. 1 hit.
PROSITEPS00094. C5_MTASE_1. 1 hit.
PS00095. C5_MTASE_2. 1 hit.
PS51679. SAM_MT_C5. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMTBP_BACSU
AccessionPrimary (citable) accession number: P68585
Secondary accession number(s): P05795
Entry history
Integrated into UniProtKB/Swiss-Prot: December 7, 2004
Last sequence update: December 7, 2004
Last modified: April 16, 2014
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Restriction enzymes and methylases

Classification of restriction enzymes and methylases and list of entries

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList