O34680 (YDIP_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable BsuMI modification methylase subunit YdiP
Short name=M2.BsuMI
EC=2.1.1.37

Alternative name(s):
Cytosine-specific methyltransferase M2.BsuMI

Gene names

Name:	ydiP
Ordered Locus Names:	BSU06070

Organism

Bacillus subtilis (strain 168) [Reference proteome] [HAMAP]

Taxonomic identifier

224308 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus subtilis group › Bacillus subtilis › Bacillus subtilis subsp. subtilis

Protein attributes

Sequence length	389 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	This methylase may recognize the double-stranded sequence CTCGAG, causing specific methylation on C-? on both strands, and protects the DNA from cleavage by the BsuMI endonuclease. Ref.3 Ref.5
Catalytic activity	S-adenosyl-L-methionine + DNA = S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine.
Subunit structure	May form a complex with YdiO, also seems to be active alone.
Developmental stage	Not expressed during sporulation. Ref.5
Induction	Constitutively expressed during exponential growth. Encoded in an operon with ydiO and in a second with groES, groEL, ydiM and ydiN. This second operon is heat-inducible. Ref.5
Disruption phenotype	Essential for growth, it can be disrupted once one of the components of the corresponding BsuMI restriction endonuclease complex (AC O34303, O34885, O35025) has been disrupted. Ref.5
Sequence similarities	Belongs to the C5-methyltransferase family.
Caution	The characterized enzyme (Ref.3) was reported to be a monomer of approximately 45 kDa; it is not clear whether this corresponds to YdiO, YdiP or to another activity altogether.

Ontologies

Keywords
Biological process	Restriction system
Ligand	S-adenosyl-L-methionine
Molecular function	Methyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	C-5 methylation of cytosine Inferred from electronic annotation. Source: GOC DNA restriction-modification system Inferred from mutant phenotype Ref.5. Source: UniProtKB
Molecular_function	DNA (cytosine-5-)-methyltransferase activity Inferred from electronic annotation. Source: EC DNA binding Inferred from electronic annotation. Source: InterPro methyltransferase activity Non-traceable author statement Ref.5. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 389	389	Probable BsuMI modification methylase subunit YdiP		PRO_0000379885
Sites
	Active site	69	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	O34680 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 16578833225AFE22	FASTA	389	43,284
	10 20 30 40 50 60 MKVVSLFSGI GGIELGLHQS GHTTEIFCEV DPLAKAVLSK NFPGVKIEDD INEIRELPSC 70 80 90 100 110 120 DLVAAGFPCQ DLSQAGGKEG IDGSRSGLVK KLFELIEKKE HANRPPWILI ENVPYMLRLN 130 140 150 160 170 180 RGKAMSYLTS VLSELGYTWA YRTVDARCFG LPQRRHRVIL LASLFEDPKD VIFSQDHSEP 190 200 210 220 230 240 DLDGKPSVVD HSNYYGFYWT EGLRGVGWAR EAVPPIKCGS SVGIASPPAV WSPYEDIVGT 250 260 270 280 290 300 INIRDAERLQ GFPEDWTNIT TETGKDIKEG ARWRLVGNAV SVRVSKWIGE NLSQPKGSIS 310 320 330 340 350 360 DFEGELVTKT WPSAAWGYGD KKYKVPVSKW VANTEQIAIS EFLNHPLKPL SARALNGFLG 370 380 RAARCTNVNY SDEFINSLER CKDRQLQKV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence analysis of the groESL-cotA region of the Bacillus subtilis genome, containing the restriction/modification system genes." Kasahara Y., Nakai S., Ogasawara N., Yata K., Sadaie Y. DNA Res. 4:335-339(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB 3610 / VKM B-501.
[2]	"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. , 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.
[3]	"DNA methyltransferase of Bacillus subtilis Marburg: purification, properties and further evidence of specificity." Guha S. Gene 74:77-81(1988) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION. Strain: 168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB 3610 / VKM B-501.
[4]	"Restriction and modification in Bacillus subtilis Marburg 168: target sites and effects on plasmid transformation." Bron S., Janniere L., Ehrlich S.D. Mol. Gen. Genet. 211:186-189(1988) [PubMed] [Europe PMC] [Abstract] Cited for: DNA TARGET SEQUENCE. Strain: 168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB 3610 / VKM B-501.
[5]	"Molecular organization of intrinsic restriction and modification genes BsuM of Bacillus subtilis Marburg." Ohshima H., Matsuoka S., Asai K., Sadaie Y. J. Bacteriol. 184:381-389(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DEVELOPMENTAL STAGE, INDUCTION, OPERON STRUCTURE, DISRUPTION PHENOTYPE. Strain: 168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB 3610 / VKM B-501.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB007637 Genomic DNA. Translation: BAA22751.1. AL009126 Genomic DNA. Translation: CAB12426.1.
PIR	A69788.
RefSeq	NP_388488.1. NC_000964.3.
3D structure databases
HSSP	HSSP built from PDB template 1SVU based on UniProtKB P05102.
ProteinModelPortal	O34680.
SMR	O34680. Positions 1-296.
ModBase	Search...
Protein-protein interaction databases
STRING	224308.BSU06070.
Protein family/group databases
REBASE	3613. M2.BsuMI.
Proteomic databases
PaxDb	O34680.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAB12426; CAB12426; BSU06070.
GeneID	939876.
KEGG	bsu:BSU06070.
PATRIC	18972846. VBIBacSub10457_0637.
Organism-specific databases
GenoList	BSU06070.
Phylogenomic databases
eggNOG	COG0270.
HOGENOM	HOG000226162.
KO	K00558.
OMA	GWAVNAV.
ProtClustDB	CLSK561028.
Enzyme and pathway databases
BioCyc	BSUB:BSU06070-MONOMER.
Family and domain databases
InterPro	IPR018117. C5_DNA_meth_AS. IPR001525. C5_MeTfrase. [Graphical view]
PANTHER	PTHR10629. PTHR10629. 1 hit.
Pfam	PF00145. DNA_methylase. 2 hits. [Graphical view]
PRINTS	PR00105. C5METTRFRASE.
TIGRFAMs	TIGR00675. dcm. 1 hit.
PROSITE	PS00094. C5_MTASE_1. 1 hit. PS00095. C5_MTASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

YDIP_BACSU

Accession

Primary (citable) accession number: O34680
Secondary accession number(s): Q797D0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 28, 2009
Last sequence update:	January 1, 1998
Last modified:	May 1, 2013
This is version 85 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program