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O34391 (XLYB_BACSU) Reviewed, UniProtKB/Swiss-Prot

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

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
N-acetylmuramoyl-L-alanine amidase XlyB
EC=3.5.1.28
Alternative name(s):
Autolysin
Cell wall hydrolase
Gene names
Name:xlyB
Synonyms:yjpB
Ordered Locus Names:BSU12460
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus ›

Protein attributes

Sequence length317 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Autolysins are involved in some important biological processes such as cell separation, cell-wall turnover, competence for genetic transformation, formation of the flagella and sporulation By similarity.

Catalytic activity

Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides.

Subcellular location

Secreted Potential.

Sequence similarities

Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.

Contains 1 LysM repeat.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3939 By similarity
Chain40 – 317278N-acetylmuramoyl-L-alanine amidase XlyB
PRO_0000006458

Regions

Repeat179 – 22244LysM

Sequences

Sequence LengthMass (Da)Tools
O34391 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 955DF80EE6DD0757

FASTA31733,863
        10         20         30         40         50         60 
MSIPVKKNLV SEAKYALKCP NAMSAEYITI HNTANDASAA NEISYMIGNT SSTSFHFAVD 

        70         80         90        100        110        120 
DQEVIQGLPL NRNAWHTGDG TNGPGNRKSI GVEICYSKSG GPKYEAAEAL AISFVAQLLK 

       130        140        150        160        170        180 
ERGWGIDRVR KHQDWSGKYC PHRILSEGRW DQVKAAIEKE LNGGVSAKKA AVSSSASEYH 

       190        200        210        220        230        240 
VKKGDTLSGI AASHGASVKT LQSINHITDP NHIKIGQVIK LPQTASASKS HAASSYPLPS 

       250        260        270        280        290        300 
GVIKVTSPLT QGTKVKQVQT ALAALYFYPD KGAKNHGVDG VYGPKTANAV KRFQSVSGLT 

       310 
ADGIYGPKTK AKMEEKL

« Hide

References

« Hide 'large scale' references
[1]"Sequencing and characterisation of the region comprising xlyB, the second lytic enzyme of the defective prophage PBSX of Bacillus subtilis."
da Silva E., Karamata D.
Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[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. 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		AF034138 Genomic DNA. Translation: AAB87514.1.
AL009126 Genomic DNA. Translation: CAB13103.1.
PIRB69734.
RefSeqNP_389128.1. NC_000964.3.

3D structure databases

ProteinModelPortalO34391.
SMRO34391. Positions 3-159, 240-316.
ModBaseSearch...

Protein-protein interaction databases

STRING224308.BSU12460.

Proteomic databases

PaxDbO34391.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB13103; CAB13103; BSU12460.
GeneID936464.
KEGGbsu:BSU12460.
PATRIC18974233. VBIBacSub10457_1309.

Organism-specific databases

GenoListBSU12460. [Micado]

Phylogenomic databases

eggNOGCOG3409.
HOGENOMHOG000273688.
KOK01447.
OMAQSINHIT.
ProtClustDBCLSK887114.

Enzyme and pathway databases

BioCycBSUB:BSU12460-MONOMER.

Family and domain databases

Gene3D1.10.101.10. 1 hit.
3.40.80.10. 1 hit.
InterProIPR002502. Amidase_domain.
IPR002477. Peptidoglycan-bd-like.
IPR018392. Peptidoglycan-bd_lysin.
IPR002482. Peptidoglycan-bd_Lysin_subgr.
[Graphical view]
PfamPF01510. Amidase_2. 1 hit.
PF01476. LysM. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view]
SMARTSM00644. Ami_2. 1 hit.
SM00257. LysM. 1 hit.
[Graphical view]
SUPFAMSSF55846. Amidase_2. 1 hit.
SSF47090. PGBD_like. 1 hit.
ProtoNetSearch...

Entry information

Entry nameXLYB_BACSU
AccessionPrimary (citable) accession number: O34391
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: January 1, 1998
Last modified: May 1, 2013
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Bacillus subtilis

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

SIMILARITY comments

Index of protein domains and families

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