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Protein

N-acetylmuramoyl-L-alanine amidase XlyB

Gene

xlyB

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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 activityi

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

GO - Molecular functioni

  1. N-acetylmuramoyl-L-alanine amidase activity Source: UniProtKB-EC

GO - Biological processi

  1. cell wall organization Source: UniProtKB-KW
  2. establishment of competence for transformation Source: UniProtKB-KW
  3. peptidoglycan catabolic process Source: InterPro
  4. sporulation resulting in formation of a cellular spore Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Cell wall biogenesis/degradation, Competence, Sporulation

Enzyme and pathway databases

BioCyciBSUB:BSU12460-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
N-acetylmuramoyl-L-alanine amidase XlyB (EC:3.5.1.28)
Alternative name(s):
Autolysin
Cell wall hydrolase
Gene namesi
Name:xlyB
Synonyms:yjpB
Ordered Locus Names:BSU12460
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570 Componenti: Chromosome

Organism-specific databases

GenoListiBSU12460. [Micado]

Subcellular locationi

Secreted Curated

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3939By similarityAdd
BLAST
Chaini40 – 317278N-acetylmuramoyl-L-alanine amidase XlyBPRO_0000006458Add
BLAST

Proteomic databases

PaxDbiO34391.

Interactioni

Protein-protein interaction databases

STRINGi224308.BSU12460.

Structurei

3D structure databases

ProteinModelPortaliO34391.
SMRiO34391. Positions 3-159, 240-316.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati179 – 22244LysMAdd
BLAST

Sequence similaritiesi

Contains 1 LysM repeat.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG3409.
HOGENOMiHOG000273688.
InParanoidiO34391.
KOiK01447.
OMAiLDRNAWH.
OrthoDBiEOG6GFGGF.
PhylomeDBiO34391.

Family and domain databases

Gene3Di1.10.101.10. 1 hit.
3.10.350.10. 1 hit.
3.40.80.10. 1 hit.
InterProiIPR002502. Amidase_domain.
IPR018392. LysM_dom.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]
PfamiPF01510. Amidase_2. 1 hit.
PF01476. LysM. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view]
SMARTiSM00644. Ami_2. 1 hit.
SM00257. LysM. 1 hit.
[Graphical view]
SUPFAMiSSF47090. SSF47090. 1 hit.
SSF54106. SSF54106. 1 hit.
SSF55846. SSF55846. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O34391-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSIPVKKNLV SEAKYALKCP NAMSAEYITI HNTANDASAA NEISYMIGNT
60 70 80 90 100
SSTSFHFAVD DQEVIQGLPL NRNAWHTGDG TNGPGNRKSI GVEICYSKSG
110 120 130 140 150
GPKYEAAEAL AISFVAQLLK ERGWGIDRVR KHQDWSGKYC PHRILSEGRW
160 170 180 190 200
DQVKAAIEKE LNGGVSAKKA AVSSSASEYH VKKGDTLSGI AASHGASVKT
210 220 230 240 250
LQSINHITDP NHIKIGQVIK LPQTASASKS HAASSYPLPS GVIKVTSPLT
260 270 280 290 300
QGTKVKQVQT ALAALYFYPD KGAKNHGVDG VYGPKTANAV KRFQSVSGLT
310
ADGIYGPKTK AKMEEKL
Length:317
Mass (Da):33,863
Last modified:January 1, 1998 - v1
Checksum:i955DF80EE6DD0757
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF034138 Genomic DNA. Translation: AAB87514.1.
AL009126 Genomic DNA. Translation: CAB13103.1.
PIRiB69734.
RefSeqiNP_389128.1. NC_000964.3.

Genome annotation databases

EnsemblBacteriaiCAB13103; CAB13103; BSU12460.
GeneIDi936464.
KEGGibsu:BSU12460.
PATRICi18974233. VBIBacSub10457_1309.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF034138 Genomic DNA. Translation: AAB87514.1.
AL009126 Genomic DNA. Translation: CAB13103.1.
PIRiB69734.
RefSeqiNP_389128.1. NC_000964.3.

3D structure databases

ProteinModelPortaliO34391.
SMRiO34391. Positions 3-159, 240-316.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.BSU12460.

Proteomic databases

PaxDbiO34391.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB13103; CAB13103; BSU12460.
GeneIDi936464.
KEGGibsu:BSU12460.
PATRICi18974233. VBIBacSub10457_1309.

Organism-specific databases

GenoListiBSU12460. [Micado]

Phylogenomic databases

eggNOGiCOG3409.
HOGENOMiHOG000273688.
InParanoidiO34391.
KOiK01447.
OMAiLDRNAWH.
OrthoDBiEOG6GFGGF.
PhylomeDBiO34391.

Enzyme and pathway databases

BioCyciBSUB:BSU12460-MONOMER.

Family and domain databases

Gene3Di1.10.101.10. 1 hit.
3.10.350.10. 1 hit.
3.40.80.10. 1 hit.
InterProiIPR002502. Amidase_domain.
IPR018392. LysM_dom.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]
PfamiPF01510. Amidase_2. 1 hit.
PF01476. LysM. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view]
SMARTiSM00644. Ami_2. 1 hit.
SM00257. LysM. 1 hit.
[Graphical view]
SUPFAMiSSF47090. SSF47090. 1 hit.
SSF54106. SSF54106. 1 hit.
SSF55846. SSF55846. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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 (OCT-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.
    , 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(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.

Entry informationi

Entry nameiXLYB_BACSU
AccessioniPrimary (citable) accession number: O34391
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: January 1, 1998
Last modified: January 7, 2015
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.