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O34391

- XLYB_BACSU

UniProt

O34391 - XLYB_BACSU

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Protein
N-acetylmuramoyl-L-alanine amidase XlyB
Gene
xlyB, yjpB, BSU12460
Organism
Bacillus subtilis (strain 168)
Status
Reviewed - 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
Complete GO annotation...

GO - Biological processi

  1. establishment of competence for transformation Source: UniProtKB-KW
  2. peptidoglycan catabolic process Source: InterPro
  3. 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: Chromosome

Organism-specific databases

GenoListiBSU12460. [Micado]

Subcellular locationi

Secreted Reviewed prediction

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 – 3939 By similarity
Add
BLAST
Chaini40 – 317278N-acetylmuramoyl-L-alanine amidase XlyB
PRO_0000006458Add
BLAST

Proteomic databases

PaxDbiO34391.

Interactioni

Protein-protein interaction databases

STRINGi224308.BSU12460.

Structurei

3D structure databases

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

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

Contains 1 LysM repeat.

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG3409.
HOGENOMiHOG000273688.
KOiK01447.
OMAiQSINHIT.
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

MSIPVKKNLV SEAKYALKCP NAMSAEYITI HNTANDASAA NEISYMIGNT    50
SSTSFHFAVD DQEVIQGLPL NRNAWHTGDG TNGPGNRKSI GVEICYSKSG 100
GPKYEAAEAL AISFVAQLLK ERGWGIDRVR KHQDWSGKYC PHRILSEGRW 150
DQVKAAIEKE LNGGVSAKKA AVSSSASEYH VKKGDTLSGI AASHGASVKT 200
LQSINHITDP NHIKIGQVIK LPQTASASKS HAASSYPLPS GVIKVTSPLT 250
QGTKVKQVQT ALAALYFYPD KGAKNHGVDG VYGPKTANAV KRFQSVSGLT 300
ADGIYGPKTK AKMEEKL 317
Length:317
Mass (Da):33,863
Last modified:January 1, 1998 - v1
Checksum:i955DF80EE6DD0757
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AF034138 Genomic DNA. Translation: AAB87514.1 .
AL009126 Genomic DNA. Translation: CAB13103.1 .
PIRi B69734.
RefSeqi NP_389128.1. NC_000964.3.

3D structure databases

ProteinModelPortali O34391.
SMRi O34391. Positions 3-159, 240-316.
ModBasei Search...

Protein-protein interaction databases

STRINGi 224308.BSU12460.

Proteomic databases

PaxDbi O34391.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB13103 ; CAB13103 ; BSU12460 .
GeneIDi 936464.
KEGGi bsu:BSU12460.
PATRICi 18974233. VBIBacSub10457_1309.

Organism-specific databases

GenoListi BSU12460. [Micado ]

Phylogenomic databases

eggNOGi COG3409.
HOGENOMi HOG000273688.
KOi K01447.
OMAi QSINHIT.
OrthoDBi EOG6GFGGF.
PhylomeDBi O34391.

Enzyme and pathway databases

BioCyci BSUB:BSU12460-MONOMER.

Family and domain databases

Gene3Di 1.10.101.10. 1 hit.
3.10.350.10. 1 hit.
3.40.80.10. 1 hit.
InterProi IPR002502. Amidase_domain.
IPR018392. LysM_dom.
IPR002477. Peptidoglycan-bd-like.
[Graphical view ]
Pfami PF01510. Amidase_2. 1 hit.
PF01476. LysM. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view ]
SMARTi SM00644. Ami_2. 1 hit.
SM00257. LysM. 1 hit.
[Graphical view ]
SUPFAMi SSF47090. SSF47090. 1 hit.
SSF54106. SSF54106. 1 hit.
SSF55846. SSF55846. 1 hit.
ProtoNeti Search...

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 (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.
    , 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.

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: September 3, 2014
This is version 90 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

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