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O34391

- XLYB_BACSU

UniProt

O34391 - XLYB_BACSU

Protein

N-acetylmuramoyl-L-alanine amidase XlyB

Gene

xlyB

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 91 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      Previous versions | rss
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    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. 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

    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 Curated

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    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.
    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...
    MobiDBi 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

    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: October 1, 2014
    This is version 91 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