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Q02114

- LYTC_BACSU

UniProt

Q02114 - LYTC_BACSU

Protein

N-acetylmuramoyl-L-alanine amidase LytC

Gene

lytC

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 1 (01 Jul 1993)
      Previous versions | rss
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    Functioni

    Autolysins are cell wall hydrolases involved in some important biological processes such as cell separation, cell-wall turnover, competence for genetic transformation, formation of the flagella - in particular of its basal body - and sporulation. Has a high affinity for teichoic acid-endowed peptidoglycan. LytC is required for efficient swarming motility but not at the level of cell separation or flagellum biosynthesis. Rather, LytC appears to be important for proper flagellar function.2 Publications

    Catalytic activityi

    Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides.1 Publication

    GO - Molecular functioni

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

    GO - Biological processi

    1. peptidoglycan catabolic process Source: InterPro

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Cell wall biogenesis/degradation

    Enzyme and pathway databases

    BioCyciBSUB:BSU35620-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    N-acetylmuramoyl-L-alanine amidase LytC (EC:3.5.1.28)
    Alternative name(s):
    Cell wall-associated polypeptide CWBP49
    Short name:
    CWBP49
    Major autolysin
    Vegetative cell wall hydrolase LytC
    Gene namesi
    Name:lytC
    Synonyms:cwlB
    Ordered Locus Names:BSU35620
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU35620. [Micado]

    Subcellular locationi

    Secretedcell wall 3 Publications
    Note: LytC localizes uniformly to the cell wall, into which the peritrichous flagella are randomly inserted.

    GO - Cellular componenti

    1. cell wall Source: UniProtKB-SubCell
    2. extracellular region Source: UniProtKB-KW

    Keywords - Cellular componenti

    Cell wall, Secreted

    Pathology & Biotechi

    Disruption phenotypei

    Inactivation of this gene leads to an approximately 90% decrease in the total cell wall hydrolytic activity of stationary-phase cells and extraordinary resistance to cell lysis, even after 6 days of incubation at 37 degrees Celsius. Cells from domesticated laboratory strains lacking this gene show no motility changes on swarm plates; however in combination with an acetylglucosaminidase deletion (lytD, AC P39848) greatly reduced motility is seen. They also show no apparent changes in cell morphology, competence, sporulation, or germination. Cells from an undomesticated strain (3610) lacking this gene show a reduction in the rate of swarming motility.3 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 24242 PublicationsAdd
    BLAST
    Chaini25 – 496472N-acetylmuramoyl-L-alanine amidase LytCPRO_0000006459Add
    BLAST

    Proteomic databases

    PaxDbiQ02114.

    Expressioni

    Inductioni

    Expressed under the control of SigD (major), the transcripts being predominants at the exponential growth phase, and SigA (minor). Repressed by LytR and YvrH.4 Publications

    Interactioni

    Protein-protein interaction databases

    STRINGi224308.BSU35620.

    Structurei

    3D structure databases

    ProteinModelPortaliQ02114.
    SMRiQ02114. Positions 320-496.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati30 – 128991Add
    BLAST
    Repeati129 – 222942Add
    BLAST
    Repeati223 – 318963Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni30 – 3182893 X tandem repeatsAdd
    BLAST

    Sequence similaritiesi

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiCOG0860.
    HOGENOMiHOG000009145.
    KOiK01448.
    OMAiAPLAYQK.
    OrthoDBiEOG6CP3X3.
    PhylomeDBiQ02114.

    Family and domain databases

    Gene3Di3.40.630.40. 1 hit.
    InterProiIPR007253. Cell_wall-bd_2.
    IPR002508. CW_Hdrlase/autolysin_cat.
    [Graphical view]
    PfamiPF01520. Amidase_3. 1 hit.
    PF04122. CW_binding_2. 3 hits.
    [Graphical view]
    SMARTiSM00646. Ami_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q02114-1 [UniParc]FASTAAdd to Basket

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    MRSYIKVLTM CFLGLILFVP TALADNSVKR VGGSNRYGTA VQISKQMYST    50
    ASTAVIVGGS SYADAISAAP LAYQKNAPLL YTNSDKLSYE TKTRLKEMQT 100
    KNVIIVGGTP AVSSNTANQI KSLGISIKRI AGSNRYDTAA RVAKAMGATS 150
    KAVILNGFLY ADAPAVIPYA AKNGYPILFT NKTSINSATT SVIKDKGISS 200
    TVVVGGTGSI SNTVYNKLPS PTRISGSNRY ELAANIVQKL NLSTSTVYVS 250
    NGFSYPDSIA GATLAAKKKQ SLILTNGENL STGARKIIGS KNMSNFMIIG 300
    NTPAVSTKVA NQLKNPVVGE TIFIDPGHGD QDSGAIGNGL LEKEVNLDIA 350
    KRVNTKLNAS GALPVLSRSN DTFYSLQERV NKAASAQADL FLSIHANAND 400
    SSSPNGSETY YDTTYQAANS KRLAEQIQPK LAANLGTRDR GVKTAAFYVI 450
    KYSKMPSVLV ETAFITNASD ASKLKQAVYK DKAAQAIHDG TVSYYR 496
    Length:496
    Mass (Da):52,626
    Last modified:July 1, 1993 - v1
    Checksum:i146FF36B41BB5EC5
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M87645 Genomic DNA. Translation: AAA22581.1.
    M81324 Genomic DNA. Translation: AAA22371.1.
    D10388 Genomic DNA. Translation: BAA01225.1.
    AL009126 Genomic DNA. Translation: CAB15579.1.
    PIRiB41322.
    RefSeqiNP_391442.1. NC_000964.3.
    WP_003242758.1. NZ_CM000487.1.

    Genome annotation databases

    EnsemblBacteriaiCAB15579; CAB15579; BSU35620.
    GeneIDi936777.
    KEGGibsu:BSU35620.
    PATRICi18979134. VBIBacSub10457_3729.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M87645 Genomic DNA. Translation: AAA22581.1 .
    M81324 Genomic DNA. Translation: AAA22371.1 .
    D10388 Genomic DNA. Translation: BAA01225.1 .
    AL009126 Genomic DNA. Translation: CAB15579.1 .
    PIRi B41322.
    RefSeqi NP_391442.1. NC_000964.3.
    WP_003242758.1. NZ_CM000487.1.

    3D structure databases

    ProteinModelPortali Q02114.
    SMRi Q02114. Positions 320-496.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224308.BSU35620.

    Proteomic databases

    PaxDbi Q02114.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB15579 ; CAB15579 ; BSU35620 .
    GeneIDi 936777.
    KEGGi bsu:BSU35620.
    PATRICi 18979134. VBIBacSub10457_3729.

    Organism-specific databases

    GenoListi BSU35620. [Micado ]

    Phylogenomic databases

    eggNOGi COG0860.
    HOGENOMi HOG000009145.
    KOi K01448.
    OMAi APLAYQK.
    OrthoDBi EOG6CP3X3.
    PhylomeDBi Q02114.

    Enzyme and pathway databases

    BioCyci BSUB:BSU35620-MONOMER.

    Family and domain databases

    Gene3Di 3.40.630.40. 1 hit.
    InterProi IPR007253. Cell_wall-bd_2.
    IPR002508. CW_Hdrlase/autolysin_cat.
    [Graphical view ]
    Pfami PF01520. Amidase_3. 1 hit.
    PF04122. CW_binding_2. 3 hits.
    [Graphical view ]
    SMARTi SM00646. Ami_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequencing and analysis of the Bacillus subtilis lytRABC divergon: a regulatory unit encompassing the structural genes of the N-acetylmuramoyl-L-alanine amidase and its modifier."
      Lazarevic V., Margot P., Soldo B., Karamata D.
      J. Gen. Microbiol. 138:1949-1961(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], REPRESSION BY LYTR.
      Strain: 168.
    2. "Molecular cloning and sequencing of a major Bacillus subtilis autolysin gene."
      Kuroda A., Sekiguchi J.
      J. Bacteriol. 173:7304-7312(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 25-44 AND 297-309, FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION.
      Strain: 168.
    3. "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.
    4. "Stabilization of cell wall proteins in Bacillus subtilis: a proteomic approach."
      Antelmann H., Yamamoto H., Sekiguchi J., Hecker M.
      Proteomics 2:591-602(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF N-TERMINUS, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, INDUCTION.
      Strain: 168.
    5. "Bacillus subtilis mutant deficient in the major autolytic amidase and glucosaminidase is impaired in motility."
      Rashid M.H., Kuroda A., Sekiguchi J.
      FEMS Microbiol. Lett. 112:135-140(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.
      Strain: 168 / AC327.
    6. "High-level transcription of the major Bacillus subtilis autolysin operon depends on expression of the sigma D gene and is affected by a sin (flaD) mutation."
      Kuroda A., Sekiguchi J.
      J. Bacteriol. 175:795-801(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
      Strain: 168 / AC327.
    7. "Localization of the vegetative cell wall hydrolases LytC, LytE, and LytF on the Bacillus subtilis cell surface and stability of these enzymes to cell wall-bound or extracellular proteases."
      Yamamoto H., Kurosawa S., Sekiguchi J.
      J. Bacteriol. 185:6666-6677(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
      Strain: 168.
    8. "Functional analysis of the YvrGHb two-component system of Bacillus subtilis: identification of the regulated genes by DNA microarray and northern blot analyses."
      Serizawa M., Kodama K., Yamamoto H., Kobayashi K., Ogasawara N., Sekiguchi J.
      Biosci. Biotechnol. Biochem. 69:2155-2169(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: REPRESSION BY YVRH.
      Strain: 168.
    9. "Role of the sigmaD-dependent autolysins in Bacillus subtilis population heterogeneity."
      Chen R., Guttenplan S.B., Blair K.M., Kearns D.B.
      J. Bacteriol. 191:5775-5784(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN SWARMING MOTILITY, DISRUPTION PHENOTYPE.
      Strain: 168 / PY79 and 3610.

    Entry informationi

    Entry nameiLYTC_BACSU
    AccessioniPrimary (citable) accession number: Q02114
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: July 1, 1993
    Last modified: October 1, 2014
    This is version 108 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, Direct protein sequencing, 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