Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q06320

- CWLC_BACSU

UniProt

Q06320 - CWLC_BACSU

Protein

Sporulation-specific N-acetylmuramoyl-L-alanine amidase

Gene

cwlC

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 98 (01 Oct 2014)
      Sequence version 1 (01 Feb 1995)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Autolysins are 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. CwlC is able to hydrolyze type A cell walls such as B.subtilis. Its main function is to lyze the mother cell wall peptidoglycan, playing a role during sporulation.2 Publications

    Catalytic activityi

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

    Cofactori

    Zinc.1 Publication

    Enzyme regulationi

    Inhibited by EDTA.1 Publication

    pH dependencei

    Optimum pH is 8.5-9.5.1 Publication

    Temperature dependencei

    Optimum temperature is 60 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi10 – 101ZincSequence Analysis
    Metal bindingi24 – 241ZincSequence Analysis
    Metal bindingi79 – 791ZincSequence Analysis
    Active sitei141 – 1411Sequence Analysis

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. 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

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciBSUB:BSU17410-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Sporulation-specific N-acetylmuramoyl-L-alanine amidase (EC:3.5.1.28)
    Alternative name(s):
    Autolysin
    Cell wall hydrolase
    Gene namesi
    Name:cwlC
    Ordered Locus Names:BSU17410
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU17410. [Micado]

    Subcellular locationi

    Secretedcell wall 1 Publication
    Note: Is associated with the mother cell wall of sporulating cells.

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cell wall, Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi10 – 101H → Q: 23% of wild-type activity. 1 Publication
    Mutagenesisi24 – 241E → A, Q or S: Loss of activity. 1 Publication
    Mutagenesisi55 – 551D → V: Loss of activity. 1 Publication
    Mutagenesisi79 – 791H → L: Loss of activity. 1 Publication
    Mutagenesisi79 – 791H → Q: 15% of wild-type activity. 1 Publication
    Mutagenesisi81 – 811N → I: Loss of activity. 1 Publication
    Mutagenesisi141 – 1411E → Q or V: Loss of activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 255254Sporulation-specific N-acetylmuramoyl-L-alanine amidasePRO_0000164418Add
    BLAST

    Proteomic databases

    PaxDbiQ06320.

    Expressioni

    Inductioni

    Induced at 6 to 7 hours after sporulation.1 Publication

    Interactioni

    Protein-protein interaction databases

    STRINGi224308.BSU17410.

    Structurei

    Secondary structure

    1
    255
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi185 – 19410
    Helixi196 – 20914
    Beta strandi213 – 2186
    Beta strandi221 – 23111
    Helixi232 – 24514
    Beta strandi250 – 2545

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1X60NMR-A177-255[»]
    ProteinModelPortaliQ06320.
    SMRiQ06320. Positions 1-255.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ06320.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini180 – 25475SPORAdd
    BLAST
    Repeati184 – 219361Add
    BLAST
    Repeati220 – 255362Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni184 – 255722 X 35 AA approximate tandem repeatsAdd
    BLAST

    Domaini

    Contains an N-terminal catalytic domain and two C-terminal tandem repeat sequences that play an important role in peptidoglycan binding.1 Publication

    Sequence similaritiesi

    Contains 1 SPOR domain.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG0860.
    HOGENOMiHOG000163501.
    KOiK01448.
    OrthoDBiEOG6CP3X3.
    PhylomeDBiQ06320.

    Family and domain databases

    Gene3Di3.30.70.1070. 1 hit.
    3.40.630.40. 1 hit.
    InterProiIPR002508. CW_Hdrlase/autolysin_cat.
    IPR007730. Sporulation-related_dom.
    [Graphical view]
    PfamiPF01520. Amidase_3. 1 hit.
    PF05036. SPOR. 1 hit.
    [Graphical view]
    SMARTiSM00646. Ami_3. 1 hit.
    [Graphical view]
    SUPFAMiSSF110997. SSF110997. 1 hit.
    PROSITEiPS51724. SPOR. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q06320-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVKIFIDPGH GGSDPGATGN GLQEKTLTLQ IALALRTILT NEYEGVSLLL    50
    SRTSDQYVSL NDRTNAANNW GADFFLSIHV NSGGGTGFES YIYPDVGAPT 100
    TTYQSTIHSE VIQAVDFADR GKKTANFHVL RESAMPALLT ENGFIDTVSD 150
    ANKLKTSSFI QSLARGHANG LEQAFNLKKT SSSGLYKVQI GAFKVKANAD 200
    SLASNAEAKG FDSIVLLKDG LYKVQIGAFS SKDNADTLAA RAKNAGFDAI 250
    VILES 255
    Length:255
    Mass (Da):27,146
    Last modified:February 1, 1995 - v1
    Checksum:i30C950116784FBC1
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti158 – 1581S → T in CAA92813. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D14666 Genomic DNA. Translation: BAA03500.1.
    AL009126 Genomic DNA. Translation: CAB13625.2.
    Z68500 Genomic DNA. Translation: CAA92813.1.
    PIRiA36935.
    RefSeqiNP_389623.2. NC_000964.3.
    WP_003244862.1. NZ_CM000487.1.

    Genome annotation databases

    EnsemblBacteriaiCAB13625; CAB13625; BSU17410.
    GeneIDi940088.
    KEGGibsu:BSU17410.
    PATRICi18975293. VBIBacSub10457_1838.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D14666 Genomic DNA. Translation: BAA03500.1 .
    AL009126 Genomic DNA. Translation: CAB13625.2 .
    Z68500 Genomic DNA. Translation: CAA92813.1 .
    PIRi A36935.
    RefSeqi NP_389623.2. NC_000964.3.
    WP_003244862.1. NZ_CM000487.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1X60 NMR - A 177-255 [» ]
    ProteinModelPortali Q06320.
    SMRi Q06320. Positions 1-255.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224308.BSU17410.

    Proteomic databases

    PaxDbi Q06320.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB13625 ; CAB13625 ; BSU17410 .
    GeneIDi 940088.
    KEGGi bsu:BSU17410.
    PATRICi 18975293. VBIBacSub10457_1838.

    Organism-specific databases

    GenoListi BSU17410. [Micado ]

    Phylogenomic databases

    eggNOGi COG0860.
    HOGENOMi HOG000163501.
    KOi K01448.
    OrthoDBi EOG6CP3X3.
    PhylomeDBi Q06320.

    Enzyme and pathway databases

    BioCyci BSUB:BSU17410-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei Q06320.

    Family and domain databases

    Gene3Di 3.30.70.1070. 1 hit.
    3.40.630.40. 1 hit.
    InterProi IPR002508. CW_Hdrlase/autolysin_cat.
    IPR007730. Sporulation-related_dom.
    [Graphical view ]
    Pfami PF01520. Amidase_3. 1 hit.
    PF05036. SPOR. 1 hit.
    [Graphical view ]
    SMARTi SM00646. Ami_3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF110997. SSF110997. 1 hit.
    PROSITEi PS51724. SPOR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of a sporulation-specific cell wall hydrolase gene of Bacillus subtilis."
      Kuroda A., Asami Y., Sekiguchi J.
      J. Bacteriol. 175:6260-6268(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION.
      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.
    3. "From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later."
      Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.
      Microbiology 155:1758-1775(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION TO 158.
    4. "Characterization of the involvement of two compensatory autolysins in mother cell lysis during sporulation of Bacillus subtilis 168."
      Smith T.J., Foster S.J.
      J. Bacteriol. 177:3855-3862(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-11, FUNCTION, CHARACTERIZATION, SUBCELLULAR LOCATION.
      Strain: 168.
    5. Scotti C., Valbuzzi A., Perego M., Galizzi A., Albertini A.M.
      Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 115-255.
      Strain: 168.
    6. "Overexpression, purification, and characterization of Bacillus subtilis N-acetylmuramoyl-L-alanine amidase CwlC."
      Shida T., Hattori H., Ise F., Sekiguchi J.
      Biosci. Biotechnol. Biochem. 64:1522-1525(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
    7. "Mutational analysis of catalytic sites of the cell wall lytic N-acetylmuramoyl-L-alanine amidases CwlC and CwlV."
      Shida T., Hattori H., Ise F., Sekiguchi J.
      J. Biol. Chem. 276:28140-28146(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: COFACTOR, MUTAGENESIS OF HIS-10; GLU-24; ASP-55; HIS-79; ASN-81 AND GLU-141.
    8. "Solution structure of the peptidoglycan binding domain of Bacillus subtilis cell wall lytic enzyme CwlC: characterization of the sporulation-related repeats by NMR."
      Mishima M., Shida T., Yabuki K., Kato K., Sekiguchi J., Kojima C.
      Biochemistry 44:10153-10163(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 177-255, DOMAIN.

    Entry informationi

    Entry nameiCWLC_BACSU
    AccessioniPrimary (citable) accession number: Q06320
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 98 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

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

    External Data

    Dasty 3