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Q06320

- CWLC_BACSU

UniProt

Q06320 - CWLC_BACSU

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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

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

Zn2+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. 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

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-KW
  2. extracellular region Source: UniProtKB-KW
Complete GO annotation...

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 – 19410Combined sources
Helixi196 – 20914Combined sources
Beta strandi213 – 2186Combined sources
Beta strandi221 – 23111Combined sources
Helixi232 – 24514Combined sources
Beta strandi250 – 2545Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
InParanoidiQ06320.
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

        10         20         30         40         50
MVKIFIDPGH GGSDPGATGN GLQEKTLTLQ IALALRTILT NEYEGVSLLL
60 70 80 90 100
SRTSDQYVSL NDRTNAANNW GADFFLSIHV NSGGGTGFES YIYPDVGAPT
110 120 130 140 150
TTYQSTIHSE VIQAVDFADR GKKTANFHVL RESAMPALLT ENGFIDTVSD
160 170 180 190 200
ANKLKTSSFI QSLARGHANG LEQAFNLKKT SSSGLYKVQI GAFKVKANAD
210 220 230 240 250
SLASNAEAKG FDSIVLLKDG LYKVQIGAFS SKDNADTLAA RAKNAGFDAI

VILES
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.
InParanoidi Q06320.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 100 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