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Q06320 (CWLC_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sporulation-specific N-acetylmuramoyl-L-alanine amidase

EC=3.5.1.28
Alternative name(s):
Autolysin
Cell wall hydrolase
Gene names
Name:cwlC
Ordered Locus Names:BSU17410
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length255 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.4 Ref.6

Catalytic activity

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

Cofactor

Zinc Probable. Ref.7

Enzyme regulation

Inhibited by EDTA. Ref.6

Subcellular location

Secretedcell wall. Note: Is associated with the mother cell wall of sporulating cells. Ref.4

Induction

Induced at 6 to 7 hours after sporulation. Ref.1 Ref.6

Domain

Contains an N-terminal catalytic domain and two C-terminal tandem repeat sequences that play an important role in peptidoglycan binding. Ref.8

Sequence similarities

Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family.

Contains 1 SPOR domain.

Biophysicochemical properties

pH dependence:

Optimum pH is 8.5-9.5. Ref.6

Temperature dependence:

Optimum temperature is 60 degrees Celsius.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4
Chain2 – 255254Sporulation-specific N-acetylmuramoyl-L-alanine amidase
PRO_0000164418

Regions

Domain183 – 25270SPOR
Repeat184 – 219361
Repeat220 – 255362
Region184 – 255722 X 35 AA approximate tandem repeats

Sites

Active site1411 Potential
Metal binding101Zinc Potential
Metal binding241Zinc Potential
Metal binding791Zinc Potential

Experimental info

Mutagenesis101H → Q: 23% of wild-type activity. Ref.7
Mutagenesis241E → A, Q or S: Loss of activity. Ref.7
Mutagenesis551D → V: Loss of activity. Ref.7
Mutagenesis791H → L: Loss of activity. Ref.7
Mutagenesis791H → Q: 15% of wild-type activity. Ref.7
Mutagenesis811N → I: Loss of activity. Ref.7
Mutagenesis1411E → Q or V: Loss of activity. Ref.7
Sequence conflict1581S → T in CAA92813. Ref.5

Secondary structure

............ 255
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q06320 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 30C950116784FBC1

FASTA25527,146
        10         20         30         40         50         60 
MVKIFIDPGH GGSDPGATGN GLQEKTLTLQ IALALRTILT NEYEGVSLLL SRTSDQYVSL 

        70         80         90        100        110        120 
NDRTNAANNW GADFFLSIHV NSGGGTGFES YIYPDVGAPT TTYQSTIHSE VIQAVDFADR 

       130        140        150        160        170        180 
GKKTANFHVL RESAMPALLT ENGFIDTVSD ANKLKTSSFI QSLARGHANG LEQAFNLKKT 

       190        200        210        220        230        240 
SSSGLYKVQI GAFKVKANAD SLASNAEAKG FDSIVLLKDG LYKVQIGAFS SKDNADTLAA 

       250 
RAKNAGFDAI VILES 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D14666 Genomic DNA. Translation: BAA03500.1.
AL009126 Genomic DNA. Translation: CAB13625.2.
Z68500 Genomic DNA. Translation: CAA92813.1.
PIRA36935.
RefSeqNP_389623.2. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1X60NMR-A177-255[»]
ProteinModelPortalQ06320.
SMRQ06320. Positions 1-255.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224308.BSU17410.

Proteomic databases

PaxDbQ06320.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB13625; CAB13625; BSU17410.
GeneID940088.
KEGGbsu:BSU17410.
PATRIC18975293. VBIBacSub10457_1838.

Organism-specific databases

GenoListBSU17410. [Micado]

Phylogenomic databases

eggNOGCOG0860.
HOGENOMHOG000163501.
KOK01448.
OrthoDBEOG6CP3X3.
ProtClustDBCLSK872830.

Enzyme and pathway databases

BioCycBSUB:BSU17410-MONOMER.

Family and domain databases

Gene3D3.30.70.1070. 1 hit.
3.40.630.40. 1 hit.
InterProIPR002508. CW_Hdrlase/autolysin_cat.
IPR007730. Sporulation-related_dom.
[Graphical view]
PfamPF01520. Amidase_3. 1 hit.
PF05036. SPOR. 1 hit.
[Graphical view]
SMARTSM00646. Ami_3. 1 hit.
[Graphical view]
SUPFAMSSF110997. SSF110997. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ06320.

Entry information

Entry nameCWLC_BACSU
AccessionPrimary (citable) accession number: Q06320
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: November 13, 2013
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList