SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q06320

- CWLC_BACSU

UniProt

Q06320 - CWLC_BACSU

(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)

Protein
Sporulation-specific N-acetylmuramoyl-L-alanine amidase
Gene
cwlC, BSU17410
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

Zinc Inferred.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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi10 – 101Zinc Reviewed prediction
Metal bindingi24 – 241Zinc Reviewed prediction
Metal bindingi79 – 791Zinc Reviewed prediction
Active sitei141 – 1411 Reviewed prediction

GO - Molecular functioni

  1. N-acetylmuramoyl-L-alanine amidase activity Source: UniProtKB-EC
  2. metal ion binding Source: UniProtKB-KW

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

GO - Cellular componenti

  1. cell wall Source: UniProtKB-SubCell
  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 amidase
PRO_0000164418Add
BLAST

Proteomic databases

PaxDbiQ06320.

Expressioni

Inductioni

Induced at 6 to 7 hours after sporulation.2 Publications

Interactioni

Protein-protein interaction databases

STRINGi224308.BSU17410.

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiQ06320.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini183 – 25270SPOR
Add
BLAST
Repeati184 – 219361
Add
BLAST
Repeati220 – 255362
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni184 – 255722 X 35 AA approximate tandem repeats
Add
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.

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.

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

Sequence conflict

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

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.
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: September 3, 2014
This is version 97 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

Similar proteinsi