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Q02114 (LYTC_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
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 names
Name:lytC
Synonyms:cwlB
Ordered Locus Names:BSU35620
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length496 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 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. Ref.2 Ref.9

Catalytic activity

Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides. Ref.2

Subcellular location

Secretedcell wall. Note: LytC localizes uniformly to the cell wall, into which the peritrichous flagella are randomly inserted. Ref.2 Ref.4 Ref.7

Induction

Expressed under the control of SigD (major), the transcripts being predominants at the exponential growth phase, and SigA (minor). Repressed by LytR and YvrH. Ref.4 Ref.6

Disruption phenotype

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. Ref.2 Ref.5 Ref.9

Sequence similarities

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

Ontologies

Keywords
   Biological processCell wall biogenesis/degradation
   Cellular componentCell wall
Secreted
   DomainRepeat
Signal
   Molecular functionHydrolase
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processpeptidoglycan catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcell wall

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular region

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionN-acetylmuramoyl-L-alanine amidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Ref.2 Ref.4
Chain25 – 496472N-acetylmuramoyl-L-alanine amidase LytC
PRO_0000006459

Regions

Repeat30 – 128991
Repeat129 – 222942
Repeat223 – 318963
Region30 – 3182893 X tandem repeats

Sequences

Sequence LengthMass (Da)Tools
Q02114 [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: 146FF36B41BB5EC5

FASTA49652,626
        10         20         30         40         50         60 
MRSYIKVLTM CFLGLILFVP TALADNSVKR VGGSNRYGTA VQISKQMYST ASTAVIVGGS 

        70         80         90        100        110        120 
SYADAISAAP LAYQKNAPLL YTNSDKLSYE TKTRLKEMQT KNVIIVGGTP AVSSNTANQI 

       130        140        150        160        170        180 
KSLGISIKRI AGSNRYDTAA RVAKAMGATS KAVILNGFLY ADAPAVIPYA AKNGYPILFT 

       190        200        210        220        230        240 
NKTSINSATT SVIKDKGISS TVVVGGTGSI SNTVYNKLPS PTRISGSNRY ELAANIVQKL 

       250        260        270        280        290        300 
NLSTSTVYVS NGFSYPDSIA GATLAAKKKQ SLILTNGENL STGARKIIGS KNMSNFMIIG 

       310        320        330        340        350        360 
NTPAVSTKVA NQLKNPVVGE TIFIDPGHGD QDSGAIGNGL LEKEVNLDIA KRVNTKLNAS 

       370        380        390        400        410        420 
GALPVLSRSN DTFYSLQERV NKAASAQADL FLSIHANAND SSSPNGSETY YDTTYQAANS 

       430        440        450        460        470        480 
KRLAEQIQPK LAANLGTRDR GVKTAAFYVI KYSKMPSVLV ETAFITNASD ASKLKQAVYK 

       490 
DKAAQAIHDG TVSYYR 

« Hide

References

« Hide 'large scale' references
[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. 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.
[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, 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M87645 Genomic DNA. Translation: AAA22581.1.
M81324 Genomic DNA. Translation: AAA22371.1.
D10388 Genomic DNA. Translation: BAA01225.1.
AL009126 Genomic DNA. Translation: CAB15579.1.
PIRB41322.
RefSeqNP_391442.1. NC_000964.3.

3D structure databases

ProteinModelPortalQ02114.
SMRQ02114. Positions 320-496.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224308.BSU35620.

Proteomic databases

PaxDbQ02114.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB15579; CAB15579; BSU35620.
GeneID936777.
KEGGbsu:BSU35620.
PATRIC18979134. VBIBacSub10457_3729.

Organism-specific databases

GenoListBSU35620. [Micado]

Phylogenomic databases

eggNOGCOG0860.
HOGENOMHOG000009145.
KOK01448.
OMAFYVIKYS.
OrthoDBEOG6CP3X3.
ProtClustDBCLSK887969.

Enzyme and pathway databases

BioCycBSUB:BSU35620-MONOMER.

Family and domain databases

Gene3D3.40.630.40. 1 hit.
InterProIPR007253. Cell_wall-bd_2.
IPR002508. CW_Hdrlase/autolysin_cat.
[Graphical view]
PfamPF01520. Amidase_3. 1 hit.
PF04122. CW_binding_2. 3 hits.
[Graphical view]
SMARTSM00646. Ami_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLYTC_BACSU
AccessionPrimary (citable) accession number: Q02114
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: November 13, 2013
This is version 102 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

Bacillus subtilis

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