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Q02114

- LYTC_BACSU

UniProt

Q02114 - LYTC_BACSU

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Protein
N-acetylmuramoyl-L-alanine amidase LytC
Gene
lytC, cwlB, BSU35620
Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides.1 Publication

GO - Molecular functioni

  1. N-acetylmuramoyl-L-alanine amidase activity Source: UniProtKB-EC

GO - Biological processi

  1. peptidoglycan catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Cell wall biogenesis/degradation

Enzyme and pathway databases

BioCyciBSUB:BSU35620-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:lytC
Synonyms:cwlB
Ordered Locus Names:BSU35620
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570: Chromosome

Organism-specific databases

GenoListiBSU35620. [Micado]

Subcellular locationi

Secretedcell wall
Note: LytC localizes uniformly to the cell wall, into which the peritrichous flagella are randomly inserted.3 Publications

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

Disruption phenotypei

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.3 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 24242 Publications
Add
BLAST
Chaini25 – 496472N-acetylmuramoyl-L-alanine amidase LytC
PRO_0000006459Add
BLAST

Proteomic databases

PaxDbiQ02114.

Expressioni

Inductioni

Expressed under the control of SigD (major), the transcripts being predominants at the exponential growth phase, and SigA (minor). Repressed by LytR and YvrH.2 Publications

Interactioni

Protein-protein interaction databases

STRINGi224308.BSU35620.

Structurei

3D structure databases

ProteinModelPortaliQ02114.
SMRiQ02114. Positions 320-496.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati30 – 128991
Add
BLAST
Repeati129 – 222942
Add
BLAST
Repeati223 – 318963
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni30 – 3182893 X tandem repeats
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiCOG0860.
HOGENOMiHOG000009145.
KOiK01448.
OMAiAPLAYQK.
OrthoDBiEOG6CP3X3.
PhylomeDBiQ02114.

Family and domain databases

Gene3Di3.40.630.40. 1 hit.
InterProiIPR007253. Cell_wall-bd_2.
IPR002508. CW_Hdrlase/autolysin_cat.
[Graphical view]
PfamiPF01520. Amidase_3. 1 hit.
PF04122. CW_binding_2. 3 hits.
[Graphical view]
SMARTiSM00646. Ami_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q02114-1 [UniParc]FASTAAdd to Basket

« Hide

MRSYIKVLTM CFLGLILFVP TALADNSVKR VGGSNRYGTA VQISKQMYST    50
ASTAVIVGGS SYADAISAAP LAYQKNAPLL YTNSDKLSYE TKTRLKEMQT 100
KNVIIVGGTP AVSSNTANQI KSLGISIKRI AGSNRYDTAA RVAKAMGATS 150
KAVILNGFLY ADAPAVIPYA AKNGYPILFT NKTSINSATT SVIKDKGISS 200
TVVVGGTGSI SNTVYNKLPS PTRISGSNRY ELAANIVQKL NLSTSTVYVS 250
NGFSYPDSIA GATLAAKKKQ SLILTNGENL STGARKIIGS KNMSNFMIIG 300
NTPAVSTKVA NQLKNPVVGE TIFIDPGHGD QDSGAIGNGL LEKEVNLDIA 350
KRVNTKLNAS GALPVLSRSN DTFYSLQERV NKAASAQADL FLSIHANAND 400
SSSPNGSETY YDTTYQAANS KRLAEQIQPK LAANLGTRDR GVKTAAFYVI 450
KYSKMPSVLV ETAFITNASD ASKLKQAVYK DKAAQAIHDG TVSYYR 496
Length:496
Mass (Da):52,626
Last modified:July 1, 1993 - v1
Checksum:i146FF36B41BB5EC5
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M87645 Genomic DNA. Translation: AAA22581.1.
M81324 Genomic DNA. Translation: AAA22371.1.
D10388 Genomic DNA. Translation: BAA01225.1.
AL009126 Genomic DNA. Translation: CAB15579.1.
PIRiB41322.
RefSeqiNP_391442.1. NC_000964.3.
WP_003242758.1. NZ_CM000487.1.

Genome annotation databases

EnsemblBacteriaiCAB15579; CAB15579; BSU35620.
GeneIDi936777.
KEGGibsu:BSU35620.
PATRICi18979134. VBIBacSub10457_3729.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M87645 Genomic DNA. Translation: AAA22581.1 .
M81324 Genomic DNA. Translation: AAA22371.1 .
D10388 Genomic DNA. Translation: BAA01225.1 .
AL009126 Genomic DNA. Translation: CAB15579.1 .
PIRi B41322.
RefSeqi NP_391442.1. NC_000964.3.
WP_003242758.1. NZ_CM000487.1.

3D structure databases

ProteinModelPortali Q02114.
SMRi Q02114. Positions 320-496.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 224308.BSU35620.

Proteomic databases

PaxDbi Q02114.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB15579 ; CAB15579 ; BSU35620 .
GeneIDi 936777.
KEGGi bsu:BSU35620.
PATRICi 18979134. VBIBacSub10457_3729.

Organism-specific databases

GenoListi BSU35620. [Micado ]

Phylogenomic databases

eggNOGi COG0860.
HOGENOMi HOG000009145.
KOi K01448.
OMAi APLAYQK.
OrthoDBi EOG6CP3X3.
PhylomeDBi Q02114.

Enzyme and pathway databases

BioCyci BSUB:BSU35620-MONOMER.

Family and domain databases

Gene3Di 3.40.630.40. 1 hit.
InterProi IPR007253. Cell_wall-bd_2.
IPR002508. CW_Hdrlase/autolysin_cat.
[Graphical view ]
Pfami PF01520. Amidase_3. 1 hit.
PF04122. CW_binding_2. 3 hits.
[Graphical view ]
SMARTi SM00646. Ami_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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, IDENTIFICATION BY 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.

Entry informationi

Entry nameiLYTC_BACSU
AccessioniPrimary (citable) accession number: Q02114
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: September 3, 2014
This is version 107 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

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

External Data

Dasty 3

Similar proteinsi