Q02114 (CWLB_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
N-acetylmuramoyl-L-alanine amidase LytC
EC=3.5.1.28

Alternative name(s):
Cell wall hydrolase
Cell wall-associated polypeptide CWBP49
Short name=CWBP49
Major autolysin

Gene names

Name:	lytC
Synonyms:	cwlB
Ordered Locus Names:	BSU35620

Organism

Bacillus subtilis

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	496 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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. Has a high affinity for teichoic acid-endowed peptidoglycan.
Catalytic activity	Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides.
Subcellular location	Secreted › cell wall Ref.4.
Induction	Under control of SigD. Repressed by LytR. Ref.4
Disruption phenotype	Cells lacking this gene show no motility changes on swarm plates; however in combination with a acetylglucosaminidase deletion (lytD, AC P39848) greatly reduced motility is seen. Ref.5
Sequence similarities	Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family.

Ontologies

Keywords
Biological process	Cell wall biogenesis/degradation Competence Sporulation
Cellular component	Cell wall Secreted
Domain	Repeat Signal
Molecular function	Hydrolase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	cellular cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW establishment of competence for transformation Inferred from electronic annotation. Source: UniProtKB-KW peptidoglycan catabolic process Inferred from electronic annotation. Source: InterPro sporulation resulting in formation of a cellular spore Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cell wall Inferred from electronic annotation. Source: UniProtKB-SubCell extracellular region Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	N-acetylmuramoyl-L-alanine amidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 24	24
	Chain	25 – 496	472	N-acetylmuramoyl-L-alanine amidase LytC		PRO_0000006459
Regions
	Repeat	30 – 128	99	1
	Repeat	129 – 222	94	2
	Repeat	223 – 318	96	3
	Region	30 – 318	289	3 X tandem repeats

Sequences

	Sequence		Length	Mass (Da)
	Q02114 [UniParc]. Last modified July 1, 1993. Version 1. Checksum: 146FF36B41BB5EC5	FASTA	496	52,626
	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

References

	« Hide 'large scale' referencesShow '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: 1357079] [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: 1682302] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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: 9384377] [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: 11987133] [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: 8405954] [Abstract] Cited for: DISRUPTION PHENOTYPE. Strain: 168 / AC327.

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.
PIR	B41322.
RefSeq	NP_391442.1. NC_000964.3.
3D structure databases
ProteinModelPortal	Q02114.
SMR	Q02114. Positions 320-496.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000002402; EBBACP00000002402; EBBACG00000002397.
GeneID	936777.
GenomeReviews	Gene locus BSU35620 in contig AL009126_GR.
KEGG	bsu:BSU35620.
NMPDR	fig|224308.1.peg.3568.
PATRIC	18979134. VBIBacSub10457_3729.
Organism-specific databases
GenoList	BSU35620. [Micado]
Phylogenomic databases
GeneTree	EBGT00070000031903.
HOGENOM	HBG459755.
OMA	FYVIKYS.
PhylomeDB	Q02114.
ProtClustDB	CLSK887969.
Enzyme and pathway databases
BioCyc	BSUB:BSU35620-MONOMER.
Family and domain databases
InterPro	IPR007253. Cell_wall-bd_2. IPR002508. CW_Hdrlase/autolysin_cat. [Graphical view]
Gene3D	G3DSA:3.40.630.40. Cell_wall_OHase/autolysin_cat. 1 hit.
KO	K01448.
Pfam	PF01520. Amidase_3. 1 hit. PF04122. CW_binding_2. 3 hits. [Graphical view]
SMART	SM00646. Ami_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CWLB_BACSU

Accession

Primary (citable) accession number: Q02114

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	July 1, 1993
Last modified:	January 25, 2012
This is version 90 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program