Reviewed, UniProtKB/Swiss-Prot O34391 (XLYB_BACSU)

Names and origin

Protein names

Recommended name:
    N-acetylmuramoyl-L-alanine amidase xlyB
    EC=3.5.1.28
Alternative name(s):
    Cell wall hydrolase
    Autolysin

Gene names

Name:	xlyB
Synonyms:	yjpB
Ordered Locus Names:	BSU12460

Organism

Bacillus subtilis [Complete proteome] [HAMAP]

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	317 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology.

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 and sporulation By similarity.
Catalytic activity	Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides.
Subcellular location	Secreted Potential.
Sequence similarities	Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family. Contains 1 LysM repeat.

Ontologies

Keywords
Biological process	Cell wall biogenesis/degradation Competence Sporulation
Cellular component	Secreted
Domain	Signal
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cell wall macromolecule catabolic process Inferred from electronic annotation. Source: InterPro 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	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
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 – 39	39	By similarity
	Chain	40 – 317	278	N-acetylmuramoyl-L-alanine amidase xlyB		PRO_0000006458
Regions
	Repeat	179 – 222	44	LysM

Sequences

	Sequence		Length	Mass (Da)
	O34391-1 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 955DF80EE6DD0757	FASTA	317	33,863
	10 20 30 40 50 60 MSIPVKKNLV SEAKYALKCP NAMSAEYITI HNTANDASAA NEISYMIGNT SSTSFHFAVD 70 80 90 100 110 120 DQEVIQGLPL NRNAWHTGDG TNGPGNRKSI GVEICYSKSG GPKYEAAEAL AISFVAQLLK 130 140 150 160 170 180 ERGWGIDRVR KHQDWSGKYC PHRILSEGRW DQVKAAIEKE LNGGVSAKKA AVSSSASEYH 190 200 210 220 230 240 VKKGDTLSGI AASHGASVKT LQSINHITDP NHIKIGQVIK LPQTASASKS HAASSYPLPS 250 260 270 280 290 300 GVIKVTSPLT QGTKVKQVQT ALAALYFYPD KGAKNHGVDG VYGPKTANAV KRFQSVSGLT 310 ADGIYGPKTK AKMEEKL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequencing and characterisation of the region comprising XlyB, the second lytic enzyme of the defective prophage PBSX of Bacillus subtilis." da Silva E., Karamata D. Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 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: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF034138 Genomic DNA. Translation: AAB87514.1. AL009126 Genomic DNA. Translation: CAB13103.1.
PIR	B69734.
RefSeq	NP_389128.1.
3D structure databases
HSSP	HSSP built from PDB template 1LBU based on UniProtKB P00733.
ModBase	Search...
Genome annotation databases
GeneID	936464.
GenomeReviews	Gene locus BSU12460 in contig AL009126_GR.
KEGG	bsu:BSU12460.
NMPDR	fig|224308.1.peg.1247.
Organism-specific databases
SubtiList	BG12699. xlyB. [Micado]
CMR	Search...
Phylogenomic databases
HOGENOM	O34391.
OMA	QSINHIT.
Enzyme and pathway databases
BioCyc	BSUB224308:BSU1247-MON.
BRENDA	3.5.1.28. 150.
Family and domain databases
InterPro	IPR002502. Amidase_2. IPR002477. Peptidoglycan-bd-like. IPR018392. Peptidoglycan-bd_lysin. IPR002482. Peptidoglycan-bd_Lysin_sg. [Graphical view]
Gene3D	G3DSA:1.10.101.10. PGBD_1. 1 hit.
Pfam	PF01510. Amidase_2. 1 hit. PF01476. LysM. 1 hit. PF01471. PG_binding_1. 1 hit. [Graphical view]
SMART	SM00644. Ami_2. 1 hit. SM00257. LysM. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

XLYB_BACSU

Accession

Primary (citable) accession number: O34391

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2004
Last sequence update:	January 1, 1998
Last modified:	November 3, 2009
This is version 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)