P39800 (XLYA_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Alternative name(s):
Autolysin
Cell wall hydrolase

Gene names

Name:	xlyA
Ordered Locus Names:	BSU12810

Organism

Bacillus subtilis (strain 168) [Reference proteome] [HAMAP]

Taxonomic identifier

224308 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus subtilis group › Bacillus subtilis › Bacillus subtilis subsp. subtilis

Protein attributes

Sequence length	297 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 and sporulation.
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	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell wall macromolecule catabolic process Inferred from electronic annotation. Source: InterPro 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 – 44

44

Potential

Chain

45 – 297

253

N-acetylmuramoyl-L-alanine amidase XlyA

PRO_0000006457

Regions

Repeat

161 – 204

44

LysM

Secondary structure

1

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.

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.

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.

.

.

.

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.

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.

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.

.

.

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297

Helix Strand Turn

Details...

Beta strand

4 – 6

3

Beta strand

25 – 30

6

Helix

40 – 47

8

Beta strand

57 – 60

4

Beta strand

65 – 67

3

Beta strand

78 – 80

3

Helix

84 – 87

4

Beta strand

88 – 94

7

Helix

102 – 119

18

Helix

124 – 126

3

Beta strand

127 – 129

3

Helix

130 – 134

5

Turn

140 – 142

3

Helix

143 – 145

3

Helix

146 – 151

6

Sequences

	Sequence		Length	Mass (Da)
	P39800 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: 33DB710059A3EC72	FASTA	297	31,913
	10 20 30 40 50 60 MVNIIQDFIP VGANNRPGYA MTPLYITVHN TANTAVGADA AAHARYLKNP DTTTSWHFTV 70 80 90 100 110 120 DDTEIYQHLP LNENGWHAGD GNGSGNRASI GIEICENADG DFAKATANAQ WLIKTLMAEH 130 140 150 160 170 180 NISLANVVPH KYWSGKECPR KLLDTWDSFK AGIGGGGSQT YVVKQGDTLT SIARAFGVTV 190 200 210 220 230 240 AQLQEWNNIE DPNLIRVGQV LIVSAPSAAE KPELYPLPDG IIQLTTPYTS GEHVFQVQRA 250 260 270 280 290 LAALYFYPDK GAVNNGIDGV YGPKTADAVA RFQSVNGLTA DGIYGPATKE KIAAQLS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Krogh S., Joergensen S.T., Diderichsen B., Devine K.M. Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168 / SO113.
[2]	"Lytic enzymes associated with defective prophages of Bacillus subtilis: sequencing and characterization of the region comprising the N-acetylmuramoyl-L-alanine amidase gene of prophage PBSX." Longchamp P.F., Mauel C., Karamata D. Microbiology 140:1855-1867(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[3]	"Lysis genes of the Bacillus subtilis defective prophage PBSX." Krogh S., Jorgensen S.T., Devine K.M. J. Bacteriol. 180:2110-2117(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[4]	"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.
[5]	"Sequence of the Bacillus subtilis genome between xlyA and ykoR." Devine K.M. Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 195-297. Strain: 168.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Z36941 Genomic DNA. Translation: CAA85403.1.
L25924 Genomic DNA. Translation: AAA22645.1.
Z70177 Genomic DNA. Translation: CAA94049.1.
AL009126 Genomic DNA. Translation: CAB13138.1.
AJ002571 Genomic DNA. Translation: CAA05561.1.

PIR

I39938.

RefSeq

NP_389164.1. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3HMB	X-ray	2.70	A/B/C	1-154	[»]
3RDR	X-ray	2.20	A	1-154	[»]

ProteinModelPortal

P39800.

SMR

P39800. Positions 2-154, 223-295.

ModBase

Search...

Protein-protein interaction databases

STRING

224308.BSU12810.

Proteomic databases

PaxDb

P39800.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

CAB13138; CAB13138; BSU12810.

GeneID

939869.

KEGG

bsu:BSU12810.

PATRIC

18974313. VBIBacSub10457_1349.

Organism-specific databases

GenoList

BSU12810. [Micado]

Phylogenomic databases

eggNOG

COG3409.

HOGENOM

HOG000273688.

KO

K01447.

OMA

WHAGDGN.

ProtClustDB

CLSK887143.

Enzyme and pathway databases

BioCyc

BSUB:BSU12810-MONOMER.

Family and domain databases

Gene3D

1.10.101.10. 1 hit.
3.40.80.10. 1 hit.

InterPro

IPR002502. Amidase_domain.
IPR002477. Peptidoglycan-bd-like.
IPR018392. Peptidoglycan-bd_lysin.
IPR002482. Peptidoglycan-bd_Lysin_subgr.
[Graphical view]

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]

SUPFAM

SSF55846. Amidase_2. 1 hit.
SSF47090. PGBD_like. 1 hit.

ProtoNet

Search...

Entry information

Entry name

XLYA_BACSU

Accession

Primary (citable) accession number: P39800

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	May 1, 2013
This is version 98 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program