P06653 (ALYS_STRPN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Autolysin
EC=3.5.1.28

Alternative name(s):
Cell wall hydrolase
Mucopeptide aminohydrolase
Murein hydrolase
N-acetylmuramoyl-L-alanine amidase

Gene names

Name:	lytA
Ordered Locus Names:	SP_1937

Organism

Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) [Complete proteome] [HAMAP]

Taxonomic identifier

170187 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Lactobacillales › Streptococcaceae › Streptococcus › Streptococcus pneumoniae

Protein attributes

Sequence length	318 AA.
Sequence status	Complete.
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. Autolysin strictly depends on the presence of choline-containing cell walls for activity.
Catalytic activity	Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides.
Subcellular location	Secreted Potential.
Domain	The C-terminal domain could be responsible for the substrate recognition.
Sequence similarities	Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family. Contains 6 cell wall-binding repeats.

Ontologies

Keywords
Biological process	Cell wall biogenesis/degradation Competence Sporulation
Cellular component	Secreted
Domain	Repeat
Molecular function	Hydrolase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological_process	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

Chain

1 – 318

318

Autolysin

PRO_0000164408

Regions

Repeat

175 – 194

20

Cell wall-binding 1

Repeat

196 – 215

20

Cell wall-binding 2

Repeat

217 – 237

21

Cell wall-binding 3

Repeat

238 – 257

20

Cell wall-binding 4

Repeat

258 – 277

20

Cell wall-binding 5

Repeat

280 – 301

22

Cell wall-binding 6

Experimental info

Sequence conflict

304

1

K → R Ref.1

Sequence conflict

304

1

K → R Ref.2

Secondary structure

1

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318

Helix Strand Turn

Details...

Beta strand

197 – 202

6

Beta strand

205 – 209

5

Beta strand

218 – 222

5

Beta strand

226 – 232

7

Beta strand

240 – 244

5

Beta strand

247 – 251

5

Beta strand

260 – 264

5

Beta strand

267 – 271

5

Turn

273 – 275

3

Beta strand

281 – 285

5

Beta strand

287 – 290

4

Beta strand

292 – 295

4

Beta strand

299 – 301

3

Helix

304 – 306

3

Beta strand

307 – 309

3

Beta strand

315 – 317

3

Sequences

	Sequence		Length	Mass (Da)
	P06653 [UniParc]. Last modified September 26, 2001. Version 2. Checksum: 3CA7F3CD132FB502	FASTA	318	36,544
	10 20 30 40 50 60 MEINVSKLRT DLPQVGVQPY RQVHAHSTGN PHSTVQNEAD YHWRKDPELG FFSHIVGNGC 70 80 90 100 110 120 IMQVGPVDNG AWDVGGGWNA ETYAAVELIE SHSTKEEFMT DYRLYIELLR NLADEAGLPK 130 140 150 160 170 180 TLDTGSLAGI KTHEYCTNNQ PNNHSDHVDP YPYLAKWGIS REQFKHDIEN GLTIETGWQK 190 200 210 220 230 240 NDTGYWYVHS DGSYPKDKFE KINGTWYYFD SSGYMLADRW RKHTDGNWYW FDNSGEMATG 250 260 270 280 290 300 WKKIADKWYY FNEEGAMKTG WVKYKDTWYY LDAKEGAMVS NAFIQSADGT GWYYLKPDGT 310 LADKPEFTVE PDGLITVK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence and expression of the pneumococcal autolysin gene from its own promoter in Escherichia coli." Garcia P., Garcia J.L., Garcia E., Lopez R. Gene 43:265-272(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	Martin B. Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: R800.
[3]	"Complete genome sequence of a virulent isolate of Streptococcus pneumoniae." Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D., Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J., Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D., Umayam L.A., White O., Salzberg S.L. , Lewis M.R., Radune D., Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L., McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K., Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A., Morrison D.A., Hollingshead S.K., Fraser C.M. Science 293:498-506(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-334 / TIGR4.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M13812 Genomic DNA. Translation: AAA26917.1.
Z34303 Genomic DNA. Translation: CAA84074.1.
AE005672 Genomic DNA. Translation: AAK76005.1.

PIR

A25634.
D95226.
H98090.

RefSeq

NP_346365.1. NC_003028.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GVM	X-ray	2.80	A/B/C/D/E/F	188-318	[»]
1H8G	X-ray	2.40	A/B	224-318	[»]
1HCX	X-ray	2.60	A/B	192-318	[»]
2BML	X-ray	2.60	A/B	193-318	[»]

ProteinModelPortal

P06653.

SMR

P06653. Positions 188-318.

ModBase

Search...

Protein-protein interaction databases

STRING

170187.SP_1937.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAK76005; AAK76005; SP_1937.

GeneID

931994.

KEGG

spn:SP_1937.

PATRIC

19708391. VBIStrPne105772_2017.

Organism-specific databases

CMR

Search...

Phylogenomic databases

eggNOG

COG5263.

HOGENOM

HOG000284833.

KO

K01447.

ProtClustDB

CLSK560258.

Family and domain databases

InterPro

IPR002502. Amidase_domain.
IPR018337. Cell_wall/Cho-bd_repeat.
[Graphical view]

Pfam

PF01510. Amidase_2. 1 hit.
PF01473. CW_binding_1. 5 hits.
[Graphical view]

SMART

SM00644. Ami_2. 1 hit.
[Graphical view]

SUPFAM

SSF55846. Amidase_2. 1 hit.

PROSITE

PS51170. CW. 6 hits.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P06653.

Entry information

Entry name

ALYS_STRPN

Accession

Primary (citable) accession number: P06653

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	September 26, 2001
Last modified:	May 1, 2013
This is version 111 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program