Autolysin - Streptococcus pneumoniae

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P06653 (ALYS_STRPN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 101. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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 [Complete proteome] [HAMAP]

Taxonomic identifier

1313 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Streptococcaceae › Streptococcus

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	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	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

Cell wall-binding 1

Repeat

196 – 215

Cell wall-binding 2

Repeat

217 – 237

Cell wall-binding 3

Repeat

238 – 257

Cell wall-binding 4

Repeat

258 – 277

Cell wall-binding 5

Repeat

280 – 301

Cell wall-binding 6

Experimental info

Sequence conflict

304

K → R Ref.1

Sequence conflict

304

K → R Ref.2

Secondary structure

318

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P06653 [UniParc].

Last modified September 26, 2001. Version 2.
Checksum: 3CA7F3CD132FB502
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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

« Hide

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: 2875013] [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. Fraser C.M. Science 293:498-506(2001) [PubMed: 11463916] [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...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBSTRT00000026683; EBSTRP00000025775; EBSTRG00000026683.

GeneID

931994.

GenomeReviews

Gene locus SP_1937 in contig AE005672_GR.

KEGG

spn:SP_1937.

PATRIC

19708391. VBIStrPne105772_2017.

TIGR

SP_1937.

Phylogenomic databases

GeneTree

EBGT00050000026602.

HOGENOM

HBG702446.

ProtClustDB

CLSK560258.

Enzyme and pathway databases

BioCyc

SPNE170187-1:SP_1937-MONOMER.

Family and domain databases

InterPro

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

K01447.

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...

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:	January 25, 2012
This is version 101 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents