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Protein

Autolysin

Gene

lytA

Organism
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Cell wall biogenesis/degradation, Competence, Sporulation

Enzyme and pathway databases

BRENDAi3.5.1.28. 1960.

Names & Taxonomyi

Protein namesi
Recommended name:
Autolysin (EC:3.5.1.28)
Alternative name(s):
Cell wall hydrolase
Mucopeptide aminohydrolase
Murein hydrolase
N-acetylmuramoyl-L-alanine amidase
Gene namesi
Name:lytA
Ordered Locus Names:SP_1937
OrganismiStreptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Taxonomic identifieri170187 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus
Proteomesi
  • UP000000585 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Chemistry databases

DrugBankiDB03754. Tris.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001644081 – 318AutolysinAdd BLAST318

Proteomic databases

PRIDEiP06653.

Interactioni

Protein-protein interaction databases

STRINGi170187.SpneT_02001462.

Structurei

Secondary structure

1318
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi22 – 27Combined sources6
Helixi35 – 44Combined sources10
Helixi47 – 49Combined sources3
Beta strandi53 – 57Combined sources5
Beta strandi60 – 63Combined sources4
Beta strandi67 – 69Combined sources3
Beta strandi74 – 76Combined sources3
Helixi77 – 81Combined sources5
Beta strandi82 – 88Combined sources7
Helixi95 – 116Combined sources22
Beta strandi125 – 132Combined sources8
Helixi133 – 139Combined sources7
Helixi151 – 156Combined sources6
Helixi161 – 170Combined sources10
Beta strandi177 – 180Combined sources4
Beta strandi185 – 188Combined sources4
Beta strandi197 – 202Combined sources6
Beta strandi205 – 209Combined sources5
Beta strandi218 – 222Combined sources5
Beta strandi228 – 231Combined sources4
Beta strandi240 – 244Combined sources5
Beta strandi247 – 251Combined sources5
Beta strandi260 – 264Combined sources5
Beta strandi267 – 271Combined sources5
Turni273 – 275Combined sources3
Beta strandi281 – 285Combined sources5
Beta strandi287 – 290Combined sources4
Beta strandi292 – 295Combined sources4
Beta strandi299 – 301Combined sources3
Helixi304 – 306Combined sources3
Beta strandi307 – 309Combined sources3
Beta strandi315 – 317Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GVMX-ray2.80A/B/C/D/E/F188-318[»]
1H8GX-ray2.40A/B224-318[»]
1HCXX-ray2.60A/B192-318[»]
2BMLX-ray2.60A/B193-318[»]
4IVVX-ray1.05A1-180[»]
4X36X-ray2.10A1-318[»]
5CTVX-ray1.05A1-180[»]
ProteinModelPortaliP06653.
SMRiP06653.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06653.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati175 – 194Cell wall-binding 1Add BLAST20
Repeati196 – 215Cell wall-binding 2Add BLAST20
Repeati217 – 237Cell wall-binding 3Add BLAST21
Repeati238 – 257Cell wall-binding 4Add BLAST20
Repeati258 – 277Cell wall-binding 5Add BLAST20
Repeati280 – 301Cell wall-binding 6Add BLAST22

Domaini

The C-terminal domain could be responsible for the substrate recognition.

Sequence similaritiesi

Contains 6 cell wall-binding repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG4105WWX. Bacteria.
ENOG41123CS. LUCA.
HOGENOMiHOG000284833.
KOiK01447.

Family and domain databases

CDDicd06583. PGRP. 1 hit.
InterProiIPR002502. Amidase_domain.
IPR018337. Cell_wall/Cho-bd_repeat.
[Graphical view]
PfamiPF01510. Amidase_2. 1 hit.
PF01473. CW_binding_1. 5 hits.
[Graphical view]
SMARTiSM00644. Ami_2. 1 hit.
[Graphical view]
SUPFAMiSSF55846. SSF55846. 1 hit.
PROSITEiPS51170. CW. 6 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P06653-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEINVSKLRT DLPQVGVQPY RQVHAHSTGN PHSTVQNEAD YHWRKDPELG
60 70 80 90 100
FFSHIVGNGC IMQVGPVDNG AWDVGGGWNA ETYAAVELIE SHSTKEEFMT
110 120 130 140 150
DYRLYIELLR NLADEAGLPK TLDTGSLAGI KTHEYCTNNQ PNNHSDHVDP
160 170 180 190 200
YPYLAKWGIS REQFKHDIEN GLTIETGWQK NDTGYWYVHS DGSYPKDKFE
210 220 230 240 250
KINGTWYYFD SSGYMLADRW RKHTDGNWYW FDNSGEMATG WKKIADKWYY
260 270 280 290 300
FNEEGAMKTG WVKYKDTWYY LDAKEGAMVS NAFIQSADGT GWYYLKPDGT
310
LADKPEFTVE PDGLITVK
Length:318
Mass (Da):36,544
Last modified:September 26, 2001 - v2
Checksum:i3CA7F3CD132FB502
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti304K → R in AAA26917 (PubMed:2875013).Curated1
Sequence conflicti304K → R in CAA84074 (Ref. 2) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M13812 Genomic DNA. Translation: AAA26917.1.
Z34303 Genomic DNA. Translation: CAA84074.1.
AE005672 Genomic DNA. Translation: AAK76005.1.
PIRiA25634.
D95226.
H98090.
RefSeqiWP_000405234.1. NZ_AKVY01000001.1.

Genome annotation databases

EnsemblBacteriaiAAK76005; AAK76005; SP_1937.
KEGGispn:SP_1937.
PATRICi19708391. VBIStrPne105772_2017.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M13812 Genomic DNA. Translation: AAA26917.1.
Z34303 Genomic DNA. Translation: CAA84074.1.
AE005672 Genomic DNA. Translation: AAK76005.1.
PIRiA25634.
D95226.
H98090.
RefSeqiWP_000405234.1. NZ_AKVY01000001.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GVMX-ray2.80A/B/C/D/E/F188-318[»]
1H8GX-ray2.40A/B224-318[»]
1HCXX-ray2.60A/B192-318[»]
2BMLX-ray2.60A/B193-318[»]
4IVVX-ray1.05A1-180[»]
4X36X-ray2.10A1-318[»]
5CTVX-ray1.05A1-180[»]
ProteinModelPortaliP06653.
SMRiP06653.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi170187.SpneT_02001462.

Chemistry databases

DrugBankiDB03754. Tris.

Proteomic databases

PRIDEiP06653.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAK76005; AAK76005; SP_1937.
KEGGispn:SP_1937.
PATRICi19708391. VBIStrPne105772_2017.

Phylogenomic databases

eggNOGiENOG4105WWX. Bacteria.
ENOG41123CS. LUCA.
HOGENOMiHOG000284833.
KOiK01447.

Enzyme and pathway databases

BRENDAi3.5.1.28. 1960.

Miscellaneous databases

EvolutionaryTraceiP06653.

Family and domain databases

CDDicd06583. PGRP. 1 hit.
InterProiIPR002502. Amidase_domain.
IPR018337. Cell_wall/Cho-bd_repeat.
[Graphical view]
PfamiPF01510. Amidase_2. 1 hit.
PF01473. CW_binding_1. 5 hits.
[Graphical view]
SMARTiSM00644. Ami_2. 1 hit.
[Graphical view]
SUPFAMiSSF55846. SSF55846. 1 hit.
PROSITEiPS51170. CW. 6 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiALYS_STRPN
AccessioniPrimary (citable) accession number: P06653
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: September 26, 2001
Last modified: November 2, 2016
This is version 132 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.