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P06653

- ALYS_STRPN

UniProt

P06653 - ALYS_STRPN

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Protein

Autolysin

Gene

lytA

Organism
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Status
Reviewed - 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

  1. N-acetylmuramoyl-L-alanine amidase activity Source: UniProtKB-EC

GO - Biological processi

  1. cell wall organization Source: UniProtKB-KW
  2. establishment of competence for transformation Source: UniProtKB-KW
  3. peptidoglycan catabolic process Source: InterPro
  4. sporulation resulting in formation of a cellular spore Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Cell wall biogenesis/degradation, Competence, Sporulation

Enzyme and pathway databases

BioCyciSPNE170187:GHGN-1967-MONOMER.

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
ProteomesiUP000000585: Chromosome

Subcellular locationi

Secreted Curated

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 318318AutolysinPRO_0000164408Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi170187.SP_1937.

Structurei

Secondary structure

1
318
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi22 – 276
Helixi35 – 4410
Helixi47 – 493
Beta strandi53 – 575
Beta strandi60 – 634
Beta strandi67 – 693
Beta strandi74 – 763
Helixi77 – 815
Beta strandi82 – 887
Helixi95 – 11622
Beta strandi125 – 1328
Helixi133 – 1397
Helixi151 – 1566
Helixi161 – 17010
Beta strandi197 – 2026
Beta strandi205 – 2095
Beta strandi218 – 2225
Beta strandi226 – 2327
Beta strandi240 – 2445
Beta strandi247 – 2515
Beta strandi260 – 2645
Beta strandi267 – 2715
Turni273 – 2753
Beta strandi281 – 2855
Beta strandi287 – 2904
Beta strandi292 – 2954
Beta strandi299 – 3013
Helixi304 – 3063
Beta strandi307 – 3093
Beta strandi315 – 3173

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP06653.
SMRiP06653. Positions 188-318.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06653.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati175 – 19420Cell wall-binding 1Add
BLAST
Repeati196 – 21520Cell wall-binding 2Add
BLAST
Repeati217 – 23721Cell wall-binding 3Add
BLAST
Repeati238 – 25720Cell wall-binding 4Add
BLAST
Repeati258 – 27720Cell wall-binding 5Add
BLAST
Repeati280 – 30122Cell wall-binding 6Add
BLAST

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

eggNOGiCOG5263.
HOGENOMiHOG000284833.
KOiK01447.
OrthoDBiEOG6FBWV3.

Family and domain databases

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti304 – 3041K → R(PubMed:2875013)Curated
Sequence conflicti304 – 3041K → R1 PublicationCurated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M13812 Genomic DNA. Translation: AAA26917.1.
Z34303 Genomic DNA. Translation: CAA84074.1.
AE005672 Genomic DNA. Translation: AAK76005.1.
PIRiA25634.
D95226.
H98090.
RefSeqiNP_346365.1. NC_003028.3.

Genome annotation databases

EnsemblBacteriaiAAK76005; AAK76005; SP_1937.
GeneIDi931994.
KEGGispn:SP_1937.
PATRICi19708391. VBIStrPne105772_2017.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M13812 Genomic DNA. Translation: AAA26917.1 .
Z34303 Genomic DNA. Translation: CAA84074.1 .
AE005672 Genomic DNA. Translation: AAK76005.1 .
PIRi A25634.
D95226.
H98090.
RefSeqi NP_346365.1. NC_003028.3.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
4IVV X-ray 1.05 A 1-180 [» ]
ProteinModelPortali P06653.
SMRi P06653. Positions 188-318.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 170187.SP_1937.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAK76005 ; AAK76005 ; SP_1937 .
GeneIDi 931994.
KEGGi spn:SP_1937.
PATRICi 19708391. VBIStrPne105772_2017.

Phylogenomic databases

eggNOGi COG5263.
HOGENOMi HOG000284833.
KOi K01447.
OrthoDBi EOG6FBWV3.

Enzyme and pathway databases

BioCyci SPNE170187:GHGN-1967-MONOMER.

Miscellaneous databases

EvolutionaryTracei P06653.

Family and domain databases

InterProi IPR002502. Amidase_domain.
IPR018337. Cell_wall/Cho-bd_repeat.
[Graphical view ]
Pfami PF01510. Amidase_2. 1 hit.
PF01473. CW_binding_1. 5 hits.
[Graphical view ]
SMARTi SM00644. Ami_2. 1 hit.
[Graphical view ]
SUPFAMi SSF55846. SSF55846. 1 hit.
PROSITEi PS51170. CW. 6 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-334 / TIGR4.

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: October 29, 2014
This is version 119 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

External Data

Dasty 3