⊟Summary[edit | edit source]
- organism: Streptococcus pneumoniae Hungary19A-6
- locus tag: SPH_2087 [new locus tag: SPH_RS10205 ]
- pan locus tag?: PNEUPAN003528000
- symbol: SPH_2087
- pan gene symbol?: lytA
- synonym:
- product: autolysin
⊟Genome View[edit | edit source]
⊟Gene[edit | edit source]
⊟General[edit | edit source]
- type: CDS
- locus tag: SPH_2087 [new locus tag: SPH_RS10205 ]
- symbol: SPH_2087
- product: autolysin
- replicon: chromosome
- strand: -
- coordinates: 1920562..1921335
- length: 774
- essential: unknown
⊟Accession numbers[edit | edit source]
- Location: CP000936 (1920562..1921335) NCBI
- BioCyc: see SPH_RS10205
- MicrobesOnline: 5696908 MicrobesOnline
- PneumoBrowse for strain D39V: SPV_1737 PneumoBrowse
⊟Phenotype[edit | edit source]
Share your knowledge and add information here. [edit]
⊟DNA sequence[edit | edit source]
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721ATGCAGGTAGGACCTGTTGATAATGGTGCCTGGGACGTTGGGGGCGGTTGGAATGCTGAG
ACCTATGCAGCGGTTGAACTGATTGAAAGCCATTCAACTAAAGAAGAGTTCATGACGGAC
TACCGCCTTTATATCGAACTCTTACGCAATCTAGCAGATGAAGCAGGTTTGCCGAAAACG
CTTGATACAGGGAGTTTAGCTGGAATTAAAACGCACGAGTATTGCACGAATAACCAACCA
AACAACCACTCAGACCATGTGGATCCATACCCTTACTTGGCAAAATGGGGCATTAGCCGT
GAGCAGTTTAAGCATGATATTGAGAACGGCTTGACGATTGAAACAGGCTGGCAGAAGAAT
GACACTGGCTACTGGTACGTACATTCAGACGGCTCTTATCCAAAAGACAAGTTTGAGAAA
ATCAATGGCACTTGGTACTACTTTGACAGTTCAGGCTATATGCTTGCAGACCGCTGGAGG
AAGCACACAGACGGCAACTGGTACTGGTTCGACAACTCAGGCGAAATGGCTACAGGCTGG
AAGAAAATCGCTGATAAGTGGTACTATTTCAACGAAGAAGGTGCCATGAAGACAGGCTGG
GTCAAGTACAAGGACACTTGGTACTACTTAGACGCTAAAGAAGGCGCCATGGTATCAAAT
GCCTTTATCCAGTCAGCGGACGGAACAGGCTGGTACTACCTCAAACCAGACGGAACACTG
GCAGACAAGCCAGAATTCACAGTAGAGCCAGATGGCTTGATTACAGTAAAATAA60
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⊟Protein[edit | edit source]
⊟General[edit | edit source]
- locus tag: SPH_2087 [new locus tag: SPH_RS10205 ]
- symbol: SPH_2087
- description: autolysin
- length: 257
- theoretical pI: 4.59912
- theoretical MW: 29649.5
- GRAVY: -0.795331
⊟Function[edit | edit source]
- reaction: EC 3.5.1.28? ExPASyN-acetylmuramoyl-L-alanine amidase Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides
- TIGRFAM: glucan-binding repeat (TIGR04035; HMM-score: 57.5)and 1 moreRegulatory functions Protein interactions exported signaling peptide, YydF/SAG_2028 family (TIGR04077; HMM-score: 8.3)
- TheSEED :
- Cell wall-associated murein hydrolase LytA
- PFAM: Choline_binding (CL0694) Choline_bind_3; Choline-binding repeat (PF19127; HMM-score: 101)Choline_bind_1; Putative cell wall binding repeat (PF01473; HMM-score: 93.2)and 1 moreCholine_bind_2; Choline-binding repeat (PF19085; HMM-score: 25.6)
⊟Structure, modifications & cofactors[edit | edit source]
- domains:
- modifications:
- cofactors:
- effectors:
⊟Localization[edit | edit source]
- PSORTb: Extracellular
- Cytoplasmic Score: 0.01
- Cytoplasmic Membrane Score: 0.09
- Cellwall Score: 0.18
- Extracellular Score: 9.72
- Internal Helices: 0
- DeepLocPro: Extracellular
- Cytoplasmic Score: 0.0585
- Cytoplasmic Membrane Score: 0.0004
- Cell wall & surface Score: 0.0425
- Extracellular Score: 0.8985
- SignalP: no predicted signal peptide
- SP(Sec/SPI): 0.005672
- TAT(Tat/SPI): 0.000221
- LIPO(Sec/SPII): 0.000604
- predicted transmembrane helices (TMHMM): 0
⊟Accession numbers[edit | edit source]
⊟Protein sequence[edit | edit source]
- MQVGPVDNGAWDVGGGWNAETYAAVELIESHSTKEEFMTDYRLYIELLRNLADEAGLPKTLDTGSLAGIKTHEYCTNNQPNNHSDHVDPYPYLAKWGISREQFKHDIENGLTIETGWQKNDTGYWYVHSDGSYPKDKFEKINGTWYYFDSSGYMLADRWRKHTDGNWYWFDNSGEMATGWKKIADKWYYFNEEGAMKTGWVKYKDTWYYLDAKEGAMVSNAFIQSADGTGWYYLKPDGTLADKPEFTVEPDGLITVK
⊟Experimental data[edit | edit source]
- protein localization:
- interaction partners:
⊟Expression & Regulation[edit | edit source]
⊟Operon[edit | edit source]
- MicrobesOnline: no polycistronic organisation predicted
⊟Regulation[edit | edit source]
- regulator:
⊟Transcription[edit | edit source]
- transcription start site:
⊟Expression data[edit | edit source]
- PneumoExpress for strain D39V: SPV_1737 PneumoExpress
⊟Biological Material[edit | edit source]
⊟Mutants[edit | edit source]
⊟Expression vector[edit | edit source]
⊟lacZ fusion[edit | edit source]
⊟GFP fusion[edit | edit source]
⊟two-hybrid system[edit | edit source]
⊟FLAG-tag construct[edit | edit source]
⊟Antibody[edit | edit source]
⊟Other Information[edit | edit source]
You can add further information about the gene and protein here. [edit]
⊟Literature[edit | edit source]
⊟References[edit | edit source]
⊟Relevant publications[edit | edit source]
P García, M Paz González, E García, J L García, R López
The molecular characterization of the first autolytic lysozyme of Streptococcus pneumoniae reveals evolutionary mobile domains.
Mol Microbiol: 1999, 33(1);128-38
[PubMed:10411730] [WorldCat.org] [DOI] (P p)P Balachandran, S K Hollingshead, J C Paton, D E Briles
The autolytic enzyme LytA of Streptococcus pneumoniae is not responsible for releasing pneumolysin.
J Bacteriol: 2001, 183(10);3108-16
[PubMed:11325939] [WorldCat.org] [DOI] (P p)E Díaz, R López, J L García
Role of the major pneumococcal autolysin in the atypical response of a clinical isolate of Streptococcus pneumoniae.
J Bacteriol: 1992, 174(17);5508-15
[PubMed:1355082] [WorldCat.org] [DOI] (P p)Peter Mellroth, Robert Daniels, Alice Eberhardt, Daniel Rönnlund, Hans Blom, Jerker Widengren, Staffan Normark, Birgitta Henriques-Normark
LytA, major autolysin of Streptococcus pneumoniae, requires access to nascent peptidoglycan.
J Biol Chem: 2012, 287(14);11018-29
[PubMed:22334685] [WorldCat.org] [DOI] (I p)J V Höltje, A Tomasz
Specific recognition of choline residues in the cell wall teichoic acid by the N-acetylmuramyl-L-alanine amidase of Pneumococcus.
J Biol Chem: 1975, 250(15);6072-6
[PubMed:238995] [WorldCat.org] (P p)A M Berry, R A Lock, D Hansman, J C Paton
Contribution of autolysin to virulence of Streptococcus pneumoniae.
Infect Immun: 1989, 57(8);2324-30
[PubMed:2568343] [WorldCat.org] [DOI] (P p)J F Garcia-Bustos, A Tomasz
Teichoic acid-containing muropeptides from Streptococcus pneumoniae as substrates for the pneumococcal autolysin.
J Bacteriol: 1987, 169(2);447-53
[PubMed:2879828] [WorldCat.org] [DOI] (P p)A Tomasz, P Moreillon, G Pozzi
Insertional inactivation of the major autolysin gene of Streptococcus pneumoniae.
J Bacteriol: 1988, 170(12);5931-4
[PubMed:2903859] [WorldCat.org] [DOI] (P p)L V Howard, H Gooder
Specificity of the autolysin of Streptococcus (Diplococcus) pneumoniae.
J Bacteriol: 1974, 117(2);796-804
[PubMed:4149515] [WorldCat.org] [DOI] (P p)P Usobiaga, F J Medrano, M Gasset, J L Garciá, J L Saiz, G Rivas, J Laynez, M Menéndez
Structural organization of the major autolysin from Streptococcus pneumoniae.
J Biol Chem: 1996, 271(12);6832-8
[PubMed:8636107] [WorldCat.org] [DOI] (P p)