Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P06653

- ALYS_STRPN

UniProt

P06653 - ALYS_STRPN

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
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 2 (26 Sep 2001)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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. establishment of competence for transformation Source: UniProtKB-KW
    2. peptidoglycan catabolic process Source: InterPro
    3. sporulation resulting in formation of a cellular spore Source: UniProtKB-KW

    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-SubCell

    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

    MEINVSKLRT DLPQVGVQPY RQVHAHSTGN PHSTVQNEAD YHWRKDPELG    50
    FFSHIVGNGC IMQVGPVDNG AWDVGGGWNA ETYAAVELIE SHSTKEEFMT 100
    DYRLYIELLR NLADEAGLPK TLDTGSLAGI KTHEYCTNNQ PNNHSDHVDP 150
    YPYLAKWGIS REQFKHDIEN GLTIETGWQK NDTGYWYVHS DGSYPKDKFE 200
    KINGTWYYFD SSGYMLADRW RKHTDGNWYW FDNSGEMATG WKKIADKWYY 250
    FNEEGAMKTG WVKYKDTWYY LDAKEGAMVS NAFIQSADGT GWYYLKPDGT 300
    LADKPEFTVE PDGLITVK 318
    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

    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 1, 2014
    This is version 118 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