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P25310

- LYSM1_STRGL

UniProt

P25310 - LYSM1_STRGL

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Protein

Lysozyme M1

Gene

acm

Organism
Streptomyces globisporus
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

This enzyme has both lysozyme (acetylmuramidase) and diacetylmuramidase activities.

Catalytic activityi

Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei86 – 861PROSITE-ProRule annotation
Active sitei177 – 1771PROSITE-ProRule annotation

GO - Molecular functioni

  1. lysozyme activity Source: UniProtKB-EC

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
  2. cell wall macromolecule catabolic process Source: InterPro
  3. peptidoglycan catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Protein family/group databases

CAZyiGH25. Glycoside Hydrolase Family 25.

Names & Taxonomyi

Protein namesi
Recommended name:
Lysozyme M1 (EC:3.2.1.17)
Alternative name(s):
1,4-beta-N-acetylmuramidase M1
Gene namesi
Name:acm
OrganismiStreptomyces globisporus
Taxonomic identifieri1908 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Subcellular locationi

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
Propeptidei? – 771 PublicationPRO_0000018517
Signal peptidei1 – ?Sequence Analysis
Chaini78 – 294217Lysozyme M1PRO_0000018518Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi185 ↔ 2241 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiP25310.

Structurei

Secondary structure

1
294
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi81 – 877Combined sources
Helixi89 – 913Combined sources
Helixi96 – 1016Combined sources
Beta strandi106 – 1138Combined sources
Turni114 – 1163Combined sources
Helixi122 – 13110Combined sources
Beta strandi135 – 1417Combined sources
Turni144 – 1463Combined sources
Helixi149 – 15810Combined sources
Beta strandi166 – 1694Combined sources
Beta strandi173 – 1753Combined sources
Beta strandi180 – 1823Combined sources
Turni184 – 1874Combined sources
Helixi190 – 20819Combined sources
Beta strandi213 – 2164Combined sources
Helixi218 – 2258Combined sources
Turni230 – 2345Combined sources
Beta strandi237 – 2404Combined sources
Beta strandi253 – 2553Combined sources
Beta strandi257 – 26711Combined sources
Beta strandi270 – 28112Combined sources
Helixi283 – 2919Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JFXX-ray1.65A78-294[»]
ProteinModelPortaliP25310.
SMRiP25310. Positions 78-294.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP25310.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 25 family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR002053. Glyco_hydro_25.
IPR008270. Glyco_hydro_25_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR018077. Glyco_hydro_fam25_subgr.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF01183. Glyco_hydro_25. 1 hit.
[Graphical view]
SMARTiSM00641. Glyco_25. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS00953. GLYCOSYL_HYDROL_F25. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P25310-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPAYSSLARR GRRPAVVLLG GLVSASLALT LAPTAAAAPL APPPGKDVGP
60 70 80 90 100
GEAYMGVGTR IEQGLGAGPD ERTIGPADTS GVQGIDVSHW QGSINWSSVK
110 120 130 140 150
SAGMSFAYIK ATEGTNYKDD RFSANYTNAY NAGIIRGAYH FARPNASSGT
160 170 180 190 200
AQADYFASNG GGWSRDNRTL PGVLDIEHNP SGAMCYGLST TQMRTWINDF
210 220 230 240 250
HARYKARTTR DVVIYTTASW WNTCTGSWNG MAAKSPFWVA HWGVSAPTVP
260 270 280 290
SGFPTWTFWQ YSATGRVGGV SGDVDRNKFN GSAARLLALA NNTA
Length:294
Mass (Da):31,169
Last modified:May 1, 1992 - v1
Checksum:iD96EFE914FA04997
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M30645 Genomic DNA. Translation: AAA26687.1.
PIRiJQ0529. MUSMM1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M30645 Genomic DNA. Translation: AAA26687.1 .
PIRi JQ0529. MUSMM1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1JFX X-ray 1.65 A 78-294 [» ]
ProteinModelPortali P25310.
SMRi P25310. Positions 78-294.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH25. Glycoside Hydrolase Family 25.

Proteomic databases

PRIDEi P25310.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P25310.

Family and domain databases

Gene3Di 3.20.20.80. 1 hit.
InterProi IPR002053. Glyco_hydro_25.
IPR008270. Glyco_hydro_25_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR018077. Glyco_hydro_fam25_subgr.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
Pfami PF01183. Glyco_hydro_25. 1 hit.
[Graphical view ]
SMARTi SM00641. Glyco_25. 1 hit.
[Graphical view ]
SUPFAMi SSF51445. SSF51445. 1 hit.
PROSITEi PS00953. GLYCOSYL_HYDROL_F25. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Cloning and nucleotide sequence of the N-acetylmuramidase M1-encoding gene from Streptomyces globisporus."
    Lichenstein H.S., Hastings A.E., Langley K.E., Mendiaz E.A., Rohde M.F., Elmore R., Zukowski M.M.
    Gene 88:81-86(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 78-117, DISULFIDE BOND.
    Strain: ATCC 21553 / DSM 40991 / FERM P-596.

Entry informationi

Entry nameiLYSM1_STRGL
AccessioniPrimary (citable) accession number: P25310
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: November 26, 2014
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3