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Protein

Autolysin

Gene

EF_0799

Organism
Enterococcus faecalis (strain ATCC 700802 / V583)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Hydrolyzes the cell wall of E.faecalis and M.lysodeikticus. May play an important role in cell wall growth and cell separation.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Antimicrobial, Bacteriolytic enzyme, Glycosidase, Hydrolase

Keywords - Biological processi

Cell cycle, Cell division, Cell wall biogenesis/degradation, Septation

Enzyme and pathway databases

BioCyciEFAE226185:GHI1-781-MONOMER.

Protein family/group databases

CAZyiCBM50. Carbohydrate-Binding Module Family 50.
GH73. Glycoside Hydrolase Family 73.

Names & Taxonomyi

Protein namesi
Recommended name:
Autolysin (EC:3.2.1.-)
Alternative name(s):
Beta-glycosidase
Peptidoglycan hydrolase
Gene namesi
Ordered Locus Names:EF_0799
OrganismiEnterococcus faecalis (strain ATCC 700802 / V583)
Taxonomic identifieri226185 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesEnterococcaceaeEnterococcus
Proteomesi
  • UP000001415 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 5353Sequence analysisAdd
BLAST
Chaini54 – 737684AutolysinPRO_0000012115Add
BLAST

Interactioni

Protein-protein interaction databases

IntActiP37710. 2 interactions.
STRINGi226185.EF0799.

Structurei

Secondary structure

1
737
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi429 – 4324Combined sources
Helixi439 – 4468Combined sources
Helixi450 – 4578Combined sources
Beta strandi469 – 4724Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2MKXNMR-A426-475[»]
ProteinModelPortaliP37710.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini361 – 40444LysM 1PROSITE-ProRule annotationAdd
BLAST
Domaini429 – 47244LysM 2PROSITE-ProRule annotationAdd
BLAST
Domaini497 – 54044LysM 3PROSITE-ProRule annotationAdd
BLAST
Domaini565 – 60844LysM 4PROSITE-ProRule annotationAdd
BLAST
Domaini631 – 67444LysM 5PROSITE-ProRule annotationAdd
BLAST
Domaini693 – 73644LysM 6PROSITE-ProRule annotationAdd
BLAST

Domaini

LysM domains are thought to be involved in peptidoglycan binding.

Sequence similaritiesi

Belongs to the glycosyl hydrolase 73 family.Curated
Contains 6 LysM domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiENOG4107X35. Bacteria.
COG1388. LUCA.
COG1705. LUCA.
OMAiYAQVIRK.

Family and domain databases

Gene3Di3.10.350.10. 6 hits.
InterProiIPR018392. LysM_dom.
IPR002901. MGlyc_endo_b_GlcNAc-like_dom.
[Graphical view]
PfamiPF01832. Glucosaminidase. 1 hit.
PF01476. LysM. 6 hits.
[Graphical view]
SMARTiSM00257. LysM. 6 hits.
SM00047. LYZ2. 1 hit.
[Graphical view]
SUPFAMiSSF54106. SSF54106. 6 hits.
PROSITEiPS51782. LYSM. 6 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P37710-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKESMSRIE RRKAQQRKKT PVQWKKSTTL FSSALIVSSV GTPVALLPVT
60 70 80 90 100
AEATEEQPTN AEVAQAPTTE TGLVETPTTE TTPGTTEQPT TDSSTTTEST
110 120 130 140 150
TESSKETPTT PSTEQPTADS TTPVESGTTD SSVAEITPVA PSATESEAAP
160 170 180 190 200
AVTPDDEVKV PEARVASAQT FSALSPTQSP SEFIAELARC AQPIAQANDL
210 220 230 240 250
YASVMMAQAI VESGWGASTL SKAPNYNLFG IKGSYNGQSV YMDTWEYLNG
260 270 280 290 300
KWLVKKEPFR KYPSYMESFQ DNAHVLKTTS FQAGVYYYAG AWKSNTSSYR
310 320 330 340 350
DATAWLTGRY ATDPSYNAKL NNVITAYNLT QYDTPSSGGN TGGGTVNPGT
360 370 380 390 400
GGSNNQSGTN TYYTVKSGDT LNKIAAQYGV SVANLRSWNG ISGDLIFVGQ
410 420 430 440 450
KLIVKKGASG NTGGSGSGGS NNNQSGTNTY YTVKSGDTLN KIAAQYGVSV
460 470 480 490 500
ANLRSWNGIS GDLIFVGQKL IVKKGASGNT GGSNNGGSNN NQSGTNTYYT
510 520 530 540 550
IKSGDTLNKI AAQYGVSVAN LRSWNGISGD LIFAGQKIIV KKGTSGNTGG
560 570 580 590 600
SSNGGSNNNQ SGTNTYYTIK SGDTLNKISA QFGVSVANLQ AWNNISGSLI
610 620 630 640 650
FAGQKIIVKK GANSGSTNTN KPTNNGGGAT TSYTIKSGDT LNKISAQFGV
660 670 680 690 700
SVANLRSWNG IKGDLIFAGQ TIIVKKGASA GGNASSTNSA SGKRHTVKSG
710 720 730
DSLWGLSMQY GISIQKIKQL NGLSGDTIYI GQTLKVG
Length:737
Mass (Da):77,025
Last modified:April 23, 2003 - v2
Checksum:iABB16BD506AC7507
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti85 – 851T → I in AAA67325 (PubMed:1679432).Curated
Sequence conflicti118 – 1181A → V in AAA67325 (PubMed:1679432).Curated
Sequence conflicti143 – 1431A → T in AAA67325 (PubMed:1679432).Curated
Sequence conflicti417 – 4171S → N in AAA67325 (PubMed:1679432).Curated
Sequence conflicti449 – 4491S → T in AAA67325 (PubMed:1679432).Curated
Sequence conflicti476 – 4761A → T in AAA67325 (PubMed:1679432).Curated
Sequence conflicti484 – 4841N → S in AAA67325 (PubMed:1679432).Curated
Sequence conflicti567 – 63266Missing (PubMed:1679432).CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M58002 Genomic DNA. Translation: AAA67325.1.
AE016830 Genomic DNA. Translation: AAO80613.1.
PIRiA38109.
RefSeqiNP_814543.1. NC_004668.1.
WP_010706701.1. NZ_KE136527.1.

Genome annotation databases

EnsemblBacteriaiAAO80613; AAO80613; EF_0799.
GeneIDi1199693.
KEGGiefa:EF0799.
PATRICi21851982. VBIEntFae7065_0740.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M58002 Genomic DNA. Translation: AAA67325.1.
AE016830 Genomic DNA. Translation: AAO80613.1.
PIRiA38109.
RefSeqiNP_814543.1. NC_004668.1.
WP_010706701.1. NZ_KE136527.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2MKXNMR-A426-475[»]
ProteinModelPortaliP37710.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP37710. 2 interactions.
STRINGi226185.EF0799.

Protein family/group databases

CAZyiCBM50. Carbohydrate-Binding Module Family 50.
GH73. Glycoside Hydrolase Family 73.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAO80613; AAO80613; EF_0799.
GeneIDi1199693.
KEGGiefa:EF0799.
PATRICi21851982. VBIEntFae7065_0740.

Phylogenomic databases

eggNOGiENOG4107X35. Bacteria.
COG1388. LUCA.
COG1705. LUCA.
OMAiYAQVIRK.

Enzyme and pathway databases

BioCyciEFAE226185:GHI1-781-MONOMER.

Family and domain databases

Gene3Di3.10.350.10. 6 hits.
InterProiIPR018392. LysM_dom.
IPR002901. MGlyc_endo_b_GlcNAc-like_dom.
[Graphical view]
PfamiPF01832. Glucosaminidase. 1 hit.
PF01476. LysM. 6 hits.
[Graphical view]
SMARTiSM00257. LysM. 6 hits.
SM00047. LYZ2. 1 hit.
[Graphical view]
SUPFAMiSSF54106. SSF54106. 6 hits.
PROSITEiPS51782. LYSM. 6 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiALYS_ENTFA
AccessioniPrimary (citable) accession number: P37710
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: April 23, 2003
Last modified: September 7, 2016
This is version 112 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, Reference proteome

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

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.