Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Lantibiotic mutacin-1140

Gene

lanA

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

Functioni

Lanthionine-containing peptide antibiotic (lantibiotic) active on Gram-positive bacteria. The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores.

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Antibiotic, Antimicrobial, Bacteriocin, Lantibiotic

Protein family/group databases

TCDBi1.C.20.1.8. the nisin (nisin) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Lantibiotic mutacin-1140
Alternative name(s):
Mutacin III
Gene namesi
Name:lanA
Synonyms:mutA
OrganismiStreptococcus mutans
Taxonomic identifieri1309 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PropeptideiPRO_00000171301 – 411 PublicationAdd BLAST41
PeptideiPRO_000001713142 – 63Lantibiotic mutacin-1140Add BLAST22

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki44 ↔ 48Lanthionine (Ser-Cys)
Modified residuei462,3-didehydroalanine (Ser)1
Cross-linki49 ↔ 52Beta-methyllanthionine (Thr-Cys)
Modified residuei552,3-didehydrobutyrine1
Cross-linki57 ↔ 62Lanthionine (Ser-Cys)
Cross-linki60 ↔ 63S-(2-aminovinyl)-D-cysteine (Ser-Cys)

Post-translational modificationi

Maturation of lantibiotics involves the enzymic conversion of Thr, and Ser into dehydrated AA and the formation of thioether bonds with cysteine. The C-terminal lanthionine undergoes decarboxylation. This is followed by membrane translocation and cleavage of the modified precursor.
The structure of the 2,3-didehydrobutyrine is not discussed in PubMed:11082191.

Keywords - PTMi

D-amino acid, Thioether bond

Miscellaneous databases

PMAP-CutDBO68586.

Family & Domainsi

Sequence similaritiesi

Belongs to the type A lantibiotic family.Curated

Family and domain databases

InterProiIPR006079. Lantibiotic_typ-A_Bacillales.
[Graphical view]
PfamiPF02052. Gallidermin. 1 hit.
[Graphical view]
PRINTSiPR00323. GALLIDERMIN.
TIGRFAMsiTIGR03731. lantibio_gallid. 1 hit.

Sequencei

Sequence statusi: Complete.

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

O68586-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNTQLLEVL GTETFDVQED LFAFDTTDTT IVASNDDPDT RFKSWSLCTP
60
GCARTGSFNS YCC
Length:63
Mass (Da):6,968
Last modified:August 1, 1998 - v1
Checksum:iED9BC73771758489
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF051560 Genomic DNA. Translation: AAC18827.1.
AF154675 Genomic DNA. Translation: AAD56142.1.
RefSeqiWP_002268802.1. NZ_LTAK01000001.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF051560 Genomic DNA. Translation: AAC18827.1.
AF154675 Genomic DNA. Translation: AAD56142.1.
RefSeqiWP_002268802.1. NZ_LTAK01000001.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

TCDBi1.C.20.1.8. the nisin (nisin) family.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

PMAP-CutDBO68586.

Family and domain databases

InterProiIPR006079. Lantibiotic_typ-A_Bacillales.
[Graphical view]
PfamiPF02052. Gallidermin. 1 hit.
[Graphical view]
PRINTSiPR00323. GALLIDERMIN.
TIGRFAMsiTIGR03731. lantibio_gallid. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiLANN_STRMG
AccessioniPrimary (citable) accession number: O68586
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: August 1, 1998
Last modified: July 6, 2016
This is version 55 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

Direct protein sequencing

Documents

  1. 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.