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Protein

Lantibiotic mutacin-2

Gene

mutA

Organism
Streptococcus mutans
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Lanthionine-containing peptide antibiotic (lantibiotic) active on Gram-positive bacteria including M.luteus, S.aureus, Streptococcus, P.micros, P.acidilactici, C.sporogenes, C.diphtheriae, A.viscosus, G.vaginalis, P.acnes, L.monocytogenes and M.smegmatis, and Gram-negative bacteria including C.jejuni, H.pylori and N.gonorrhoeae. Transiently and partially depolarizes the transmembrane electrical potential and pH gradient of susceptible cells, inhibits the uptake of amino acids and depletes the intracellular ATP pool.3 Publications

pH dependencei

Stable from pH 2.0 to 4.0. Activity decreases gradually with increasing pH.2 Publications

Temperature dependencei

Thermostable.2 Publications

GO - Molecular functioni

GO - Biological processi

  • amino acid transport Source: UniProtKB
  • cytolysis Source: UniProtKB-KW
  • defense response to Gram-negative bacterium Source: UniProtKB
  • defense response to Gram-positive bacterium Source: UniProtKB
  • regulation of membrane potential Source: UniProtKB

Keywordsi

Molecular functionAntibiotic, Antimicrobial, Bacteriocin, Lantibiotic

Names & Taxonomyi

Protein namesi
Recommended name:
Lantibiotic mutacin-2
Alternative name(s):
Lantibiotic mutacin H-29B
Mutacin II
Gene namesi
Name:mutAImported
OrganismiStreptococcus mutans
Taxonomic identifieri1309 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Subcellular locationi

GO - Cellular componenti

  • extracellular region Source: UniProtKB

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi14E → D: No loss of activity or protein production. 1 Publication1
Mutagenesisi14E → K: Reduced protein production to about 10% of wild-type level. 1 Publication1
Mutagenesisi15V → I or A: No loss of activity or protein production. 1 Publication1
Mutagenesisi15V → L: Reduced protein production to about 50% of wild-type level. 1 Publication1
Mutagenesisi16S → T or A: No loss of activity or protein production. 1 Publication1
Mutagenesisi19E → D: No loss of activity or protein production. 1 Publication1
Mutagenesisi19E → K: Reduced protein production to about 75% of wild-type level. 1 Publication1
Mutagenesisi20L → K: No mature protein is produced. 1 Publication1
Mutagenesisi20L → M: No loss of activity or protein production. 1 Publication1
Mutagenesisi23I → D: No mature protein is produced. 1 Publication1
Mutagenesisi23I → V: No loss of activity or protein production. 1 Publication1
Mutagenesisi25G → A: No mature protein is produced. 1 Publication1
Mutagenesisi26G → A: No mature protein is produced. 1 Publication1
Mutagenesisi27Missing : No protein is secreted. 1 Publication1
Mutagenesisi33V → A: No loss of activity. 1 Publication1
Mutagenesisi35P → A: Low activity, less than 10% of wild-type. 1 Publication1
Mutagenesisi36T → A: Loss of secretion. 1 Publication1
Mutagenesisi36T → S: No loss of activity. 1 Publication1
Mutagenesisi41C → A: Loss of activity. 2 Publications1
Mutagenesisi52C → A: Loss of activity. 2 Publications1
Mutagenesisi53C → A: Low activity, less than 10% of wild-type level. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PropeptideiPRO_00000171281 – 264 PublicationsAdd BLAST26
PeptideiPRO_000001712927 – 53Lantibiotic mutacin-2Add BLAST27

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki36 ↔ 41Beta-methyllanthionine (Thr-Cys)1 Publication
Cross-linki38 ↔ 52Lanthionine (Ser-Cys)1 Publication
Cross-linki45 ↔ 53Lanthionine (Ser-Cys)1 Publication
Modified residuei512,3-didehydrobutyrine1 Publication1

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. This is followed by membrane translocation and cleavage of the modified precursor.Curated
It is not established whether the 2,3-didehydrobutyrine is the E- or Z-isomer (PubMed:10821848, PubMed:16626493, PubMed:9647795, PubMed:8021218 and PubMed:8660519).

Keywords - PTMi

Thioether bond

Miscellaneous databases

PMAP-CutDBiO54329

Interactioni

GO - Molecular functioni

Family & Domainsi

Sequence similaritiesi

Belongs to the type A lantibiotic family.Sequence analysis

Family and domain databases

InterProiView protein in InterPro
IPR007682 Lantibiotic_typ-A_Lactobact
PfamiView protein in Pfam
PF04604 L_biotic_typeA, 1 hit

Sequencei

Sequence statusi: Complete.

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

O54329-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNKLNSNAVV SLNEVSDSEL DTILGGNRWW QGVVPTVSYE CRMNSWQHVF

TCC
Length:53
Mass (Da):6,020
Last modified:June 1, 1998 - v1
Checksum:i6C3788E2C9EC6525
GO

Mass spectrometryi

Molecular mass is 3244.64±1.15 Da from positions 27 - 53. Determined by ESI. 1 Publication
Molecular mass is 3245.4±0.58 Da from positions 27 - 53. Determined by ESI. 1 Publication
Molecular mass is 3246.08±0.1 Da from positions 27 - 53. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U40620 Genomic DNA Translation: AAC38144.1
PIRiJC6526

Similar proteinsi

Entry informationi

Entry nameiLANA_STRMG
AccessioniPrimary (citable) accession number: O54329
Secondary accession number(s): P84110
Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: June 1, 1998
Last modified: November 22, 2017
This is version 53 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health