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Protein

Lantibiotic mersacidin

Gene

mrsA

Organism
Bacillus sp. (strain HIL-Y85/54728)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Kills a number of Gram-positive bacteria. Acts at the level of cell wall biosynthesis by interfering with bacterial peptidoglycan biosynthesis. Specifically inhibits the conversion of the lipid II intermediate into polymeric nascent glycan strands by transglycosylation. May interact with the peptidoglycan precursor rather than with the enzyme.

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Antibiotic, Antimicrobial, Bacteriocin, Lantibiotic

Names & Taxonomyi

Protein namesi
Recommended name:
Lantibiotic mersacidin
Gene namesi
Name:mrsA
OrganismiBacillus sp. (strain HIL-Y85/54728)
Taxonomic identifieri69002 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 4848PRO_0000017150Add
BLAST
Peptidei49 – 6820Lantibiotic mersacidinPRO_0000017151Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki49 ↔ 50Beta-methyllanthionine (Cys-Thr)
Cross-linki52 ↔ 60Beta-methyllanthionine (Thr-Cys)
Cross-linki61 ↔ 66Beta-methyllanthionine (Thr-Cys)
Cross-linki63 ↔ 68S-(2-aminovinyl)-3-methyl-D-cysteine (Thr-Cys)
Modified residuei64 – 6412,3-didehydroalanine (Ser)

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 carboxy-terminal beta-methyllanthionine undergoes decarboxylation. This is followed by membrane translocation and cleavage of the modified precursor.

Keywords - PTMi

D-amino acid, Thioether bond

Miscellaneous databases

PMAP-CutDBP43683.

Structurei

Secondary structure

1
68
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi51 – 533Combined sources
Beta strandi56 – 583Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MQXNMR-A49-67[»]
1MQYNMR-A49-67[»]
1MQZNMR-A49-67[»]
1QOWX-ray1.06A/B/C/D/E/F49-67[»]
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP43683.

Family & Domainsi

Sequence similaritiesi

Belongs to the type B lantibiotic family.Curated

Family and domain databases

InterProiIPR027635. Lantibiotic2_lead_pep_dom.
[Graphical view]
TIGRFAMsiTIGR03898. lanti_MRSA_kill. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P43683-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQEAIIRSW KDPFSRENST QNPAGNPFSE LKEAQMDKLV GAGDMEAACT
60
FTLPGGGGVC TLTSECIC
Length:68
Mass (Da):7,228
Last modified:November 1, 1995 - v1
Checksum:i7718B772AE56A51F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z47559 Genomic DNA. Translation: CAA87640.1.
AJ250862 Genomic DNA. Translation: CAB60258.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z47559 Genomic DNA. Translation: CAA87640.1.
AJ250862 Genomic DNA. Translation: CAB60258.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MQXNMR-A49-67[»]
1MQYNMR-A49-67[»]
1MQZNMR-A49-67[»]
1QOWX-ray1.06A/B/C/D/E/F49-67[»]
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP43683.
PMAP-CutDBP43683.

Family and domain databases

InterProiIPR027635. Lantibiotic2_lead_pep_dom.
[Graphical view]
TIGRFAMsiTIGR03898. lanti_MRSA_kill. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiMRSA_BACSY
AccessioniPrimary (citable) accession number: P43683
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 26, 2014
This is version 59 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

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.