P29559 (LANZ_LACLL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Lantibiotic nisin-Z

Gene names

Name:

nisZ

Organism

Lactococcus lactis subsp. lactis (Streptococcus lactis)

Taxonomic identifier

1360 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Lactobacillales › Streptococcaceae › Lactococcus › Lactococcus lactis

Protein attributes

Sequence length	57 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.
Post-translational modification	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. The structure of the 2,3-didehydrobutyrine is not discussed in Ref.4. It is probably the Z-isomer by similarity.
Sequence similarities	Belongs to the type A lantibiotic family.

Ontologies

Keywords
Molecular function	Antibiotic Antimicrobial Bacteriocin Lantibiotic
PTM	Thioether bond
Technical term	3D-structure
Gene Ontology (GO)
Biological_process	cytolysis Inferred from electronic annotation. Source: UniProtKB-KW defense response to Gram-positive bacterium Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Propeptide

1 – 23

23

PRO_0000017124

Peptide

24 – 57

34

Lantibiotic nisin-Z

PRO_0000017125

Amino acid modifications

Modified residue

25

1

2,3-didehydrobutyrine

Modified residue

28

1

2,3-didehydroalanine (Ser)

Modified residue

56

1

2,3-didehydroalanine (Ser)

Cross-link

26 ↔ 30

Lanthionine (Ser-Cys)

Cross-link

31 ↔ 34

Beta-methyllanthionine (Thr-Cys)

Cross-link

36 ↔ 42

Beta-methyllanthionine (Thr-Cys)

Cross-link

46 ↔ 49

Beta-methyllanthionine (Thr-Cys)

Cross-link

48 ↔ 51

Beta-methyllanthionine (Thr-Cys)

Natural variations

Natural variant

50

1

N → H in strain: JCM 7638.

Secondary structure

1

.

.

.

.

.

57

Helix Strand Turn

Details...

Helix

32 – 35

4

Turn

38 – 40

3

Sequences

	Sequence		Length	Mass (Da)
	P29559 [UniParc]. Last modified April 1, 1993. Version 1. Checksum: DF5E4428AC70BFEF	FASTA	57	5,940
	10 20 30 40 50 MSTKDFNLDL VSVSKKDSGA SPRITSISLC TPGCKTGALM GCNMKTATCN CSIHVSK

References

[1]	"Identification and characterization of the lantibiotic nisin Z, a natural nisin variant." Mulders J.W.M., Boerrigter I.J., Rollema H.S., Siezen R.J., de Vos W.M. Eur. J. Biochem. 201:581-584(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: NIZO 22186.
[2]	"Genetic evidence that Lactococcus lactis JCM7638 produces a mutated form of nisin." Araya T., Ishibashi N., Shimamura S. J. Gen. Appl. Microbiol. 38:271-278(1992) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: JCM 7638.
[3]	"The codon usage of the nisZ operon in Lactococcus lactis N8 suggests a non-lactococcal origin of the conjugative nisin-sucrose transposon." Immonen T., Ye S., Ra R., Qiao M., Paulin L., Saris P.E.J. DNA Seq. 5:203-218(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: N8.
[4]	"The nisin-lipid II complex reveals a pyrophosphate cage that provides a blueprint for novel antibiotics." Hsu S.T., Breukink E., Tischenko E., Lutters M.A., de Kruijff B., Kaptein R., Bonvin A.M., van Nuland N.A. Nat. Struct. Mol. Biol. 11:963-967(2004) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 24-57, DISULFIDE BONDS.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X61144 Genomic DNA. Translation: CAA43440.1.
D10768 Genomic DNA. Translation: BAA01598.1.
Z18947 Genomic DNA. Translation: CAA79467.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1WCO	NMR	-	N	24-57	[»]

ProteinModelPortal

P29559.

SMR

P29559. Positions 28-56.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR006079. Lan.
IPR000446. Nisin.
[Graphical view]

Pfam

PF02052. Gallidermin. 1 hit.
[Graphical view]

PRINTS

PR00324. NISIN.

TIGRFAMs

TIGR03731. lantibio_gallid. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P29559.

Entry information

Entry name

LANZ_LACLL

Accession

Primary (citable) accession number: P29559

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	April 1, 1993
Last modified:	April 3, 2013
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program