P10946 (SPAS_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Lantibiotic subtilin

Gene names

Name:	spaS
Synonyms:	sub

Organism

Bacillus subtilis

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	56 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. Succinylated subtilin is 10-20 times less active than subtilin. The ratio subtilin/succinylated subtilin is about 1:2 after 24 hours growth. The 2,3-didehydrobutyrine is determined to be the Z-isomer (Ref.9).
Miscellaneous	Subtilin activity is observed during stationary phase, but not during exponential growth.
Sequence similarities	Belongs to the type A lantibiotic family.

Ontologies

Keywords
Molecular function	Antibiotic Antimicrobial Bacteriocin Lantibiotic
PTM	Thioether bond
Technical term	Direct protein sequencing
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
Molecular function	receptor binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Propeptide	1 – 24	24			PRO_0000017142
	Peptide	25 – 56	32	Lantibiotic subtilin Ref.6		PRO_0000017143
Amino acid modifications
	Modified residue	25	1	N2-succinyltryptophan; partial
	Modified residue	29	1	2,3-didehydroalanine (Ser) Ref.1
	Modified residue	42	1	(Z)-2,3-didehydrobutyrine
	Modified residue	55	1	2,3-didehydroalanine (Ser) Ref.1
	Cross-link	27 ↔ 31		Lanthionine (Ser-Cys) Ref.9
	Cross-link	32 ↔ 35		Beta-methyllanthionine (Thr-Cys) Ref.9
	Cross-link	37 ↔ 43		Beta-methyllanthionine (Thr-Cys) Ref.9
	Cross-link	47 ↔ 50		Beta-methyllanthionine (Thr-Cys) Ref.9
	Cross-link	49 ↔ 52		Beta-methyllanthionine (Thr-Cys) Ref.9
Experimental info
	Mutagenesis	29	1	S → A: Devoid of antimicrobial activity; keeps full lysis capacity. Ref.10

Sequences

	Sequence		Length	Mass (Da)
	P10946 [UniParc]. Last modified July 1, 1989. Version 1. Checksum: DA9707FBF8A1EBBA	FASTA	56	6,218
	10 20 30 40 50 MSKFDDFDLD VVKVSKQDSK ITPQWKSESL CTPGCVTGAL QTCFLQTLTC NCKISK

References

[1]	"Structure and expression of a gene encoding the precursor of subtilin, a small protein antibiotic." Banerjee S., Hansen J.N. J. Biol. Chem. 263:9508-9514(1988) [PubMed: 2837490] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The subtilin gene of Bacillus subtilis ATCC 6633 is encoded in an operon that contains a homolog of the hemolysin B transport protein." Chung Y.J., Steen M.T., Hansen J.N. J. Bacteriol. 174:1417-1422(1992) [PubMed: 1735728] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 6633 / PCI 219 / NRS 231.
[3]	"Analysis of genes involved in biosynthesis of the lantibiotic subtilin." Klein C., Kaletta C., Schnell N., Entian K.-D. Appl. Environ. Microbiol. 58:132-142(1992) [PubMed: 1539969] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 6633 / PCI 219 / NRS 231.
[4]	"Determination of the sequence of spaE and identification of a promoter in the subtilin (spa) operon in Bacillus subtilis." Chung Y.J., Hansen J.N. J. Bacteriol. 174:6699-6702(1992) [PubMed: 1400221] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"Genes involved in self-protection against the lantibiotic subtilin produced by Bacillus subtilis ATCC 6633." Klein C., Entian K.-D. Appl. Environ. Microbiol. 60:2793-2801(1994) [PubMed: 8085823] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]	"Subtilin, VI: the structure of subtilin." Gross E., Kiltz H.H., Nebelin E. Hoppe-Seyler's Z. Physiol. Chem. 354:810-812(1973) [PubMed: 4154277] [Abstract] Cited for: PROTEIN SEQUENCE OF 25-56.
[7]	"The peptide antibiotic subtilin acts by formation of voltage-dependent multi-state pores in bacterial and artificial membranes." Schueller F., Benz R., Sahl H.-G. Eur. J. Biochem. 182:181-186(1989) [PubMed: 2471644] [Abstract] Cited for: MODE OF ACTION.
[8]	"A novel post-translational modification of the peptide antibiotic subtilin: isolation and characterization of a natural variant from Bacillus subtilis A.T.C.C. 6633." Chan W.C., Bycroft B.W., Leyland M.L., Lian L.-Y., Roberts G.C.K. Biochem. J. 291:23-27(1993) [PubMed: 8471040] [Abstract] Cited for: SUCCINYLATION AT TRP-25, MASS SPECTROMETRY.
[9]	"Sequence-specific resonance assignment and conformational analysis of subtilin by 2D NMR." Chan W.C., Bycroft B.W., Leylands M.L., Lian L.-Y., Yang J.C., Roberts G.C.K. FEBS Lett. 300:56-62(1992) [PubMed: 1547888] [Abstract] Cited for: STRUCTURE BY NMR. Strain: ATCC 6633 / PCI 219 / NRS 231.
[10]	"The antimicrobial effect of a structural variant of subtilin against outgrowing Bacillus cereus T spores and vegetative cells occurs by different mechanisms." Liu W., Hansen J.N. Appl. Environ. Microbiol. 59:648-651(1993) [PubMed: 8434932] [Abstract] Cited for: MUTAGENESIS OF SER-29.

Cross-references

Sequence databases
EMBL GenBank DDBJ	J03767 Genomic DNA. Translation: AAA22841.1. M83944 Genomic DNA. Translation: AAA22772.1. M86869 Genomic DNA. Translation: AAA22840.1. M99263 Genomic DNA. Translation: AAA22778.1. U09819 Genomic DNA. Translation: AAB91589.1.
PIR	NIBSSA. A28112.
3D structure databases
ProteinModelPortal	P10946.
ModBase	Search...
Protein family/group databases
TCDB	1.C.20.1.5. nisin family.
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...

Entry information

Entry name

SPAS_BACSU

Accession

Primary (citable) accession number: P10946

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	May 3, 2011
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program