Reviewed, UniProtKB/Swiss-Prot O07623 (SBOA_BACSU)

Names and origin

Protein names

Recommended name:
    Subtilosin-A
Alternative name(s):
    Antilisterial bacteriocin subtilosin

Gene names

Name:	sboA
Synonyms:	sbo
Ordered Locus Names:	BSU37350

Organism

Bacillus subtilis [Complete proteome] [HAMAP]

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	43 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	Has bacteriocidal activity against some Gram-positive bacteria such as Listeria, some species of Bacillus and E.faecium. Ref.5
Subcellular location	Secreted.
Developmental stage	The production of subtilosin A begins at the end of vegetative growth and finishes before spore formation.
Induction	Transcription is highly induced by oxygen limitation and is under dual and independent control of spo0A-abrB and resDE.
Post-translational modification	This peptide undergoes unique processing steps that include proteolytic cleavage after Glu-8, and covalent linkage of the alpha-amino of Asn-9 with the carboxyl of Gly-43 to form a cyclopeptide. Thioether cross-links are formed between cysteines and the alpha-carbons of other amino acids, Cys-12 to Phe-39, Cys-15 to Thr-36, and Cys-21 to Phe-30. In forming these cross-links, Thr-36 and Phe-39 are converted to D-amino-acids.
Sequence similarities	Belongs to the bacteriocin class V family.
Caution	Ref.4 sequence does not report residues in positions 30 and 39 probably due to their modification, and reports a cyclic permutation of the peptide sequence.
Mass spectrometry	Molecular mass is 3398.9 Da from positions 9 - 43. Determined by FAB. Ref.4

Ontologies

Keywords
Cellular component	Secreted
Molecular function	Antibiotic Antimicrobial Bacteriocin
PTM	D-amino acid Thioether bond
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	cytolysis Inferred from electronic annotation. Source: UniProtKB-KW defense response to bacterium Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
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 – 8

8

PRO_0000002780

Peptide

9 – 43

35

Subtilosin-A Ref.4

PRO_0000002781

Amino acid modifications

Cross-link

9 ↔ 43

Cyclopeptide (Asn-Gly)

Cross-link

12 ↔ 39

2-cysteinyl-D-phenylalanine (Cys-Phe)

Cross-link

15 ↔ 36

2-cysteinyl-D-allo-threonine (Cys-Thr)

Cross-link

21 ↔ 30

2-cysteinyl-L-phenylalanine (Cys-Phe)

Secondary structure

1

.

.

.

.

.

.

.

43

Helix Strand Turn

Details...

Turn

12 – 15

4

Turn

23 – 26

4

Helix

37 – 42

6

Sequences

	Sequence		Length	Mass (Da)
	O07623-1 [UniParc]. Last modified July 1, 1997. Version 1. Checksum: 055A81DA0D378794	FASTA	43	4,325
	10 20 30 40 MKKAVIVENK GCATCSIGAA CLVDGPIPDF EIAGATGLFG LWG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Subtilosin A biosynthesis is conserved among two different classes of Bacillus subtilis strains." Stein T., Duesterhus S., Entian K.-D. Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 6633 / PCI 219 / NRS 231.
[2]	"The Bacillus subtilis genome from gerBC (311 degrees) to licR (334 degrees)." Presecan E., Moszer I., Boursier L., Cruz Ramos H., De La Fuente V., Hullo M.-F., Lelong C., Schleich S., Sekowska A., Song B.H., Villani G., Kunst F., Danchin A., Glaser P. Microbiology 143:3313-3328(1997) [PubMed: 9353933] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[3]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A. Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[4]	"Subtilosin A, a new antibiotic peptide produced by Bacillus subtilis 168: isolation, structural analysis, and biogenesis." Babasaki K., Takao T., Shimonishi Y., Kurahashi K. J. Biochem. 98:585-603(1985) [PubMed: 3936839] [Abstract] Cited for: PROTEIN SEQUENCE OF 9-43, CHARACTERIZATION, MASS SPECTROMETRY. Strain: 168.
[5]	"Genes of the sbo-alb locus of Bacillus subtilis are required for production of the antilisterial bacteriocin subtilosin." Zheng G., Yan L.Z., Vederas J.C., Zuber P. J. Bacteriol. 181:7346-7355(1999) [PubMed: 10572140] [Abstract] Cited for: FUNCTION. Strain: 168 / JH642 and 22a.
[6]	"Dual control of sbo-alb operon expression by the Spo0 and ResDE systems of signal transduction under anaerobic conditions in Bacillus subtilis." Nakano M.M., Zheng G., Zuber P. J. Bacteriol. 182:3274-3277(2000) [PubMed: 10809710] [Abstract] Cited for: TRANSCRIPTIONAL REGULATION. Strain: 168 / JH642.
[7]	"Structure of subtilosin A, an antimicrobial peptide from Bacillus subtilis with unusual posttranslational modifications linking cysteine sulfurs to alpha-carbons of phenylalanine and threonine." Kawulka K., Sprules T., McKay R.T., Mercier P., Diaper C.M., Zuber P., Vederas J.C. J. Am. Chem. Soc. 125:4726-4727(2003) [PubMed: 12696888] [Abstract] Cited for: STRUCTURE BY NMR, CROSS-LINKS CYS-PHE AND CYS-THR.
[8]	Vederas J.C. Unpublished observations (MAY-2003) Cited for: STEREOCHEMISTRY OF D-ALLO-THR-36.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AJ430547 Genomic DNA. Translation: CAD23198.1.
Z97024 Genomic DNA. Translation: CAB09701.1.
AL009126 Genomic DNA. Translation: CAB15763.1.

PIR

A69704.

RefSeq

NP_391616.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1PXQ	NMR	-	A	9-43	[»]

ModBase

Search...

Protein family/group databases

TCDB

1.C.84.1.1. subtilosin family.

Genome annotation databases

GeneID

938512.

GenomeReviews

Gene locus BSU37350 in contig AL009126_GR.

KEGG

bsu:BSU37350.

Organism-specific databases

SubtiList

BG12671. sboA. [Micado]

CMR

Search...

Family and domain databases

ProtoNet

Search...

Entry information

Entry name

SBOA_BACSU

Accession

Primary (citable) accession number: O07623

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 10, 2003
Last sequence update:	July 1, 1997
Last modified:	November 24, 2009
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)