SBOA_BACSU
ID SBOA_BACSU Reviewed; 43 AA.
AC O07623;
DT 10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Subtilosin-A;
DE AltName: Full=Antilisterial bacteriocin subtilosin;
DE Flags: Precursor;
GN Name=sboA; Synonyms=sbo; OrderedLocusNames=BSU37350;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 6633 / PCI 219 / NRS 231;
RA Stein T., Duesterhus S., Entian K.-D.;
RT "Subtilosin A biosynthesis is conserved among two different classes of
RT Bacillus subtilis strains.";
RL Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9353933; DOI=10.1099/00221287-143-10-3313;
RA Presecan E., Moszer I., Boursier L., Cruz Ramos H., De La Fuente V.,
RA Hullo M.-F., Lelong C., Schleich S., Sekowska A., Song B.H., Villani G.,
RA Kunst F., Danchin A., Glaser P.;
RT "The Bacillus subtilis genome from gerBC (311 degrees) to licR (334
RT degrees).";
RL Microbiology 143:3313-3328(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP PROTEIN SEQUENCE OF 9-43, FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL
RP STAGE, AND MASS SPECTROMETRY.
RC STRAIN=168;
RX PubMed=3936839; DOI=10.1093/oxfordjournals.jbchem.a135315;
RA Babasaki K., Takao T., Shimonishi Y., Kurahashi K.;
RT "Subtilosin A, a new antibiotic peptide produced by Bacillus subtilis 168:
RT isolation, structural analysis, and biogenesis.";
RL J. Biochem. 98:585-603(1985).
RN [5]
RP FUNCTION.
RC STRAIN=168 / JH642, and 22a;
RX PubMed=10572140; DOI=10.1128/jb.181.23.7346-7355.1999;
RA Zheng G., Yan L.Z., Vederas J.C., Zuber P.;
RT "Genes of the sbo-alb locus of Bacillus subtilis are required for
RT production of the antilisterial bacteriocin subtilosin.";
RL J. Bacteriol. 181:7346-7355(1999).
RN [6]
RP TRANSCRIPTIONAL REGULATION.
RC STRAIN=168 / JH642;
RX PubMed=10809710; DOI=10.1128/jb.182.11.3274-3277.2000;
RA Nakano M.M., Zheng G., Zuber P.;
RT "Dual control of sbo-alb operon expression by the Spo0 and ResDE systems of
RT signal transduction under anaerobic conditions in Bacillus subtilis.";
RL J. Bacteriol. 182:3274-3277(2000).
RN [7]
RP FUNCTION, MASS SPECTROMETRY, AND MUTAGENESIS OF THR-14.
RC STRAIN=168 / JH642;
RX PubMed=19633086; DOI=10.1128/jb.00541-09;
RA Huang T., Geng H., Miyyapuram V.R., Sit C.S., Vederas J.C., Nakano M.M.;
RT "Isolation of a variant of subtilosin A with hemolytic activity.";
RL J. Bacteriol. 191:5690-5696(2009).
RN [8]
RP CROSS-LINKS CYS-PHE AND CYS-THR, AND MUTAGENESIS OF 1-MET--GLU-8; CYS-12;
RP CYS-15; CYS-21; PHE-30; THR-36 AND PHE-39.
RC STRAIN=168;
RX PubMed=22366720; DOI=10.1038/nchembio.798;
RA Fluehe L., Knappe T.A., Gattner M.J., Schaefer A., Burghaus O., Linne U.,
RA Marahiel M.A.;
RT "The radical SAM enzyme AlbA catalyzes thioether bond formation in
RT subtilosin A.";
RL Nat. Chem. Biol. 8:350-357(2012).
RN [9]
RP STRUCTURE BY NMR, AND CROSS-LINKS CYS-PHE AND CYS-THR.
RX PubMed=12696888; DOI=10.1021/ja029654t;
RA Kawulka K., Sprules T., McKay R.T., Mercier P., Diaper C.M., Zuber P.,
RA Vederas J.C.;
RT "Structure of subtilosin A, an antimicrobial peptide from Bacillus subtilis
RT with unusual posttranslational modifications linking cysteine sulfurs to
RT alpha-carbons of phenylalanine and threonine.";
RL J. Am. Chem. Soc. 125:4726-4727(2003).
RN [10]
RP STEREOCHEMISTRY OF D-ALLO-THR-36.
RA Vederas J.C.;
RL Unpublished observations (MAY-2003).
CC -!- FUNCTION: Has bacteriocidal activity against some Gram-positive
CC bacteria such as Listeria, some species of Bacillus and E.faecium
CC (PubMed:10572140, PubMed:19633086, PubMed:3936839). A single mutation
CC (Thr-14-Ile) confers hemolytic activity against rabbit and human blood
CC (PubMed:19633086). {ECO:0000269|PubMed:10572140,
CC ECO:0000269|PubMed:19633086, ECO:0000269|PubMed:3936839}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:3936839}.
CC -!- DEVELOPMENTAL STAGE: The production of subtilosin A begins at the end
CC of vegetative growth and finishes before spore formation.
CC {ECO:0000269|PubMed:3936839}.
CC -!- INDUCTION: Transcription is highly induced by oxygen limitation and is
CC under dual and independent control of Spo0A-AbrB and ResDE.
CC {ECO:0000269|PubMed:10809710}.
CC -!- PTM: This sactipeptide undergoes unique processing steps that include
CC proteolytic cleavage after Glu-8, and covalent linkage of the alpha-
CC amino of Asn-9 with the carboxyl of Gly-43 to form a cyclopeptide
CC (PubMed:12696888, PubMed:22366720). Thioether cross-links are formed
CC between cysteines and the alpha-carbons of other amino acids, Cys-12 to
CC Phe-39, Cys-15 to Thr-36, and Cys-21 to Phe-30 (PubMed:12696888,
CC PubMed:22366720). In forming these cross-links, Thr-36 and Phe-39 are
CC converted to D-amino acids (PubMed:12696888). Propeptide cleavage and
CC cyclopeptide formation only occur after all 3 thioether cross-links are
CC formed (PubMed:22366720). {ECO:0000269|PubMed:12696888,
CC ECO:0000269|PubMed:22366720}.
CC -!- MASS SPECTROMETRY: Mass=3398.9; Method=FAB;
CC Evidence={ECO:0000269|PubMed:3936839};
CC -!- MASS SPECTROMETRY: Mass=3412.5; Method=MALDI; Note=The Thr-14-Ile
CC mutant.; Evidence={ECO:0000269|PubMed:19633086};
CC -!- SIMILARITY: Belongs to the bacteriocin class V family. {ECO:0000305}.
CC -!- CAUTION: PubMed:3936839 sequence does not report residues in positions
CC 30 and 39 probably due to their modification, and reports a cyclic
CC permutation of the peptide sequence. {ECO:0000305}.
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DR EMBL; AJ430547; CAD23198.1; -; Genomic_DNA.
DR EMBL; Z97024; CAB09701.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15763.1; -; Genomic_DNA.
DR PIR; A69704; A69704.
DR RefSeq; NP_391616.1; NC_000964.3.
DR RefSeq; WP_003222002.1; NZ_JNCM01000034.1.
DR PDB; 1PXQ; NMR; -; A=9-43.
DR PDBsum; 1PXQ; -.
DR AlphaFoldDB; O07623; -.
DR BMRB; O07623; -.
DR SMR; O07623; -.
DR STRING; 224308.BSU37350; -.
DR TCDB; 1.C.84.1.1; the subtilosin (subtilosin) family.
DR PaxDb; O07623; -.
DR EnsemblBacteria; CAB15763; CAB15763; BSU_37350.
DR GeneID; 50135688; -.
DR GeneID; 64305512; -.
DR GeneID; 938512; -.
DR KEGG; bsu:BSU37350; -.
DR PATRIC; fig|224308.179.peg.4046; -.
DR BioCyc; BSUB:BSU37350-MON; -.
DR EvolutionaryTrace; O07623; -.
DR PRO; PR:O07623; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR InterPro; IPR021539; Subtilosin_A.
DR Pfam; PF11420; Subtilosin_A; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic; Antimicrobial; Bacteriocin; D-amino acid;
KW Direct protein sequencing; Reference proteome; Secreted; Thioether bond.
FT PROPEP 1..8
FT /evidence="ECO:0000269|PubMed:3936839"
FT /id="PRO_0000002780"
FT PEPTIDE 9..43
FT /note="Subtilosin-A"
FT /evidence="ECO:0000269|PubMed:3936839"
FT /id="PRO_0000002781"
FT CROSSLNK 9..43
FT /note="Cyclopeptide (Asn-Gly)"
FT /evidence="ECO:0000269|PubMed:12696888"
FT CROSSLNK 12..39
FT /note="2-cysteinyl-D-phenylalanine (Cys-Phe)"
FT /evidence="ECO:0000269|PubMed:12696888,
FT ECO:0000269|PubMed:22366720"
FT CROSSLNK 15..36
FT /note="2-cysteinyl-D-allo-threonine (Cys-Thr)"
FT /evidence="ECO:0000269|PubMed:12696888,
FT ECO:0000269|PubMed:22366720"
FT CROSSLNK 21..30
FT /note="2-cysteinyl-L-phenylalanine (Cys-Phe)"
FT /evidence="ECO:0000269|PubMed:12696888,
FT ECO:0000269|PubMed:22366720"
FT MUTAGEN 1..8
FT /note="Missing: No thioether bonds formed."
FT /evidence="ECO:0000269|PubMed:22366720"
FT MUTAGEN 12
FT /note="C->A: In vitro no longer makes the first thioether
FT cross-link, in vivo no cyclopeptide formed."
FT /evidence="ECO:0000269|PubMed:22366720"
FT MUTAGEN 12
FT /note="C->S: In vivo forms 2 thioether cross-links, no
FT cyclopeptide formed."
FT /evidence="ECO:0000269|PubMed:22366720"
FT MUTAGEN 14
FT /note="T->I: In sboA1; protein has acquired hemolytic
FT activity and is more effective against tested Gram-positive
FT bacteria."
FT /evidence="ECO:0000269|PubMed:19633086"
FT MUTAGEN 15
FT /note="C->A: In vitro can no longer make the Cys-thioether
FT cross-link, variable loss of the other 2 thioether cross-
FT links, in vivo no cyclopeptide formed."
FT /evidence="ECO:0000269|PubMed:22366720"
FT MUTAGEN 15
FT /note="C->S: In vivo forms 2 thioether cross-links, no
FT cyclopeptide formed."
FT /evidence="ECO:0000269|PubMed:22366720"
FT MUTAGEN 21
FT /note="C->A: In vitro no longer makes the second thioether
FT cross-link, in vivo no cyclopeptide formed."
FT /evidence="ECO:0000269|PubMed:22366720"
FT MUTAGEN 21
FT /note="C->S: In vivo forms 2 thioether cross-links, no
FT cyclopeptide formed."
FT /evidence="ECO:0000269|PubMed:22366720"
FT MUTAGEN 30
FT /note="F->S: In vivo forms 2 thioether cross-links, no
FT cyclopeptide formed."
FT /evidence="ECO:0000269|PubMed:22366720"
FT MUTAGEN 36
FT /note="T->S: In vivo forms 2 thioether cross-links, no
FT cyclopeptide formed."
FT /evidence="ECO:0000269|PubMed:22366720"
FT MUTAGEN 39
FT /note="F->S: In vivo forms 2 thioether cross-links, no
FT cyclopeptide formed."
FT /evidence="ECO:0000269|PubMed:22366720"
FT MUTAGEN 39
FT /note="F->Y: In vivo forms 3 thioether cross-links, forms
FT the cyclopeptide."
FT /evidence="ECO:0000269|PubMed:22366720"
FT TURN 12..15
FT /evidence="ECO:0007829|PDB:1PXQ"
FT TURN 23..26
FT /evidence="ECO:0007829|PDB:1PXQ"
FT HELIX 37..42
FT /evidence="ECO:0007829|PDB:1PXQ"
SQ SEQUENCE 43 AA; 4325 MW; 055A81DA0D378794 CRC64;
MKKAVIVENK GCATCSIGAA CLVDGPIPDF EIAGATGLFG LWG
