SUNA_BACSU
ID SUNA_BACSU Reviewed; 56 AA.
AC P68577; O34781; O64033;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=SPbeta prophage-derived bacteriocin sublancin-168;
DE Flags: Precursor;
GN Name=sunA; Synonyms=yolG; OrderedLocusNames=BSU21480;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 20-37, MASS
RP SPECTROMETRY, AND CHARACTERIZATION OF ANTIBIOTIC ACTIVITY.
RC STRAIN=168 / BR151;
RX PubMed=9722542; DOI=10.1074/jbc.273.36.23134;
RA Paik S.H., Chakicherla A., Hansen J.N.;
RT "Identification and characterization of the structural and transporter
RT genes for, and the chemical and biological properties of, sublancin 168, a
RT novel lantibiotic produced by Bacillus subtilis 168.";
RL J. Biol. Chem. 273:23134-23142(1998).
RN [2]
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 [3]
RP PROTEIN SEQUENCE OF 21-46 AND 49-54, AND GLYCOSYLATION AT CYS-41.
RX PubMed=21251913; DOI=10.1016/j.febslet.2011.01.023;
RA Stepper J., Shastri S., Loo T.S., Preston J.C., Novak P., Man P.,
RA Moore C.H., Havlicek V., Patchett M.L., Norris G.E.;
RT "Cysteine S-glycosylation, a new post-translational modification found in
RT glycopeptide bacteriocins.";
RL FEBS Lett. 585:645-650(2011).
RN [4]
RP PROTEIN SEQUENCE OF 31-51, FUNCTION, SUBCELLULAR LOCATION, MASS
RP SPECTROMETRY, GLYCOSYLATION AT CYS-41, DISULFIDE BONDS, PRELIMINARY
RP STRUCTURE BY NMR, AND MUTAGENESIS OF GLY-40; CYS-41 AND GLY-42.
RC STRAIN=168;
RX PubMed=21196935; DOI=10.1038/nchembio.509;
RA Oman T.J., Boettcher J.M., Wang H., Okalibe X.N., van der Donk W.A.;
RT "Sublancin is not a lantibiotic but an S-linked glycopeptide.";
RL Nat. Chem. Biol. 7:78-80(2011).
RN [5]
RP REQUIREMENT FOR SUNT AND BDBB OR BDBC FOR ANTIBIOTIC PRODUCTION.
RC STRAIN=168;
RX PubMed=11872755; DOI=10.1074/jbc.m201158200;
RA Dorenbos R., Stein T., Kabel J., Bruand C., Bolhuis A., Bron S., Quax W.J.,
RA Van Dijl J.M.;
RT "Thiol-disulfide oxidoreductases are essential for the production of the
RT lantibiotic sublancin 168.";
RL J. Biol. Chem. 277:16682-16688(2002).
RN [6]
RP DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=19047653; DOI=10.1128/aac.01189-08;
RA Dubois J.Y., Kouwen T.R., Schurich A.K., Reis C.R., Ensing H.T., Trip E.N.,
RA Zweers J.C., van Dijl J.M.;
RT "Immunity to the bacteriocin sublancin 168 is determined by the SunI (YolF)
RT protein of Bacillus subtilis.";
RL Antimicrob. Agents Chemother. 53:651-661(2009).
CC -!- FUNCTION: Bacteriocin active against Gram-positive bacteria. Inhibits
CC B.cereus spore outgrowth, after the germination stage, approximately
CC 1000-fold better than it inhibits exponential growth of the same cells.
CC Inhibits B.subtilis strain ATCC 6633. {ECO:0000269|PubMed:21196935}.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21196935}.
CC Note=Extracellular region.
CC -!- PTM: Production of active sublancin-168 requires at least one thiol-
CC disulfide oxidoreductase (BdbB or, in its absence, BdbC). Membrane
CC translocation and cleavage of the precursor are probably performed by
CC SunT.
CC -!- MASS SPECTROMETRY: Mass=3878; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:9722542};
CC -!- MASS SPECTROMETRY: Mass=3875.74; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:21196935};
CC -!- MASS SPECTROMETRY: Mass=3875.7454; Method=Electrospray; Note=Dual
CC Electrospray/MALDI source.; Evidence={ECO:0000269|PubMed:21251913};
CC -!- DISRUPTION PHENOTYPE: Loss of bacteriocin sublancin 168 production, but
CC not resistance to sublancin. {ECO:0000269|PubMed:19047653}.
CC -!- CAUTION: Was originally (PubMed:9722542 and PubMed:11872755) thought to
CC be a lantibiotic but was later shown to be an S-linked glycopeptide.
CC {ECO:0000305|PubMed:21196935}.
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DR EMBL; AF014938; AAC63531.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14066.1; -; Genomic_DNA.
DR RefSeq; NP_390031.1; NC_000964.3.
DR RefSeq; WP_009967544.1; NZ_JNCM01000036.1.
DR PDB; 2MIJ; NMR; -; A=20-56.
DR PDBsum; 2MIJ; -.
DR AlphaFoldDB; P68577; -.
DR BMRB; P68577; -.
DR SMR; P68577; -.
DR STRING; 224308.BSU21480; -.
DR iPTMnet; P68577; -.
DR jPOST; P68577; -.
DR PaxDb; P68577; -.
DR PRIDE; P68577; -.
DR EnsemblBacteria; CAB14066; CAB14066; BSU_21480.
DR GeneID; 939121; -.
DR KEGG; bsu:BSU21480; -.
DR PATRIC; fig|224308.179.peg.2345; -.
DR BioCyc; BSUB:BSU21480-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR InterPro; IPR026479; Glycopep_SunS.
DR Pfam; PF19151; Sublancin; 1.
DR TIGRFAMs; TIGR04196; glycopep_SunS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic; Antimicrobial; Bacteriocin;
KW Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Reference proteome; Secreted.
FT PROPEP 1..19
FT /evidence="ECO:0000269|PubMed:9722542"
FT /id="PRO_0000017144"
FT PEPTIDE 20..56
FT /note="SPbeta prophage-derived bacteriocin sublancin-168"
FT /id="PRO_0000017145"
FT CARBOHYD 41
FT /note="S-linked (Glc) cysteine"
FT /evidence="ECO:0000269|PubMed:21196935,
FT ECO:0000269|PubMed:21251913"
FT DISULFID 26..55
FT /evidence="ECO:0000269|PubMed:21196935"
FT DISULFID 33..48
FT /evidence="ECO:0000269|PubMed:21196935"
FT MUTAGEN 40
FT /note="G->E: No effect on glycosylation."
FT /evidence="ECO:0000269|PubMed:21196935"
FT MUTAGEN 40
FT /note="G->Q: No effect on glycosylation; when associated
FT with A-42."
FT /evidence="ECO:0000269|PubMed:21196935"
FT MUTAGEN 41
FT /note="C->S: Abolishes glycosylation."
FT /evidence="ECO:0000269|PubMed:21196935"
FT MUTAGEN 42
FT /note="G->A: No effect on glycosylation; when associated
FT with Q-40."
FT /evidence="ECO:0000269|PubMed:21196935"
FT MUTAGEN 42
FT /note="G->E,K: No effect on glycosylation."
FT /evidence="ECO:0000269|PubMed:21196935"
FT HELIX 25..32
FT /evidence="ECO:0007829|PDB:2MIJ"
FT TURN 33..35
FT /evidence="ECO:0007829|PDB:2MIJ"
FT TURN 44..46
FT /evidence="ECO:0007829|PDB:2MIJ"
FT HELIX 47..54
FT /evidence="ECO:0007829|PDB:2MIJ"
SQ SEQUENCE 56 AA; 5982 MW; 79EC0BF822F9F4C0 CRC64;
MEKLFKEVKL EELENQKGSG LGKAQCAALW LQCASGGTIG CGGGAVACQN YRQFCR
