SPAS_BACIU
ID SPAS_BACIU Reviewed; 56 AA.
AC P10946;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Lantibiotic subtilin;
DE Flags: Precursor;
GN Name=spaS; Synonyms=sub;
OS Bacillus subtilis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1423;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], DEHYDRATION AT SER-29; THR-42 AND
RP SER-55, AND LANTHIONINE CROSS-LINKS.
RX PubMed=2837490; DOI=10.1016/s0021-9258(19)76571-5;
RA Banerjee S., Hansen J.N.;
RT "Structure and expression of a gene encoding the precursor of subtilin, a
RT small protein antibiotic.";
RL J. Biol. Chem. 263:9508-9514(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 6633 / PCI 219 / NRS 231;
RX PubMed=1735728; DOI=10.1128/jb.174.4.1417-1422.1992;
RA Chung Y.J., Steen M.T., Hansen J.N.;
RT "The subtilin gene of Bacillus subtilis ATCC 6633 is encoded in an operon
RT that contains a homolog of the hemolysin B transport protein.";
RL J. Bacteriol. 174:1417-1422(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 6633 / PCI 219 / NRS 231;
RX PubMed=1539969; DOI=10.1128/aem.58.1.132-142.1992;
RA Klein C., Kaletta C., Schnell N., Entian K.-D.;
RT "Analysis of genes involved in biosynthesis of the lantibiotic subtilin.";
RL Appl. Environ. Microbiol. 58:132-142(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1400221; DOI=10.1128/jb.174.20.6699-6702.1992;
RA Chung Y.J., Hansen J.N.;
RT "Determination of the sequence of spaE and identification of a promoter in
RT the subtilin (spa) operon in Bacillus subtilis.";
RL J. Bacteriol. 174:6699-6702(1992).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8085823; DOI=10.1128/aem.60.8.2793-2801.1994;
RA Klein C., Entian K.-D.;
RT "Genes involved in self-protection against the lantibiotic subtilin
RT produced by Bacillus subtilis ATCC 6633.";
RL Appl. Environ. Microbiol. 60:2793-2801(1994).
RN [6]
RP PROTEIN SEQUENCE OF 25-56.
RX PubMed=4154277;
RA Gross E., Kiltz H.H., Nebelin E.;
RT "Subtilin, VI: the structure of subtilin.";
RL Hoppe-Seyler's Z. Physiol. Chem. 354:810-812(1973).
RN [7]
RP FUNCTION, AND MODE OF ACTION.
RX PubMed=2471644; DOI=10.1111/j.1432-1033.1989.tb14815.x;
RA Schueller F., Benz R., Sahl H.-G.;
RT "The peptide antibiotic subtilin acts by formation of voltage-dependent
RT multi-state pores in bacterial and artificial membranes.";
RL Eur. J. Biochem. 182:181-186(1989).
RN [8]
RP SUCCINYLATION AT TRP-25, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=8471040; DOI=10.1042/bj2910023;
RA Chan W.C., Bycroft B.W., Leyland M.L., Lian L.-Y., Roberts G.C.K.;
RT "A novel post-translational modification of the peptide antibiotic
RT subtilin: isolation and characterization of a natural variant from Bacillus
RT subtilis A.T.C.C. 6633.";
RL Biochem. J. 291:23-27(1993).
RN [9]
RP STRUCTURE BY NMR, AND LANTHIONINE CROSS-LINKS.
RC STRAIN=ATCC 6633 / PCI 219 / NRS 231;
RX PubMed=1547888; DOI=10.1016/0014-5793(92)80163-b;
RA Chan W.C., Bycroft B.W., Leylands M.L., Lian L.-Y., Yang J.C.,
RA Roberts G.C.K.;
RT "Sequence-specific resonance assignment and conformational analysis of
RT subtilin by 2D NMR.";
RL FEBS Lett. 300:56-62(1992).
RN [10]
RP MUTAGENESIS OF SER-29.
RX PubMed=8434932; DOI=10.1128/aem.59.2.648-651.1993;
RA Liu W., Hansen J.N.;
RT "The antimicrobial effect of a structural variant of subtilin against
RT outgrowing Bacillus cereus T spores and vegetative cells occurs by
RT different mechanisms.";
RL Appl. Environ. Microbiol. 59:648-651(1993).
CC -!- FUNCTION: Lanthionine-containing peptide antibiotic (lantibiotic)
CC active on Gram-positive bacteria. The bactericidal activity of
CC lantibiotics is based on depolarization of energized bacterial
CC cytoplasmic membranes, initiated by the formation of aqueous
CC transmembrane pores. {ECO:0000269|PubMed:2471644}.
CC -!- PTM: Maturation of lantibiotics involves the enzymatic conversion of
CC Thr, and Ser into dehydrated AA and the formation of thioether bonds
CC with cysteine. This is followed by membrane translocation and cleavage
CC of the modified precursor. {ECO:0000269|PubMed:2837490}.
CC -!- PTM: Succinylated subtilin is 10-20 times less active than subtilin.
CC The ratio subtilin/succinylated subtilin is about 1:2 after 24 hours
CC growth. {ECO:0000269|PubMed:8471040}.
CC -!- PTM: The 2,3-didehydrobutyrine is determined to be the Z-isomer.
CC {ECO:0000269|PubMed:1547888}.
CC -!- MISCELLANEOUS: Subtilin activity is observed during stationary phase,
CC but not during exponential growth.
CC -!- SIMILARITY: Belongs to the type A lantibiotic family. {ECO:0000305}.
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DR EMBL; J03767; AAA22841.1; -; Genomic_DNA.
DR EMBL; M83944; AAA22772.1; -; Genomic_DNA.
DR EMBL; M86869; AAA22840.1; -; Genomic_DNA.
DR EMBL; M99263; AAA22778.1; -; Genomic_DNA.
DR EMBL; U09819; AAB91589.1; -; Genomic_DNA.
DR PIR; A28112; NIBSSA.
DR RefSeq; WP_003220055.1; NZ_ML241279.1.
DR AlphaFoldDB; P10946; -.
DR SMR; P10946; -.
DR TCDB; 1.C.20.1.5; the nisin (nisin) family.
DR GeneID; 64305136; -.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0005102; F:signaling receptor binding; IEA:UniProtKB-KW.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR InterPro; IPR006079; Lantibiotic_typ-A_Bacillales.
DR Pfam; PF02052; Gallidermin; 1.
DR PRINTS; PR00324; NISIN.
DR TIGRFAMs; TIGR03731; lantibio_gallid; 1.
PE 1: Evidence at protein level;
KW Antibiotic; Antimicrobial; Bacteriocin; Direct protein sequencing;
KW Lantibiotic; Thioether bond.
FT PROPEP 1..24
FT /evidence="ECO:0000269|PubMed:4154277"
FT /id="PRO_0000017142"
FT PEPTIDE 25..56
FT /note="Lantibiotic subtilin"
FT /id="PRO_0000017143"
FT MOD_RES 25
FT /note="N2-succinyltryptophan; partial"
FT /evidence="ECO:0000269|PubMed:8471040"
FT MOD_RES 29
FT /note="2,3-didehydroalanine (Ser)"
FT /evidence="ECO:0000269|PubMed:2837490"
FT MOD_RES 42
FT /note="(Z)-2,3-didehydrobutyrine"
FT /evidence="ECO:0000269|PubMed:2837490"
FT MOD_RES 55
FT /note="2,3-didehydroalanine (Ser)"
FT /evidence="ECO:0000269|PubMed:2837490"
FT CROSSLNK 27..31
FT /note="Lanthionine (Ser-Cys)"
FT /evidence="ECO:0000269|PubMed:1547888,
FT ECO:0000269|PubMed:2837490"
FT CROSSLNK 32..35
FT /note="Beta-methyllanthionine (Thr-Cys)"
FT /evidence="ECO:0000269|PubMed:1547888,
FT ECO:0000269|PubMed:2837490"
FT CROSSLNK 37..43
FT /note="Beta-methyllanthionine (Thr-Cys)"
FT /evidence="ECO:0000269|PubMed:1547888,
FT ECO:0000269|PubMed:2837490"
FT CROSSLNK 47..50
FT /note="Beta-methyllanthionine (Thr-Cys)"
FT /evidence="ECO:0000269|PubMed:1547888,
FT ECO:0000269|PubMed:2837490"
FT CROSSLNK 49..52
FT /note="Beta-methyllanthionine (Thr-Cys)"
FT /evidence="ECO:0000269|PubMed:1547888,
FT ECO:0000269|PubMed:2837490"
FT MUTAGEN 29
FT /note="S->A: Devoid of antimicrobial activity; keeps full
FT lysis capacity."
FT /evidence="ECO:0000269|PubMed:8434932"
SQ SEQUENCE 56 AA; 6218 MW; DA9707FBF8A1EBBA CRC64;
MSKFDDFDLD VVKVSKQDSK ITPQWKSESL CTPGCVTGAL QTCFLQTLTC NCKISK
