LANNA_STAWA
ID LANNA_STAWA Reviewed; 57 AA.
AC Q9KWM4;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 60.
DE RecName: Full=Lantibiotic nukacin;
DE AltName: Full=Bacteriocin ISK-1;
DE Flags: Precursor;
GN Name=nukA;
OS Staphylococcus warneri.
OG Plasmid pPI-1.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 31-57, DEHYDRATION
RP AT THR-54, AND LANTHIONINE CROSS-LINKS.
RC STRAIN=ISK-1;
RX PubMed=11193411; DOI=10.1271/bbb.64.2420;
RA Sashihara T., Kimura H., Higuchi T., Adachi A., Matsusaki H., Sonomoto K.,
RA Ishizaki A.;
RT "A novel lantibiotic, nukacin ISK-1, of Staphylococcus warneri ISK-1:
RT cloning of the structural gene and identification of the structure.";
RL Biosci. Biotechnol. Biochem. 64:2420-2428(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ISK-1;
RX PubMed=15322349; DOI=10.1271/bbb.68.1663;
RA Aso Y., Sashihara T., Nagao J., Kanemasa Y., Koga H., Hashimoto T.,
RA Higuchi T., Adachi A., Nomiyama H., Ishizaki A., Nakayama J., Sonomoto K.;
RT "Characterization of a gene cluster of Staphylococcus warneri ISK-1
RT encoding the biosynthesis of and immunity to the lantibiotic, nukacin ISK-
RT 1.";
RL Biosci. Biotechnol. Biochem. 68:1663-1671(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ISK-1;
RX PubMed=15737403; DOI=10.1016/j.plasmid.2004.08.003;
RA Aso Y., Koga H., Sashihara T., Nagao J., Kanemasa Y., Nakayama J.,
RA Sonomoto K.;
RT "Description of complete DNA sequence of two plasmids from the nukacin ISK-
RT 1 producer, Staphylococcus warneri ISK-1.";
RL Plasmid 53:164-178(2005).
RN [4]
RP PROTEIN SEQUENCE OF 31-37, AMINO-ACID COMPOSITION, FUNCTION, SUBCELLULAR
RP LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=ISK-1;
RA Kimura H., Matsusaki H., Sashihara T., Sonomoto K., Ishizaki A.;
RT "Purification and partial identification of bacteriocin ISK-1, a new
RT lantibiotic produced by Pediococcus sp. ISK-1.";
RL Biosci. Biotechnol. Biochem. 62:2341-2345(1998).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RC STRAIN=ISK-1;
RX PubMed=16233732; DOI=10.1263/jbb.98.429;
RA Aso Y., Nagao J., Koga H., Okuda K., Kanemasa Y., Sashihara T.,
RA Nakayama J., Sonomoto K.;
RT "Heterologous expression and functional analysis of the gene cluster for
RT the biosynthesis of and immunity to the lantibiotic, nukacin ISK-1.";
RL J. Biosci. Bioeng. 98:429-436(2004).
RN [6]
RP FUNCTION.
RC STRAIN=ISK-1;
RX PubMed=16957223; DOI=10.1128/aem.00678-06;
RA Asaduzzaman S.M., Nagao J., Aso Y., Nakayama J., Sonomoto K.;
RT "Lysine-oriented charges trigger the membrane binding and activity of
RT nukacin ISK-1.";
RL Appl. Environ. Microbiol. 72:6012-6017(2006).
CC -!- FUNCTION: Lanthionine-containing peptide antibiotic (lantibiotic)
CC active on Gram-positive bacteria, such as Lactobacillus sakei,
CC Leuconostoc mesenteroides and Pediococcus pentosaceus. The bactericidal
CC activity of lantibiotics is based on depolarization of energized
CC bacterial cytoplasmic membranes, initiated by the formation of aqueous
CC transmembrane pores. {ECO:0000269|PubMed:16233732,
CC ECO:0000269|PubMed:16957223, ECO:0000269|Ref.4}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16233732,
CC ECO:0000269|Ref.4}. Note=Through the specific ABC transporter NukT.
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.
CC -!- MASS SPECTROMETRY: Mass=2960.1; Method=FAB;
CC Evidence={ECO:0000269|PubMed:16233732};
CC -!- SIMILARITY: Belongs to the type A lantibiotic family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-7 is the initiator.
CC {ECO:0000305}.
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DR EMBL; AB034941; BAA95674.1; -; Genomic_DNA.
DR EMBL; AB121757; BAC98759.1; -; Genomic_DNA.
DR EMBL; AB125341; BAD01007.1; -; Genomic_DNA.
DR RefSeq; NP_940772.1; NC_005207.3.
DR RefSeq; WP_011152951.1; NZ_VDOJ01000018.1.
DR PDB; 5Z5Q; NMR; -; A=31-57.
DR PDB; 5Z5R; NMR; -; A=31-57.
DR PDBsum; 5Z5Q; -.
DR PDBsum; 5Z5R; -.
DR AlphaFoldDB; Q9KWM4; -.
DR BMRB; Q9KWM4; -.
DR SMR; Q9KWM4; -.
DR TCDB; 1.C.21.1.5; the lacticin 481 (lacticin 481) family.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; IPR007682; Lantibiotic_typ-A_Lactobact.
DR Pfam; PF04604; L_biotic_typeA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic; Antimicrobial; Bacteriocin;
KW Direct protein sequencing; Lantibiotic; Plasmid; Secreted; Thioether bond.
FT PROPEP 1..30
FT /evidence="ECO:0000269|PubMed:11193411, ECO:0000269|Ref.4"
FT /id="PRO_0000307094"
FT PEPTIDE 31..57
FT /note="Lantibiotic nukacin"
FT /id="PRO_0000307095"
FT MOD_RES 54
FT /note="2,3-didehydrobutyrine"
FT /evidence="ECO:0000305|PubMed:11193411"
FT CROSSLNK 39..44
FT /note="Beta-methyllanthionine (Thr-Cys)"
FT /evidence="ECO:0000305|PubMed:11193411"
FT CROSSLNK 41..55
FT /note="Lanthionine (Ser-Cys)"
FT /evidence="ECO:0000305|PubMed:11193411"
FT CROSSLNK 48..56
FT /note="Lanthionine (Ser-Cys)"
FT /evidence="ECO:0000305|PubMed:11193411"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:5Z5Q"
FT TURN 41..43
FT /evidence="ECO:0007829|PDB:5Z5Q"
SQ SEQUENCE 57 AA; 6403 MW; 9BF0046242995426 CRC64;
MENSKVMKDI EVANLLEEVQ EDELNEVLGA KKKSGVIPTV SHDCHMNSFQ FVFTCCS
