ID   SBOA_CYTFI              Reviewed;          34 AA.
AC   C0HLK6;
DT   31-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT   31-JUL-2019, sequence version 1.
DT   25-MAY-2022, entry version 7.
DE   RecName: Full=Subtilosin-A {ECO:0000305};
OS   Cytobacillus firmus (Bacillus firmus).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Cytobacillus.
OX   NCBI_TaxID=1399;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE.
RA   Manikandan P., Senthilkumar P.K.;
RT   "Studies on purification and molecular characterization of antimicrobial
RT   protein from salt pan halophilic bacteria Bacillus firmus.";
RL   Submitted (MAY-2019) to UniProtKB.
CC   -!- FUNCTION: Has bactericidal activity against some Gram-positive
CC       bacteria. {ECO:0000250|UniProtKB:O07623}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:O07623}.
CC   -!- PTM: Alpha-amino of Asn-1 is covalently linked with the carboxyl of
CC       Gly-34 to form a cyclopeptide (By similarity). Thioether cross-links
CC       are formed between cysteines and the alpha-carbons of other amino
CC       acids, Cys-7 to Thr-28 and Cys-13 to Phe-22 (By similarity). In forming
CC       this cross-link, Thr-28 is converted to D-amino acid (By similarity).
CC       {ECO:0000250|UniProtKB:O07623}.
CC   -!- SIMILARITY: Belongs to the bacteriocin class V family. {ECO:0000305}.
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DR   AlphaFoldDB; C0HLK6; -.
DR   SMR; C0HLK6; -.
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   Antibiotic; Antimicrobial; Bacteriocin; D-amino acid;
KW   Direct protein sequencing; Secreted; Thioether bond.
FT   PEPTIDE         1..34
FT                   /note="Subtilosin-A"
FT                   /id="PRO_0000447649"
FT   CROSSLNK        1..34
FT                   /note="Cyclopeptide (Asn-Gly)"
FT                   /evidence="ECO:0000250|UniProtKB:O07623"
FT   CROSSLNK        7..28
FT                   /note="2-cysteinyl-D-allo-threonine (Cys-Thr)"
FT                   /evidence="ECO:0000250|UniProtKB:O07623"
FT   CROSSLNK        13..22
FT                   /note="2-cysteinyl-L-phenylalanine (Cys-Phe)"
FT                   /evidence="ECO:0000250|UniProtKB:O07623"
SQ   SEQUENCE   34 AA;  3311 MW;  5A985AA119EFB12F CRC64;
     NKGCATCSIG IACLVDGPIP DFECAGATGL GLWG