THCL_BACCR
ID THCL_BACCR Reviewed; 52 AA.
AC Q812G9;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=Thiocillin;
DE AltName: Full=Antibiotic YM-266183;
DE AltName: Full=Antibiotic YM-266184;
DE AltName: Full=Micrococcin P1;
DE AltName: Full=Micrococcin P2;
DE AltName: Full=Thiocillin I;
DE AltName: Full=Thiocillin II;
DE AltName: Full=Thiocillin III;
DE AltName: Full=Thiocillin IV;
DE Flags: Precursor;
GN OrderedLocusNames=BC_5087;
GN and
GN OrderedLocusNames=BC_5088;
GN and
GN OrderedLocusNames=BC_5089;
GN and
GN OrderedLocusNames=BC_5090;
OS Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=226900;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC / NCTC 2599 / NRRL B-3711;
RX PubMed=12721630; DOI=10.1038/nature01582;
RA Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.;
RT "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT anthracis.";
RL Nature 423:87-91(2003).
RN [2]
RP IDENTIFICATION AS THIOCILLIN.
RA Garavelli J.S.;
RL Unpublished observations (NOV-2008).
RN [3]
RP DEHYDRATION AT THR-42 AND THR-51, HYDROXYLATION AT VAL-44, METHYLATION AT
RP THR-46, AND DECARBOXYLATION AT THR-52.
RX PubMed=19196969; DOI=10.1073/pnas.0900008106;
RA Brown L.C.W., Acker M.G., Clardy J., Walsh C.T., Fischbach M.A.;
RT "Thirteen posttranslational modifications convert a 14-residue peptide into
RT the antibiotic thiocillin.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:2549-2553(2009).
CC -!- FUNCTION: Has bacteriocidal activity against Gram-positive bacteria,
CC but not against Gram-negative bacteria. Inhibits bacterial protein
CC biosynthesis by acting on the elongation factor Tu (EF-Tu) (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- PTM: Maturation of thiazole and oxazole containing antibiotics involves
CC the enzymatic condensation of a Cys, Ser or Thr with the alpha-carbonyl
CC of the preceding amino acid to form a thioether or ether bond, then
CC dehydration to form a double bond with the alpha-amino nitrogen.
CC Thiazoline or oxazoline ring are dehydrogenated to form thiazole or
CC oxazole rings.
CC -!- PTM: Maturation of pyridinyl containing antibiotics involves the cross-
CC linking of a Ser and a Cys-Ser pair usually separated by 7 or 8
CC residues along the peptide chain. The Ser residues are dehydrated to
CC didehydroalanines, then bonded between their beta carbons. The alpha
CC carbonyl of the Cys condenses with alpha carbon of the first Ser to
CC form a pyridinyl ring. The ring may be multiply dehydrogenated to form
CC a pyridine ring with loss of the amino nitrogen of the first Ser.
CC -!- PTM: The 8 possible modification isomers, differing in the presence of
CC modifications at three positions, have been characterized in
CC PubMed:19196969. Val-44 is modified to 3-hydroxyvaline in forms
CC thiocillin I, thiocillin II, YM-266183, and YM-266184. Thr-46 is
CC modified to O-methylthreonine in forms thiocillin II, thiocillin III,
CC thiocillin IV, and YM-266184. Thr-52 is decarboxylated to (R)-1-
CC aminopropan-2-ol in forms micrococcin P1, thiocillin I, thiocillin II,
CC and thiocillin III. Thr-52 is decarboxylated and oxidized to 1-amino-2-
CC propanone in forms micrococcin P2, YM-266183, YM-266184. and thiocillin
CC IV. {ECO:0000269|PubMed:19196969}.
CC -!- PTM: The structure of 2,3-didehydrobutyrines is not discussed in
CC PubMed:19196969. However, in Fig. 3 the residues are diagrammed as Z-
CC isomers.
CC -!- SIMILARITY: Belongs to the thiocillin family. {ECO:0000305}.
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DR EMBL; AE016877; AAP11956.1; -; Genomic_DNA.
DR EMBL; AE016877; AAP11957.1; -; Genomic_DNA.
DR EMBL; AE016877; AAP11958.1; -; Genomic_DNA.
DR EMBL; AE016877; AAP11959.1; -; Genomic_DNA.
DR RefSeq; NP_834755.1; NC_004722.1.
DR RefSeq; NP_834756.1; NC_004722.1.
DR RefSeq; NP_834757.1; NC_004722.1.
DR RefSeq; NP_834758.1; NC_004722.1.
DR RefSeq; WP_001289699.1; NZ_CP034551.1.
DR AlphaFoldDB; Q812G9; -.
DR SMR; Q812G9; -.
DR iPTMnet; Q812G9; -.
DR EnsemblBacteria; AAP11956; AAP11956; BC_5087.
DR EnsemblBacteria; AAP11957; AAP11957; BC_5088.
DR EnsemblBacteria; AAP11958; AAP11958; BC_5089.
DR EnsemblBacteria; AAP11959; AAP11959; BC_5090.
DR KEGG; bce:BC5087; -.
DR KEGG; bce:BC5088; -.
DR KEGG; bce:BC5089; -.
DR KEGG; bce:BC5090; -.
DR PATRIC; fig|226900.8.peg.5246; -.
DR HOGENOM; CLU_3076638_0_0_9; -.
DR Proteomes; UP000001417; 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; IPR023895; Thiopep_bacteriocin_prcur.
DR TIGRFAMs; TIGR03892; thiopep_precurs; 1.
PE 1: Evidence at protein level;
KW Antibiotic; Antimicrobial; Bacteriocin; Hydroxylation; Methylation;
KW Reference proteome; Secreted; Thioether bond.
FT PROPEP 1..38
FT /evidence="ECO:0000250"
FT /id="PRO_0000363165"
FT PEPTIDE 39..52
FT /note="Thiocillin"
FT /id="PRO_0000363166"
FT MOD_RES 42
FT /note="(Z)-2,3-didehydrobutyrine"
FT /evidence="ECO:0000269|PubMed:19196969"
FT MOD_RES 44
FT /note="3-hydroxyvaline (Val); partial"
FT /evidence="ECO:0000269|PubMed:19196969"
FT MOD_RES 46
FT /note="O-methylthreonine; partial"
FT /evidence="ECO:0000269|PubMed:19196969"
FT MOD_RES 51
FT /note="(Z)-2,3-didehydrobutyrine"
FT /evidence="ECO:0000269|PubMed:19196969"
FT MOD_RES 52
FT /note="1-amino-2-propanone; alternate"
FT MOD_RES 52
FT /note="Decarboxylated threonine; alternate"
FT /evidence="ECO:0000269|PubMed:19196969"
FT CROSSLNK 39..48
FT /note="Pyridine-2,5-dicarboxylic acid (Ser-Ser) (with C-
FT 47)"
FT CROSSLNK 39..47
FT /note="Pyridine-2,5-dicarboxylic acid (Ser-Cys) (with S-
FT 48)"
FT CROSSLNK 39..40
FT /note="Thiazole-4-carboxylic acid (Ser-Cys)"
FT CROSSLNK 42..43
FT /note="Thiazole-4-carboxylic acid (Thr-Cys)"
FT CROSSLNK 44..45
FT /note="Thiazole-4-carboxylic acid (Val-Cys)"
FT CROSSLNK 46..47
FT /note="Thiazole-4-carboxylic acid (Thr-Cys)"
FT CROSSLNK 48..49
FT /note="Thiazole-4-carboxylic acid (Ser-Cys)"
FT CROSSLNK 49..50
FT /note="Thiazole-4-carboxylic acid (Cys-Cys)"
SQ SEQUENCE 52 AA; 5624 MW; 9F7279622C52DDF0 CRC64;
MSEIKKALNT LEIEDFDAIE MVDVDAMPEN EALEIMGASC TTCVCTCSCC TT
