Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Thiocillin

Gene

BC_5087

more
Organism
Bacillus cereus (strain ATCC 14579 / DSM 31 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NRRL B-3711)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Has bacteriocidal activity against Gram-positive bacteria, but not against Gram-negative bacteria. Inhibits bacterial protein biosynthesis by acting on the elongation factor Tu (EF-Tu) (By similarity).By similarity

GO - Biological processi

Keywordsi

Molecular functionAntibiotic, Antimicrobial, Bacteriocin

Names & Taxonomyi

Protein namesi
Recommended name:
Thiocillin
Alternative name(s):
Antibiotic YM-266183
Antibiotic YM-266184
Micrococcin P1
Micrococcin P2
Thiocillin I
Thiocillin II
Thiocillin III
Thiocillin IV
Gene namesi
Ordered Locus Names:BC_5087
AND
Ordered Locus Names:BC_5088
AND
Ordered Locus Names:BC_5089
AND
Ordered Locus Names:BC_5090
OrganismiBacillus cereus (strain ATCC 14579 / DSM 31 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NRRL B-3711)
Taxonomic identifieri226900 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
Proteomesi
  • UP000001417 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PropeptideiPRO_00003631651 – 38By similarityAdd BLAST38
PeptideiPRO_000036316639 – 52ThiocillinAdd BLAST14

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki39 ↔ 48Pyridine-2,5-dicarboxylic acid (Ser-Ser) (with C-47)
Cross-linki39 ↔ 47Pyridine-2,5-dicarboxylic acid (Ser-Cys) (with S-48)
Cross-linki39 ↔ 40Thiazole-4-carboxylic acid (Ser-Cys)
Cross-linki42 ↔ 43Thiazole-4-carboxylic acid (Thr-Cys)
Modified residuei42(Z)-2,3-didehydrobutyrine1
Cross-linki44 ↔ 45Thiazole-4-carboxylic acid (Val-Cys)
Modified residuei443-hydroxyvaline; partial1 Publication1
Cross-linki46 ↔ 47Thiazole-4-carboxylic acid (Thr-Cys)
Modified residuei46O-methylthreonine; partial1 Publication1
Cross-linki48 ↔ 49Thiazole-4-carboxylic acid (Ser-Cys)
Cross-linki49 ↔ 50Thiazole-4-carboxylic acid (Cys-Cys)
Modified residuei51(Z)-2,3-didehydrobutyrine1
Modified residuei521-amino-2-propanone; alternate1
Modified residuei52Decarboxylated threonine; alternate1 Publication1

Post-translational modificationi

Maturation of thiazole and oxazole containing antibiotics involves the enzymic condensation of a Cys, Ser or Thr with the alpha-carbonyl of the preceding amino acid to form a thioether or ether bond, then dehydration to form a double bond with the alpha-amino nitrogen. Thiazoline or oxazoline ring are dehydrogenated to form thiazole or oxazole rings.
Maturation of pyridinyl containing antibiotics involves the cross-linking of a Ser and a Cys-Ser pair usually separated by 7 or 8 residues along the peptide chain. The Ser residues are dehydrated to didehydroalanines, then bonded between their beta carbons. The alpha carbonyl of the Cys condenses with alpha carbon of the first Ser to form a pyridinyl ring. The ring may be multiply dehydrogenated to form a pyridine ring with loss of the amino nitrogen of the first Ser.
The 8 possible modification isomers, differing in the presence of modifications at three positions, have been characterized in PubMed:19196969. Val-44 is modified to 3-hydroxyvaline in forms thiocillin I, thiocillin II, YM-266183, and YM-266184. Thr-46 is modified to O-methylthreonine in forms thiocillin II, thiocillin III, thiocillin IV, and YM-266184. Thr-52 is decarboxylated to (R)-1-aminopropan-2-ol in forms micrococcin P1, thiocillin I, thiocillin II, and thiocillin III. Thr-52 is decarboxylated and oxidized to 1-amino-2-propanone in forms micrococcin P2, YM-266183, YM-266184. and thiocillin IV.1 Publication
The structure of 2,3-didehydrobutyrines is not discussed in PubMed:19196969. However, in Fig. 3 the residues are diagrammed as Z-isomers.

Keywords - PTMi

Hydroxylation, Methylation, Thioether bond

Interactioni

Protein-protein interaction databases

STRINGi226900.BC5090.

Family & Domainsi

Sequence similaritiesi

Belongs to the thiocillin family.Curated

Family and domain databases

InterProiView protein in InterPro
IPR023895. Thiopep_bacteriocin_prcur.
TIGRFAMsiTIGR03892. thiopep_precurs. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q812G9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEIKKALNT LEIEDFDAIE MVDVDAMPEN EALEIMGASC TTCVCTCSCC

TT
Length:52
Mass (Da):5,624
Last modified:June 1, 2003 - v1
Checksum:i9F7279622C52DDF0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016877 Genomic DNA. Translation: AAP11956.1.
AE016877 Genomic DNA. Translation: AAP11957.1.
AE016877 Genomic DNA. Translation: AAP11958.1.
AE016877 Genomic DNA. Translation: AAP11959.1.
RefSeqiNP_834755.1. NC_004722.1.
NP_834756.1. NC_004722.1.
NP_834757.1. NC_004722.1.
NP_834758.1. NC_004722.1.
WP_001289699.1. NC_004722.1.

Genome annotation databases

EnsemblBacteriaiAAP11956; AAP11956; BC_5087.
AAP11957; AAP11957; BC_5088.
AAP11958; AAP11958; BC_5089.
AAP11959; AAP11959; BC_5090.
GeneIDi1207428.
1207429.
1207430.
1207431.
KEGGibce:BC5087.
bce:BC5088.
bce:BC5089.
bce:BC5090.
PATRICifig|226900.8.peg.5246.

Similar proteinsi

Entry informationi

Entry nameiTHCL_BACCR
AccessioniPrimary (citable) accession number: Q812G9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: June 1, 2003
Last modified: June 7, 2017
This is version 66 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families