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Rubber oxygenase (EC 1.13.-.-) (Latex clearing protein) (b-type cytochrome Lcp)

 LCP_STRK3               Reviewed;         407 AA.
Q3L8N0;
05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
05-OCT-2010, sequence version 2.
25-OCT-2017, entry version 17.
RecName: Full=Rubber oxygenase {ECO:0000303|PubMed:24907333, ECO:0000303|PubMed:27590810};
EC=1.13.-.- {ECO:0000269|PubMed:24907333, ECO:0000269|PubMed:25819959};
AltName: Full=Latex clearing protein {ECO:0000303|PubMed:18606806, ECO:0000303|PubMed:25819959, ECO:0000303|PubMed:27590810};
AltName: Full=b-type cytochrome Lcp {ECO:0000303|PubMed:25819959};
Flags: Precursor;
Name=lcp {ECO:0000303|PubMed:18606806};
Streptomyces sp. (strain K30).
Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
Streptomyces.
NCBI_TaxID=256642;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-50, IDENTIFICATION OF START
SITE, FUNCTION, SUBCELLULAR LOCATION, EXPORT VIA THE TAT-SYSTEM,
INDUCTION, AND MUTAGENESIS OF MET-1; ARG-6; ARG-7 AND MET-11.
STRAIN=K30;
PubMed=18606806; DOI=10.1128/AEM.01001-08;
Yikmis M., Arenskotter M., Rose K., Lange N., Wernsmann H., Wiefel L.,
Steinbuchel A.;
"Secretion and transcriptional regulation of the latex-clearing
protein, Lcp, by the rubber-degrading bacterium Streptomyces sp.
strain K30.";
Appl. Environ. Microbiol. 74:5373-5382(2008).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 11-407, FUNCTION, AND PATHWAY.
STRAIN=K30;
PubMed=15638519; DOI=10.1021/bm0496110;
Rose K., Tenberge K.B., Steinbuchel A.;
"Identification and characterization of genes from Streptomyces sp.
strain K30 responsible for clear zone formation on natural rubber
latex and poly(cis-1,4-isoprene) rubber degradation.";
Biomacromolecules 6:180-188(2005).
[3]
DISRUPTION PHENOTYPE, FUNCTION, AND PATHWAY.
STRAIN=K30;
PubMed=22950008; DOI=10.1002/mbo3.3;
Yikmis M., Steinbuechel A.;
"Importance of the latex-clearing protein (Lcp) for poly(cis-1,4-
isoprene) rubber cleavage in Streptomyces sp. K30.";
MicrobiologyOpen 1:13-24(2012).
[4]
FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND
BIOPHYSICOCHEMICAL PROPERTIES.
STRAIN=K30;
PubMed=24907333; DOI=10.1128/AEM.01271-14;
Birke J., Jendrossek D.;
"Rubber oxygenase and latex clearing protein cleave rubber to
different products and use different cleavage mechanisms.";
Appl. Environ. Microbiol. 80:5012-5020(2014).
[5]
FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL
PROPERTIES.
STRAIN=K30;
PubMed=25819959; DOI=10.1128/AEM.00275-15;
Birke J., Roether W., Jendrossek D.;
"Latex clearing protein (Lcp) of Streptomyces sp. strain K30 is a b-
type cytochrome and differs from rubber oxygenase A (RoxA) in its
biophysical properties.";
Appl. Environ. Microbiol. 81:3793-3799(2015).
[6]
MUTAGENESIS OF ARG-164; THR-168; ARG-195; HIS-198; ARG-202; HIS-203;
HIS-232; HIS-259; HIS-266 AND ARG-328.
STRAIN=K30;
PubMed=27590810; DOI=10.1128/AEM.02176-16;
Roether W., Austen S., Birke J., Jendrossek D.;
"Cleavage of rubber by the latex clearing protein (Lcp) of
Streptomyces sp. strain K30: molecular insights.";
Appl. Environ. Microbiol. 82:6593-6602(2016).
-!- FUNCTION: Involved in the initial step of rubber degradation
(PubMed:22950008, PubMed:15638519, PubMed:18606806). Catalyzes the
oxidative C-C cleavage of poly(cis-1,4-isoprene) in synthetic as
well as in natural rubber by the addition of oxygen (O2) to the
double bonds, leading to a mixture of oligonucleotide-isoprenoids
with terminal keto and aldehyde groups (endo-type cleavage)
(PubMed:25819959, PubMed:24907333). The cleavage products are of
different lengths, ranging from C20 (four isoprene units) to
higher oligo-isoprenoids (PubMed:24907333). Is not able to cleave
low-molecular-weight substrate analogs with isoprenoid structure
such as squalene (1,4-trans-isoprenoid), carotenoids, or alpha-
tocopherol (PubMed:24907333). {ECO:0000269|PubMed:15638519,
ECO:0000269|PubMed:18606806, ECO:0000269|PubMed:22950008,
ECO:0000269|PubMed:24907333, ECO:0000269|PubMed:25819959}.
-!- COFACTOR:
Name=heme b; Xref=ChEBI:CHEBI:60344;
Evidence={ECO:0000269|PubMed:25819959};
Note=Binds 1 b-type heme group non-covalently per subunit.
{ECO:0000269|PubMed:25819959};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 6-8. {ECO:0000269|PubMed:24907333};
Temperature dependence:
Shows a 3-fold higher specific activity at 37 degrees Celsius
than at 25 degrees Celsius. Has a melting temperature of 61.5
degrees Celsius. {ECO:0000269|PubMed:25819959};
-!- PATHWAY: Biopolymer metabolism. {ECO:0000269|PubMed:15638519,
ECO:0000269|PubMed:22950008}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18606806}.
-!- INDUCTION: Weakly transcribed during growth on glucose. Strongly
induced by poly(cis-1,4-isoprene). {ECO:0000269|PubMed:18606806}.
-!- PTM: Exported by the Tat system. The position of the signal
peptide cleavage has not been experimentally proven.
{ECO:0000269|PubMed:18606806}.
-!- DISRUPTION PHENOTYPE: Cells lacking this gene exhibit reduced
growth in medium containing poly(cis-1,4-isoprene) as the sole
carbon and energy source. Additionally, they show no detectable
Lcp activity on latex overlay agar plates, being unable to form a
clear zone and to produce aldehydes. Complementation with the
wild-type lcp gene restores the wild-type phenotype.
{ECO:0000269|PubMed:22950008}.
-!- SIMILARITY: Belongs to the rubber oxygenase Lcp family.
{ECO:0000305}.
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EMBL; AY387589; AAR25849.1; -; Genomic_DNA.
PDB; 5O1L; X-ray; 1.48 A; A/B=1-407.
PDB; 5O1M; X-ray; 2.20 A; A/B=32-402.
PDBsum; 5O1L; -.
PDBsum; 5O1M; -.
ProteinModelPortal; Q3L8N0; -.
SMR; Q3L8N0; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0020037; F:heme binding; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0016701; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen; IDA:UniProtKB.
GO; GO:0008300; P:isoprenoid catabolic process; IDA:UniProtKB.
InterPro; IPR018713; DUF2236.
InterPro; IPR006311; TAT_signal.
Pfam; PF09995; DUF2236; 1.
PROSITE; PS51318; TAT; 1.
1: Evidence at protein level;
3D-structure; Heme; Iron; Metal-binding; Oxidoreductase; Secreted;
Signal.
SIGNAL 1 30 Tat-type signal. {ECO:0000255|PROSITE-
ProRule:PRU00648}.
CHAIN 31 407 Rubber oxygenase.
/FTId=PRO_0000398168.
METAL 198 198 Iron (heme axial ligand).
{ECO:0000305|PubMed:27590810}.
MUTAGEN 1 1 M->A: Impairs clear zone and aldehyde
formation. {ECO:0000269|PubMed:18606806}.
MUTAGEN 6 6 R->A: Impairs clear zone and aldehyde
formation. {ECO:0000269|PubMed:18606806}.
MUTAGEN 7 7 R->A: Does not impair clear zone and
aldehyde formation.
{ECO:0000269|PubMed:18606806}.
MUTAGEN 11 11 M->A: Does not impair clear zone
formation. {ECO:0000269|PubMed:18606806}.
MUTAGEN 164 164 R->A: Loss of catalytic activity. Still
contains a heme group.
{ECO:0000269|PubMed:27590810}.
MUTAGEN 168 168 T->A: 2% of wild-type catalytic activity.
Still contains a heme group.
{ECO:0000269|PubMed:27590810}.
MUTAGEN 195 195 R->A: Unstable.
{ECO:0000269|PubMed:27590810}.
MUTAGEN 198 198 H->A: Loss of catalytic activity. Loss of
heme binding.
{ECO:0000269|PubMed:27590810}.
MUTAGEN 202 202 R->A: Unstable.
{ECO:0000269|PubMed:27590810}.
MUTAGEN 203 203 H->A: No effect on catalytic activity and
on heme binding.
{ECO:0000269|PubMed:27590810}.
MUTAGEN 232 232 H->A: No effect on catalytic activity and
on heme binding.
{ECO:0000269|PubMed:27590810}.
MUTAGEN 259 259 H->A: No effect on catalytic activity and
on heme binding.
{ECO:0000269|PubMed:27590810}.
MUTAGEN 266 266 H->A: No effect on catalytic activity and
on heme binding.
{ECO:0000269|PubMed:27590810}.
MUTAGEN 328 328 R->A: No effect on catalytic activity and
on heme binding.
{ECO:0000269|PubMed:27590810}.
SEQUENCE 407 AA; 44006 MW; C235E48ED413142C CRC64;
MDGFSRRRML MTGGALGAVG ALGAATRALA RPLWTWSPSA SVAGTGVGVD PEYVWDEEAD
PVLAAVIDRG EVPAVNALLK QWTRNDQALP GGLPGDLREF MEHARRMPSW ADKAALDRGA
QFSKTKGIYV GALYGLGSGL MSTAIPRESR AVYYSKGGAD MKDRIAKTAR LGYDIGDLDA
YLPHGSMIVT AVKTRMVHAA VRHLLPQSPA WSQTSGGQKI PISQADIMVT WHSLATFVMR
KMKQWGVRVN TADAEAYLHV WQVSAHMLGV SDEYIPATWD AANAQSKQVL DPILAHTPEG
EALTEVLLGI VAELDAGLTR PLIGAFSRYT LGGEVGDMIG LAKQPVLERL IATAWPLLVA
FREGLIPLPA VPAVLWTLEE ALRKFVLLFL SEGRRIAIDI PDVNRPS


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