LCP_STRK3
ID LCP_STRK3 Reviewed; 407 AA.
AC Q3L8N0;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 03-AUG-2022, entry version 29.
DE RecName: Full=Rubber oxygenase {ECO:0000303|PubMed:24907333, ECO:0000303|PubMed:27590810};
DE EC=1.13.-.- {ECO:0000269|PubMed:24907333, ECO:0000269|PubMed:25819959};
DE AltName: Full=Latex clearing protein {ECO:0000303|PubMed:18606806, ECO:0000303|PubMed:25819959, ECO:0000303|PubMed:27590810};
DE AltName: Full=b-type cytochrome Lcp {ECO:0000303|PubMed:25819959};
DE Flags: Precursor;
GN Name=lcp {ECO:0000303|PubMed:18606806};
OS Streptomyces sp. (strain K30).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=256642;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-50, IDENTIFICATION OF START SITE,
RP FUNCTION, SUBCELLULAR LOCATION, EXPORT VIA THE TAT-SYSTEM, INDUCTION, AND
RP MUTAGENESIS OF MET-1; ARG-6; ARG-7 AND MET-11.
RC STRAIN=K30;
RX PubMed=18606806; DOI=10.1128/aem.01001-08;
RA Yikmis M., Arenskotter M., Rose K., Lange N., Wernsmann H., Wiefel L.,
RA Steinbuchel A.;
RT "Secretion and transcriptional regulation of the latex-clearing protein,
RT Lcp, by the rubber-degrading bacterium Streptomyces sp. strain K30.";
RL Appl. Environ. Microbiol. 74:5373-5382(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 11-407, FUNCTION, AND PATHWAY.
RC STRAIN=K30;
RX PubMed=15638519; DOI=10.1021/bm0496110;
RA Rose K., Tenberge K.B., Steinbuchel A.;
RT "Identification and characterization of genes from Streptomyces sp. strain
RT K30 responsible for clear zone formation on natural rubber latex and
RT poly(cis-1,4-isoprene) rubber degradation.";
RL Biomacromolecules 6:180-188(2005).
RN [3]
RP DISRUPTION PHENOTYPE, FUNCTION, AND PATHWAY.
RC STRAIN=K30;
RX PubMed=22950008; DOI=10.1002/mbo3.3;
RA Yikmis M., Steinbuechel A.;
RT "Importance of the latex-clearing protein (Lcp) for poly(cis-1,4-isoprene)
RT rubber cleavage in Streptomyces sp. K30.";
RL MicrobiologyOpen 1:13-24(2012).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC STRAIN=K30;
RX PubMed=24907333; DOI=10.1128/aem.01271-14;
RA Birke J., Jendrossek D.;
RT "Rubber oxygenase and latex clearing protein cleave rubber to different
RT products and use different cleavage mechanisms.";
RL Appl. Environ. Microbiol. 80:5012-5020(2014).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=K30;
RX PubMed=25819959; DOI=10.1128/aem.00275-15;
RA Birke J., Roether W., Jendrossek D.;
RT "Latex clearing protein (Lcp) of Streptomyces sp. strain K30 is a b-type
RT cytochrome and differs from rubber oxygenase A (RoxA) in its biophysical
RT properties.";
RL Appl. Environ. Microbiol. 81:3793-3799(2015).
RN [6]
RP MUTAGENESIS OF ARG-164; THR-168; ARG-195; HIS-198; ARG-202; HIS-203;
RP HIS-232; HIS-259; HIS-266 AND ARG-328.
RC STRAIN=K30;
RX PubMed=27590810; DOI=10.1128/aem.02176-16;
RA Roether W., Austen S., Birke J., Jendrossek D.;
RT "Cleavage of rubber by the latex clearing protein (Lcp) of Streptomyces sp.
RT strain K30: molecular insights.";
RL Appl. Environ. Microbiol. 82:6593-6602(2016).
CC -!- FUNCTION: Involved in the initial step of rubber degradation
CC (PubMed:22950008, PubMed:15638519, PubMed:18606806). Catalyzes the
CC oxidative C-C cleavage of poly(cis-1,4-isoprene) in synthetic as well
CC as in natural rubber by the addition of oxygen (O2) to the double
CC bonds, leading to a mixture of oligonucleotide-isoprenoids with
CC terminal keto and aldehyde groups (endo-type cleavage)
CC (PubMed:25819959, PubMed:24907333). The cleavage products are of
CC different lengths, ranging from C20 (four isoprene units) to higher
CC oligo-isoprenoids (PubMed:24907333). Is not able to cleave low-
CC molecular-weight substrate analogs with isoprenoid structure such as
CC squalene (1,4-trans-isoprenoid), carotenoids, or alpha-tocopherol
CC (PubMed:24907333). {ECO:0000269|PubMed:15638519,
CC ECO:0000269|PubMed:18606806, ECO:0000269|PubMed:22950008,
CC ECO:0000269|PubMed:24907333, ECO:0000269|PubMed:25819959}.
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000269|PubMed:25819959};
CC Note=Binds 1 b-type heme group non-covalently per subunit.
CC {ECO:0000269|PubMed:25819959};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6-8. {ECO:0000269|PubMed:24907333};
CC Temperature dependence:
CC Shows a 3-fold higher specific activity at 37 degrees Celsius than at
CC 25 degrees Celsius. Has a melting temperature of 61.5 degrees
CC Celsius. {ECO:0000269|PubMed:25819959};
CC -!- PATHWAY: Biopolymer metabolism. {ECO:0000269|PubMed:15638519,
CC ECO:0000269|PubMed:22950008}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18606806}.
CC -!- INDUCTION: Weakly transcribed during growth on glucose. Strongly
CC induced by poly(cis-1,4-isoprene). {ECO:0000269|PubMed:18606806}.
CC -!- PTM: Exported by the Tat system. The position of the signal peptide
CC cleavage has not been experimentally proven.
CC {ECO:0000269|PubMed:18606806}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene exhibit reduced growth in
CC medium containing poly(cis-1,4-isoprene) as the sole carbon and energy
CC source. Additionally, they show no detectable Lcp activity on latex
CC overlay agar plates, being unable to form a clear zone and to produce
CC aldehydes. Complementation with the wild-type lcp gene restores the
CC wild-type phenotype. {ECO:0000269|PubMed:22950008}.
CC -!- SIMILARITY: Belongs to the rubber oxygenase Lcp family. {ECO:0000305}.
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DR EMBL; AY387589; AAR25849.1; -; Genomic_DNA.
DR PDB; 5O1L; X-ray; 1.48 A; A/B=1-407.
DR PDB; 5O1M; X-ray; 2.20 A; A/B=32-402.
DR PDBsum; 5O1L; -.
DR PDBsum; 5O1M; -.
DR AlphaFoldDB; Q3L8N0; -.
DR SMR; Q3L8N0; -.
DR KEGG; ag:AAR25849; -.
DR BioCyc; MetaCyc:MON-20301; -.
DR BRENDA; 1.13.11.85; 15404.
DR BRENDA; 1.13.11.87; 15404.
DR BRENDA; 1.13.99.B1; 15404.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0020037; F:heme binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016701; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen; IDA:UniProtKB.
DR GO; GO:0008300; P:isoprenoid catabolic process; IDA:UniProtKB.
DR InterPro; IPR037473; Lcp-like.
DR InterPro; IPR018713; MPAB/Lcp_cat_dom.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR37539; PTHR37539; 1.
DR Pfam; PF09995; MPAB_Lcp_cat; 1.
DR PROSITE; PS51318; TAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Heme; Iron; Metal-binding; Oxidoreductase; Secreted; Signal.
FT SIGNAL 1..30
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT CHAIN 31..407
FT /note="Rubber oxygenase"
FT /id="PRO_0000398168"
FT BINDING 198
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000305|PubMed:27590810"
FT MUTAGEN 1
FT /note="M->A: Impairs clear zone and aldehyde formation."
FT /evidence="ECO:0000269|PubMed:18606806"
FT MUTAGEN 6
FT /note="R->A: Impairs clear zone and aldehyde formation."
FT /evidence="ECO:0000269|PubMed:18606806"
FT MUTAGEN 7
FT /note="R->A: Does not impair clear zone and aldehyde
FT formation."
FT /evidence="ECO:0000269|PubMed:18606806"
FT MUTAGEN 11
FT /note="M->A: Does not impair clear zone formation."
FT /evidence="ECO:0000269|PubMed:18606806"
FT MUTAGEN 164
FT /note="R->A: Loss of catalytic activity. Still contains a
FT heme group."
FT /evidence="ECO:0000269|PubMed:27590810"
FT MUTAGEN 168
FT /note="T->A: 2% of wild-type catalytic activity. Still
FT contains a heme group."
FT /evidence="ECO:0000269|PubMed:27590810"
FT MUTAGEN 195
FT /note="R->A: Unstable."
FT /evidence="ECO:0000269|PubMed:27590810"
FT MUTAGEN 198
FT /note="H->A: Loss of catalytic activity. Loss of heme
FT binding."
FT /evidence="ECO:0000269|PubMed:27590810"
FT MUTAGEN 202
FT /note="R->A: Unstable."
FT /evidence="ECO:0000269|PubMed:27590810"
FT MUTAGEN 203
FT /note="H->A: No effect on catalytic activity and on heme
FT binding."
FT /evidence="ECO:0000269|PubMed:27590810"
FT MUTAGEN 232
FT /note="H->A: No effect on catalytic activity and on heme
FT binding."
FT /evidence="ECO:0000269|PubMed:27590810"
FT MUTAGEN 259
FT /note="H->A: No effect on catalytic activity and on heme
FT binding."
FT /evidence="ECO:0000269|PubMed:27590810"
FT MUTAGEN 266
FT /note="H->A: No effect on catalytic activity and on heme
FT binding."
FT /evidence="ECO:0000269|PubMed:27590810"
FT MUTAGEN 328
FT /note="R->A: No effect on catalytic activity and on heme
FT binding."
FT /evidence="ECO:0000269|PubMed:27590810"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:5O1L"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:5O1L"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:5O1L"
FT HELIX 59..68
FT /evidence="ECO:0007829|PDB:5O1L"
FT HELIX 72..79
FT /evidence="ECO:0007829|PDB:5O1L"
FT HELIX 95..104
FT /evidence="ECO:0007829|PDB:5O1L"
FT HELIX 113..125
FT /evidence="ECO:0007829|PDB:5O1L"
FT HELIX 127..135
FT /evidence="ECO:0007829|PDB:5O1L"
FT HELIX 137..142
FT /evidence="ECO:0007829|PDB:5O1L"
FT HELIX 146..154
FT /evidence="ECO:0007829|PDB:5O1L"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:5O1L"
FT HELIX 161..169
FT /evidence="ECO:0007829|PDB:5O1L"
FT TURN 170..176
FT /evidence="ECO:0007829|PDB:5O1L"
FT TURN 178..181
FT /evidence="ECO:0007829|PDB:5O1L"
FT HELIX 187..204
FT /evidence="ECO:0007829|PDB:5O1L"
FT HELIX 205..207
FT /evidence="ECO:0007829|PDB:5O1L"
FT HELIX 209..214
FT /evidence="ECO:0007829|PDB:5O1L"
FT STRAND 219..222
FT /evidence="ECO:0007829|PDB:5O1L"
FT HELIX 224..244
FT /evidence="ECO:0007829|PDB:5O1L"
FT HELIX 251..267
FT /evidence="ECO:0007829|PDB:5O1L"
FT STRAND 274..278
FT /evidence="ECO:0007829|PDB:5O1L"
FT HELIX 279..289
FT /evidence="ECO:0007829|PDB:5O1L"
FT HELIX 291..293
FT /evidence="ECO:0007829|PDB:5O1L"
FT HELIX 298..313
FT /evidence="ECO:0007829|PDB:5O1L"
FT HELIX 320..331
FT /evidence="ECO:0007829|PDB:5O1L"
FT HELIX 333..339
FT /evidence="ECO:0007829|PDB:5O1L"
FT HELIX 345..362
FT /evidence="ECO:0007829|PDB:5O1L"
FT STRAND 365..367
FT /evidence="ECO:0007829|PDB:5O1M"
FT HELIX 373..393
FT /evidence="ECO:0007829|PDB:5O1L"
SQ 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
