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STR5_STRTC
ID   STR5_STRTC              Reviewed;         278 AA.
AC   A0A3B1EFQ0;
DT   22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT   05-DEC-2018, sequence version 1.
DT   25-MAY-2022, entry version 10.
DE   RecName: Full=Beta-lactamase-like protein str5 {ECO:0000303|PubMed:30258052};
DE            EC=3.5.-.- {ECO:0000305|PubMed:30258052};
DE   AltName: Full=Strobilurin A biosynthesis cluster protein r5 {ECO:0000303|PubMed:30258052};
GN   Name=str5 {ECO:0000303|PubMed:30258052};
OS   Strobilurus tenacellus.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Physalacriaceae; Strobilurus.
OX   NCBI_TaxID=41251;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND BIOTECHNOLOGY.
RC   STRAIN=CBS 621.79;
RX   PubMed=30258052; DOI=10.1038/s41467-018-06202-4;
RA   Nofiani R., de Mattos-Shipley K., Lebe K.E., Han L.C., Iqbal Z.,
RA   Bailey A.M., Willis C.L., Simpson T.J., Cox R.J.;
RT   "Strobilurin biosynthesis in Basidiomycete fungi.";
RL   Nat. Commun. 9:3940-3940(2018).
RN   [2]
RP   BIOTECHNOLOGY.
RX   PubMed=563391; DOI=10.7164/antibiotics.30.806;
RA   Anke T., Oberwinkler F., Steglich W., Schramm G.;
RT   "The strobilurins--new antifungal antibiotics from the basidiomycete
RT   Strobilurus tenacellus.";
RL   J. Antibiot. 30:806-810(1977).
RN   [3]
RP   BIOTECHNOLOGY.
RX   PubMed=6271595; DOI=10.1016/0014-5793(81)81190-8;
RA   Becker W.F., von Jagow G., Anke T., Steglich W.;
RT   "Oudemansin, strobilurin A, strobilurin B and myxothiazol: new inhibitors
RT   of the bc1 segment of the respiratory chain with an E-beta-methoxyacrylate
RT   system as common structural element.";
RL   FEBS Lett. 132:329-333(1981).
RN   [4]
RP   REVIEW ON BIOTECHNOLOGY.
RX   PubMed=29711574;
RX   DOI=10.1002/(sici)1521-3773(19990517)38:10<1328::aid-anie1328>3.0.co;2-1;
RA   Sauter H., Steglich W., Anke T.;
RT   "Strobilurins: evolution of a new class of active substances.";
RL   Angew. Chem. Int. Ed. 38:1328-1349(1999).
RN   [5]
RP   REVIEW ON BIOTECHNOLOGY.
RX   PubMed=12146165; DOI=10.1002/ps.520;
RA   Bartlett D.W., Clough J.M., Godwin J.R., Hall A.A., Hamer M.,
RA   Parr-Dobrzanski B.;
RT   "The strobilurin fungicides.";
RL   Pest Manag. Sci. 58:649-662(2002).
CC   -!- FUNCTION: Beta-lactamase-like protein; part of the gene cluster that
CC       mediates the biosynthesis of strobilurin A, an antifungal polyketide
CC       that contains a key beta-methoxyacrylate toxophore that targets the
CC       complex III of the mitochondrial electron transport chain
CC       (PubMed:30258052). Strobilurin biosynthesis begins with construction of
CC       benzoyl CoA by step-wise elimination of ammonia from phenylalanine by
CC       the phenylalanine ammonia-lyase str11, oxygenation by str8 and retro-
CC       Claisen reaction to form benzoic acid, which is activated to its CoA
CC       thiolester benzoyl CoA by the dedicated CoA ligase str10
CC       (PubMed:30258052). Benzoyl CoA forms the starter unit for the highly
CC       reducing polyketide synthase stpks1 that produces the polyketide
CC       prestrobilutin A (PubMed:30258052). The FAD-dependent oxygenase str9
CC       then catalyzes the key oxidative rearrangement responsible for the
CC       creation of the beta-methoxyacrylate toxophore (PubMed:30258052). Str9
CC       performs epoxidation of the 2,3 olefin of prestrobilutin A, followed by
CC       Meinwald rearrangement to furnish the aldehyde intermediate (Probable).
CC       Rapid enolization of the aldehyde intermediate would give the beta-
CC       methoxyacrylate skeleton and methylations catalyzed by str2 and str3
CC       complete the synthesis and lead to the peroduction of strobilurin A
CC       (Probable). The short-chain dehydrogenase stl2 and the dehydrogenase
CC       str4 play a role in the shunt pathway leading to the production of
CC       bolineol (PubMed:30258052). The cluster encodes no obvious halogenase
CC       gene that could be involved in production of strobilurin B, nor any
CC       obvious dimethylallyl-transferase that could be involved in the
CC       production of strobilurin G (Probable). It is possible that unknown
CC       proteins encoded in, or near, the cluster (such as str1 or stl1) may
CC       form new classes of halogenases or dimethylally-transferases, or that
CC       the responsible genes are located elsewhere on the genome (Probable).
CC       Similarly, proteins encoded by str5/str6 hydrolases appear to have no
CC       chemical role in the biosynthesis of strobilurin A (Probable). Finally,
CC       no obvious self-resistance gene is found within the cluster (Probable).
CC       {ECO:0000269|PubMed:30258052, ECO:0000305|PubMed:30258052}.
CC   -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000305|PubMed:30258052}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- BIOTECHNOLOGY: The structure of strobilurin A was used for the
CC       development of the major class of beta-methoxyacrylate agricultural
CC       fungicides since its beta-methoxyacrylate toxophore targets the Qo site
CC       of complex III of the mitochondrial electron transport chain and
CC       prevents adenosine triphosphate synthesis (PubMed:563391,
CC       PubMed:6271595). Compounds such as azoxystrobin (Syngenta) and Kresoxim
CC       methyl (BASF) are among the most widely used fungicides worldwide
CC       (PubMed:29711574, PubMed:12146165). This class of antifungals are used
CC       as effective treatments against a broad range of destructive fungal
CC       plant pathogens and make significant contributions to food security
CC       (PubMed:29711574, PubMed:12146165). The strobilurin fungicides are
CC       estimated to have been worth 3.4 billion dollars in 2015 and they make
CC       up 25% of the fungicide market and 6.7% of the total crop protection
CC       market (PubMed:30258052). {ECO:0000269|PubMed:563391,
CC       ECO:0000269|PubMed:6271595, ECO:0000303|PubMed:12146165,
CC       ECO:0000303|PubMed:29711574, ECO:0000303|PubMed:30258052}.
CC   -!- SIMILARITY: Belongs to the beta-lactamase family. {ECO:0000305}.
CC   -!- CAUTION: Str5 and str6 form two genes in S.tenacellus whereas they are
CC       fused in close related species. {ECO:0000305|PubMed:30258052}.
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DR   EMBL; KY070339; ATV82115.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3B1EFQ0; -.
DR   SMR; A0A3B1EFQ0; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.710.10; -; 1.
DR   InterPro; IPR001466; Beta-lactam-related.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   Pfam; PF00144; Beta-lactamase; 1.
DR   SUPFAM; SSF56601; SSF56601; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Hydrolase; Membrane; Transmembrane; Transmembrane helix.
FT   CHAIN           1..278
FT                   /note="Beta-lactamase-like protein str5"
FT                   /id="PRO_0000449342"
FT   TRANSMEM        20..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        112
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   278 AA;  30695 MW;  E7E01ECA725E1C5B CRC64;
     MGSDLTHLEG RPPQRWQWRV FVLAALLSAT FAFFTHTCSS PLPQRCRPYL PNVFNKHSLQ
     HNEPEVRDAL LAVDSFVRQS FHENPEIDGL VAAVVTANGA IYETALGPLK ANETRPEDRG
     AVDRYSIFRL ASGSKLFAML EILILRERGA LQLDDPIAKY LPQFAHKHGG WANEDDIDEG
     PITIRHLASH MSGMTREYPR GNMDHWPHSL EGIGPPPMNG APFPDTLEET VLGISHYPLN
     LPTSTYPVYS NAGMALLGQI AVVANAAAER SQGVDVAR
 
 
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