CE1_SORC5
ID CE1_SORC5 Reviewed; 456 AA.
AC A9GMG8;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Multifunctional esterase {ECO:0000305|PubMed:25907516};
DE EC=3.1.1.- {ECO:0000269|PubMed:25907516};
DE AltName: Full=Multiple nucleophilic elbowed esterase {ECO:0000303|PubMed:25907516};
DE Short=MNEE {ECO:0000303|PubMed:25907516};
DE Flags: Precursor;
GN OrderedLocusNames=sce3277 {ECO:0000312|EMBL:CAN93436.1};
OS Sorangium cellulosum (strain So ce56) (Polyangium cellulosum (strain So
OS ce56)).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; Sorangiineae;
OC Polyangiaceae; Sorangium.
OX NCBI_TaxID=448385;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=So ce56;
RX PubMed=17965706; DOI=10.1038/nbt1354;
RA Schneiker S., Perlova O., Kaiser O., Gerth K., Alici A., Altmeyer M.O.,
RA Bartels D., Bekel T., Beyer S., Bode E., Bode H.B., Bolten C.J.,
RA Choudhuri J.V., Doss S., Elnakady Y.A., Frank B., Gaigalat L., Goesmann A.,
RA Groeger C., Gross F., Jelsbak L., Jelsbak L., Kalinowski J., Kegler C.,
RA Knauber T., Konietzny S., Kopp M., Krause L., Krug D., Linke B., Mahmud T.,
RA Martinez-Arias R., McHardy A.C., Merai M., Meyer F., Mormann S.,
RA Munoz-Dorado J., Perez J., Pradella S., Rachid S., Raddatz G., Rosenau F.,
RA Rueckert C., Sasse F., Scharfe M., Schuster S.C., Suen G.,
RA Treuner-Lange A., Velicer G.J., Vorholter F.-J., Weissman K.J., Welch R.D.,
RA Wenzel S.C., Whitworth D.E., Wilhelm S., Wittmann C., Bloecker H.,
RA Puehler A., Mueller R.;
RT "Complete genome sequence of the myxobacterium Sorangium cellulosum.";
RL Nat. Biotechnol. 25:1281-1289(2007).
RN [2]
RP FUNCTION, ESTERASE ACTIVITY, SUBSTRATE SPECIFICITY, MUTAGENESIS OF SER-148;
RP SER-149; SER-386; SER-412 AND SER-419, DOMAIN, AND ACTIVE SITE.
RX PubMed=25907516; DOI=10.1016/j.jsb.2015.04.009;
RA Udatha D.B., Madsen K.M., Panagiotou G., Olsson L.;
RT "Multiple nucleophilic elbows leading to multiple active sites in a single
RT module esterase from Sorangium cellulosum.";
RL J. Struct. Biol. 190:314-327(2015).
CC -!- FUNCTION: Esterase with broad substrate specificity, that may be
CC involved in degradation of plant biomass present in the habitat of
CC S.cellulosum. In vitro, displays acetyl esterase activity, aryl
CC esterase activity, paraben esterase activity, carboxyl esterase
CC activity, poly-3-hydroxybutyric acid (PHB) depolymerase activity, and a
CC low feruloyl esterase activity. Does not possess any paraoxonase
CC activity. Is able to bind to multiple substrate molecules
CC simultaneously. {ECO:0000269|PubMed:25907516}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- DOMAIN: Comprises a single domain but contains five nucleophilic
CC elbows. Each nucleophilic elbow forms a local active site with varied
CC substrate specificities and affinities, thus possessing one or more
CC enzyme activities. {ECO:0000269|PubMed:25907516}.
CC -!- SIMILARITY: Belongs to the carbohydrate esterase 1 (CE1) family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AM746676; CAN93436.1; -; Genomic_DNA.
DR RefSeq; WP_012235908.1; NC_010162.1.
DR AlphaFoldDB; A9GMG8; -.
DR SMR; A9GMG8; -.
DR STRING; 448385.sce3277; -.
DR EnsemblBacteria; CAN93436; CAN93436; sce3277.
DR KEGG; scl:sce3277; -.
DR eggNOG; COG3509; Bacteria.
DR HOGENOM; CLU_027551_1_2_7; -.
DR OrthoDB; 1195966at2; -.
DR BioCyc; SCEL448385:SCE_RS16795-MON; -.
DR Proteomes; UP000002139; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR010126; Esterase_phb.
DR InterPro; IPR024038; MYXO-CTERM.
DR Pfam; PF10503; Esterase_PHB; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR TIGRFAMs; TIGR03901; MYXO-CTERM; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Hydrolase; Membrane; Reference proteome; Serine esterase;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..456
FT /note="Multifunctional esterase"
FT /id="PRO_5002738878"
FT TRANSMEM 433..449
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 382..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..425
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 148
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:25907516"
FT ACT_SITE 149
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:25907516"
FT ACT_SITE 386
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:25907516"
FT ACT_SITE 412
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:25907516"
FT ACT_SITE 419
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:25907516"
FT MUTAGEN 148
FT /note="S->A: About 30% decrease in acetyl esterase
FT activity. Loss of PHB depolymerase activity."
FT /evidence="ECO:0000269|PubMed:25907516"
FT MUTAGEN 149
FT /note="S->A: About 30% decrease in acetyl esterase
FT activity. Loss of PHB depolymerase activity."
FT /evidence="ECO:0000269|PubMed:25907516"
FT MUTAGEN 386
FT /note="S->A: About 20% decrease in aryl esterase activity.
FT Loss of carboxyl esterase activity. Loss of PHB
FT depolymerase activity."
FT /evidence="ECO:0000269|PubMed:25907516"
FT MUTAGEN 412
FT /note="S->A: Loss of PHB depolymerase activity."
FT /evidence="ECO:0000269|PubMed:25907516"
FT MUTAGEN 419
FT /note="S->A: About 90% decrease in aryl esterase activity.
FT About 80% decrease in acetyl esterase activity. Nearly loss
FT of paraben esterase activity. Loss of PHB depolymerase
FT activity."
FT /evidence="ECO:0000269|PubMed:25907516"
SQ SEQUENCE 456 AA; 45126 MW; 7E22EC03C0F54464 CRC64;
MDQFKTHVLG LASLSLALLV ALPARGASLQ KVNQSEWGAD GLPSYVNMYI YVPDKLATKP
PIVVAPHHCQ GNGQGTFSEM SSLVSIANTS GFIMIFPEAT GQNCWDAGST RSLNHGGGGD
TGAIVQMVKY TLAKYGGDAG RVYSVGGSSG GIMTEALLGV YPDVFMAGVS LMGVPCGCWA
EGYNDVTGTG SSAQWSGPCG GGNVTKTGQQ WGDLVRSYYP GYTGHRPRLQ HWHGTADTIL
SYKNMAEDIK EWTNVLGLSE TPSGTDTPKR GTTRQFWKSA CGYTVYEAFS MDGVGHAVPF
DGPAVAAYFG LDRAGGQDPE TAACPGAVPG GSDTGGAGGA TGAGGAGGEA GTGGAGGEVG
AGGAGGEAGA GAGGAGGVTV SGSGGSAGSG GAMDTASGGA NGQDASAGTG DSTGGEGSSS
GCSCAVGNDA RDAGAQAGFL LAALGLLLGR QKRRPR
