ID A9GMG6_SORC5 Unreviewed; 356 AA.
AC A9GMG6;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Esterase/lipase/thioesterase family protein {ECO:0000313|EMBL:CAN93435.1};
GN OrderedLocusNames=sce3276 {ECO:0000313|EMBL:CAN93435.1};
OS Sorangium cellulosum (strain So ce56) (Polyangium cellulosum (strain So
OS ce56)).
OC Bacteria; Myxococcota; Polyangia; Polyangiales; Polyangiaceae; Sorangium.
OX NCBI_TaxID=448385 {ECO:0000313|EMBL:CAN93435.1, ECO:0000313|Proteomes:UP000002139};
RN [1] {ECO:0000313|EMBL:CAN93435.1, ECO:0000313|Proteomes:UP000002139}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=So ce56 {ECO:0000313|Proteomes:UP000002139};
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).
CC -!- FUNCTION: Involved in degradation of plant cell walls. Hydrolyzes the
CC feruloyl-arabinose ester bond in arabinoxylans, and the feruloyl-
CC galactose ester bond in pectin. Active against paranitrophenyl-acetate,
CC methyl ferulate and wheat arabinoxylan.
CC {ECO:0000256|ARBA:ARBA00025250}.
CC -!- SIMILARITY: Belongs to the faeC family.
CC {ECO:0000256|ARBA:ARBA00010278}.
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DR EMBL; AM746676; CAN93435.1; -; Genomic_DNA.
DR AlphaFoldDB; A9GMG6; -.
DR STRING; 448385.sce3276; -.
DR ESTHER; sorc5-a9gmg6; FaeC.
DR KEGG; scl:sce3276; -.
DR eggNOG; COG3509; Bacteria.
DR HOGENOM; CLU_027551_2_0_7; -.
DR OrthoDB; 9767239at2; -.
DR Proteomes; UP000002139; Chromosome.
DR GO; GO:0030600; F:feruloyl esterase activity; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR043595; FaeB/C/D.
DR PANTHER; PTHR38050; -; 1.
DR PANTHER; PTHR38050:SF1; FERULOYL ESTERASE C; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000002139};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..356
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002738122"
FT REGION 53..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 356 AA; 35214 MW; AA12657EBA60284D CRC64;
MHYEKKAVSR FHVFCLLSSV AMLACGDESG DAAQAAGAGS SSVSAASAAS TGVTAGSSSA
SGGTSSGEAA SSGGATAGAG GAGSGGAGSG GAGGAGGAGT GGSGGGGGGG DAVKSAGCGK
MRTLQNGAGT VQSGGKSRKY ALRVPDDYDN GHPYRLILSF HGATGNSGQV APSYFGLWSL
SEGSTIFIAP DAVDGFWSAD DVTFVDDILE QVTGDLCIDT SRIELEGFSQ GGAMAWTLAC
ARPEVYRAAV VHSGGGLPRP ASCPPVAFMS SLGQQESGGA GQTSNSDFFA KQNGCTVEAL
PKAPRGGHAC SDYKGCSAGH PTRWCDYDGG HTPSPNDAGK QMSWMPEEVW AFLNQF
//
