ID A9EVP2_SORC5 Unreviewed; 217 AA.
AC A9EVP2;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 24-JAN-2024, entry version 73.
DE SubName: Full=Pectinesterase 2 {ECO:0000313|EMBL:CAN94243.1};
DE EC=3.1.1.11 {ECO:0000313|EMBL:CAN94243.1};
GN OrderedLocusNames=sce4080 {ECO:0000313|EMBL:CAN94243.1};
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:CAN94243.1, ECO:0000313|Proteomes:UP000002139};
RN [1] {ECO:0000313|EMBL:CAN94243.1, 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).
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DR EMBL; AM746676; CAN94243.1; -; Genomic_DNA.
DR AlphaFoldDB; A9EVP2; -.
DR STRING; 448385.sce4080; -.
DR KEGG; scl:sce4080; -.
DR eggNOG; COG4677; Bacteria.
DR HOGENOM; CLU_1271589_0_0_7; -.
DR Proteomes; UP000002139; Chromosome.
DR GO; GO:0045330; F:aspartyl esterase activity; IEA:UniProtKB-KW.
DR GO; GO:0030599; F:pectinesterase activity; IEA:UniProtKB-EC.
DR GO; GO:0042545; P:cell wall modification; IEA:InterPro.
DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 1.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR000070; Pectinesterase_cat.
DR Pfam; PF01095; Pectinesterase; 1.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
PE 4: Predicted;
KW Aspartyl esterase {ECO:0000256|ARBA:ARBA00023085};
KW Hydrolase {ECO:0000313|EMBL:CAN94243.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002139}.
FT DOMAIN 136..202
FT /note="Pectinesterase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01095"
FT REGION 188..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 217 AA; 22240 MW; EBECD43FD2CC1846 CRC64;
MSALFPAPGA RGLCPDPPLR ITFPGAPALG SAGAVRVFNA ARPGAAVATV DMASMTVSAT
IGGRTFNVPR PVYVDGNDVV VSLPSRALDY GESYYVTVDP GAIVPPGGGS FAIADATAWR
FDTANAGPSS VASLDVALDG SGDFCSVQGA LDAVPANNRD SVLITVQRGT HHGVVYFENK
HNITLRGADR KGTVLSGTNN NNLNPSTRGA RSSARTR
//
