ID E8V2Q7_TERSS Unreviewed; 353 AA.
AC E8V2Q7;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Pectinesterase {ECO:0000313|EMBL:ADV83532.1};
GN OrderedLocusNames=AciPR4_2759 {ECO:0000313|EMBL:ADV83532.1};
OS Terriglobus saanensis (strain ATCC BAA-1853 / DSM 23119 / SP1PR4).
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC Terriglobus.
OX NCBI_TaxID=401053 {ECO:0000313|EMBL:ADV83532.1, ECO:0000313|Proteomes:UP000006844};
RN [1] {ECO:0000313|EMBL:ADV83532.1, ECO:0000313|Proteomes:UP000006844}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC BAA-1853 / DSM 23119 / SP1PR4
RC {ECO:0000313|Proteomes:UP000006844};
RX PubMed=23450133; DOI=10.4056/sigs.3036810;
RA Rawat S.R., Mannisto M.K., Starovoytov V., Goodwin L., Nolan M., Hauser L.,
RA Land M., Davenport K.W., Woyke T., Haggblom M.M.;
RT "Complete genome sequence of Terriglobus saanensis type strain SP1PR4(T),
RT an Acidobacteria from tundra soil.";
RL Stand. Genomic Sci. 7:59-69(2012).
CC -!- SIMILARITY: Belongs to the pectinesterase family.
CC {ECO:0000256|ARBA:ARBA00008891}.
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DR EMBL; CP002467; ADV83532.1; -; Genomic_DNA.
DR AlphaFoldDB; E8V2Q7; -.
DR STRING; 401053.AciPR4_2759; -.
DR KEGG; tsa:AciPR4_2759; -.
DR eggNOG; COG4677; Bacteria.
DR HOGENOM; CLU_012243_3_1_0; -.
DR OrthoDB; 9804686at2; -.
DR Proteomes; UP000006844; Chromosome.
DR GO; GO:0045330; F:aspartyl esterase activity; IEA:UniProtKB-KW.
DR GO; GO:0030599; F:pectinesterase activity; IEA:InterPro.
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 PANTHER; PTHR31321; ACYL-COA THIOESTER HYDROLASE YBHC-RELATED; 1.
DR PANTHER; PTHR31321:SF141; ACYL-COA THIOESTER HYDROLASE YBHC-RELATED; 1.
DR Pfam; PF01095; Pectinesterase; 2.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
PE 3: Inferred from homology;
KW Aspartyl esterase {ECO:0000256|ARBA:ARBA00023085};
KW Hydrolase {ECO:0000256|ARBA:ARBA00023085};
KW Reference proteome {ECO:0000313|Proteomes:UP000006844};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..353
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011118307"
FT DOMAIN 29..166
FT /note="Pectinesterase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01095"
FT DOMAIN 188..318
FT /note="Pectinesterase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01095"
FT REGION 331..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 353 AA; 39161 MW; CF02B3E9BEC3F4CA CRC64;
MSRTCAFFTF ALATLCVTSS LTAESMKRVT VSASGDTDFH TLQEAVDHAP STGEIILLAP
GRYREKIHIT TPNIRLIGVG KRPQDVVLSW NDSARRAGGT GKSGSVSVDA DGFAAENLTI
ENTWEMENER TEEGAQAVAL LLNSDRAVLD NVRLLGAQDT LYANSRTCHE NLPKDGSVPP
PGQTACSASR EYFRNCYIEG HVDYIFGDAK AVFDHCEMHS RHHDTVMLTA QSRHFPEEDS
GYFFLHSRIT GEDVGDKVVL GRPWRDYSTV LFYDTDVQQK LSADGWSEWA GRLKTSSYHE
YKSHGPGVNG GHRIVNYPPL SAAEEEQLTP TGLLGGKDHW NPMEEANRLR ERR
//
