ID E8V1Z8_TERSS Unreviewed; 330 AA.
AC E8V1Z8;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Pectinesterase {ECO:0000313|EMBL:ADV83486.1};
GN OrderedLocusNames=AciPR4_2712 {ECO:0000313|EMBL:ADV83486.1};
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:ADV83486.1, ECO:0000313|Proteomes:UP000006844};
RN [1] {ECO:0000313|EMBL:ADV83486.1, 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; ADV83486.1; -; Genomic_DNA.
DR RefSeq; WP_013569219.1; NC_014963.1.
DR AlphaFoldDB; E8V1Z8; -.
DR STRING; 401053.AciPR4_2712; -.
DR KEGG; tsa:AciPR4_2712; -.
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; 1.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..330
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011118287"
FT DOMAIN 38..316
FT /note="Pectinesterase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01095"
SQ SEQUENCE 330 AA; 36598 MW; 893F13BC2AB410B9 CRC64;
MLLRSYMMVL FTLLSCSLLE AQDVHIHVSP TSTGTTASTD DFPTIQMALD HAPDVGPRGR
LYLHIAPGTY RERVWVSPLR ARTTLLGTGS DPSQVVITAA QNAKTSQSTF FSETVEVNGD
GFQADNITFE NTAGNNGQAV AIAVHSDRAI FKRCRFLGDQ DTLLANFGRQ YYVDSYIQGG
VDFIFGNAAA VFEKSEIHIA RPGYLTAQSR TQPWQATGFV FQHSRVTADD FGDKVFYLGR
PWRLYSRVVF LDTELPASLS PEGWSPWKHG DEPRDTFYAE RNSSGPGARA ESRVSWSHQL
TARQAIPFGT LEFLAGKDHW NPVREAANLP
//
