ID A0A0Q7T178_9BURK Unreviewed; 474 AA.
AC A0A0Q7T178;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Pectinesterase catalytic domain-containing protein {ECO:0000259|Pfam:PF01095};
GN ORFNames=ASD35_15845 {ECO:0000313|EMBL:KQY88990.1};
OS Pelomonas sp. Root1444.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Roseateles.
OX NCBI_TaxID=1736464 {ECO:0000313|EMBL:KQY88990.1, ECO:0000313|Proteomes:UP000051648};
RN [1] {ECO:0000313|Proteomes:UP000051648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1444 {ECO:0000313|Proteomes:UP000051648};
RA Garrido-Oter R., Mueller D.B.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQY88990.1, ECO:0000313|Proteomes:UP000051648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1444 {ECO:0000313|EMBL:KQY88990.1,
RC ECO:0000313|Proteomes:UP000051648};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the pectinesterase family.
CC {ECO:0000256|ARBA:ARBA00008891}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQY88990.1}.
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DR EMBL; LMFP01000003; KQY88990.1; -; Genomic_DNA.
DR RefSeq; WP_056874196.1; NZ_LMFP01000003.1.
DR AlphaFoldDB; A0A0Q7T178; -.
DR STRING; 1736464.ASD35_15845; -.
DR Proteomes; UP000051648; Unassembled WGS sequence.
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.
PE 3: Inferred from homology;
KW Aspartyl esterase {ECO:0000256|ARBA:ARBA00023085};
KW Hydrolase {ECO:0000256|ARBA:ARBA00023085};
KW Reference proteome {ECO:0000313|Proteomes:UP000051648};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..474
FT /note="Pectinesterase catalytic domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011117080"
FT DOMAIN 164..329
FT /note="Pectinesterase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01095"
SQ SEQUENCE 474 AA; 50989 MW; 613B969448F98BCE CRC64;
MKSLLLWAAC LPAVAWGQEA SPVPSPAPQA TGVSPDTQLA IRFDSPPTLG SSGLIRIHDA
DDGRVVDTLD LAISASPNRR MAPAEATADA AKNAYQSTRI AGRDWHFRPV IVRGNVATIY
PHHGVLAYGR RYRVTVDGGV LQPAAIAWTF ATRKAPPAAD SPRLVVAADG SGDFATVQGA
VDFVPGKPAK RVTIFIRNGF YEEIVSLAGK RNLTIRGESR NKVQVGYANN SAFNPGGRAR
WAFSIVDGED IQLSSFTISN HAVGQAEALM TRGERIVLSD MTLNGSGDAL TTYGTLYVQD
SKLTGHGDTI LGYAAAYFLR TELQSIGPFS WTRTPAGQHG NVFVDCSFIA SDAPLPWAAS
APVANPAAVF ARLPRNNSAT RTADNFPHAE MVLINTRTQG IPPEGWGPVE EAPGFDSSQV
RFWEFNTTDL QGKPVDVSRR HPVSRQLTME KDAALIADYK RPEFVLGGWK PVVE
//
