ID L1KNI9_9ACTN Unreviewed; 664 AA.
AC L1KNI9;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Pectinesterase {ECO:0000313|EMBL:EKX61948.1};
GN ORFNames=STRIP9103_02002 {ECO:0000313|EMBL:EKX61948.1};
OS Streptomyces ipomoeae 91-03.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=698759 {ECO:0000313|EMBL:EKX61948.1, ECO:0000313|Proteomes:UP000010411};
RN [1] {ECO:0000313|EMBL:EKX61948.1, ECO:0000313|Proteomes:UP000010411}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91-03 {ECO:0000313|EMBL:EKX61948.1,
RC ECO:0000313|Proteomes:UP000010411};
RA Huguet-Tapia J.C., Durkin A.S., Pettis G.S., Badger J.H.;
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|RuleBase:RU361173}.
CC -!- SIMILARITY: Belongs to the pectinesterase family.
CC {ECO:0000256|ARBA:ARBA00008891}.
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 1 family.
CC {ECO:0000256|RuleBase:RU361173}.
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:EKX61948.1}.
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DR EMBL; AEJC01000551; EKX61948.1; -; Genomic_DNA.
DR AlphaFoldDB; L1KNI9; -.
DR PATRIC; fig|698759.3.peg.7357; -.
DR Proteomes; UP000010411; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0045330; F:aspartyl esterase activity; IEA:UniProtKB-KW.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0030599; F:pectinesterase activity; IEA:InterPro.
DR GO; GO:0042545; P:cell wall modification; IEA:InterPro.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 2.
DR InterPro; IPR002022; Pec_lyase.
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; PF00544; Pectate_lyase_4; 1.
DR Pfam; PF01095; Pectinesterase; 1.
DR SMART; SM00656; Amb_all; 1.
DR SUPFAM; SSF51126; Pectin lyase-like; 2.
PE 3: Inferred from homology;
KW Aspartyl esterase {ECO:0000256|ARBA:ARBA00023085};
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU361173};
KW Hydrolase {ECO:0000256|ARBA:ARBA00023085};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU361173};
KW Polysaccharide degradation {ECO:0000256|RuleBase:RU361173};
KW Reference proteome {ECO:0000313|Proteomes:UP000010411};
KW Secreted {ECO:0000256|RuleBase:RU361173}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..37
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 38..664
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003951524"
FT DOMAIN 67..287
FT /note="Pectate lyase"
FT /evidence="ECO:0000259|SMART:SM00656"
FT REGION 43..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 664 AA; 71844 MW; 4B87A53CEDE7E7C8 CRC64;
MPESEPPGPR PGIGRALVTV AALVASLGLG AIAPAEAAPE TAVRAPGGWS DEPHGFASLD
GGTTGGAGGK VVTVTDQASL VRYASAAEPY VIRVKGAIDV EPFGSDIVVT SNKTIIGVGD
TGEIVHGELH LNPGTSNVII RNLTIRDSYV EGDWDGKTTD FDAIQMDTVD HVWIDHNRFE
HMGDGLLDIR KDSRYVTVSY NQFKNHNKAF GIGWTTNVRT EITIDHNWFT GTKQRNPSAD
NCAYAHLYNN YVSAQVADGD PVWTYGNWAR GRTRMVIENS YYDGVQHPYQ ADATAELVQR
GSILKNVSGR QDAWGTAFEP RDLYDYRLDP AAAVPALVTR FSGPQKRIGT NTVLDVPGSY
ATVQAAVDAV PDGNDGTVTI RIAPGTYREQ VRIPAGRSNL VLQGTGQDRA DTVIVYDTPA
AYGGSNGSAT VRIAANDVTA RNLTFSNDFD EAAHELNGEQ ALAMKTVGDR IVFEDTAFLG
NQDTLMTDSP RLDAISRVYI RDSYIEGDVD FIYGRATTVI ERSVIKALSR GSTTNNGYIT
AASTWKDNPY GFLITGSRVI SDAPAGTYHL GRPWHPGGEP NAIAQVLFRD TELPAAIKSS
PWTDMSGFSW KDARFTEYRT YGPGAGVTVD RPQLADADAD AYTVVKYLSG TDSWAPHRAA
RHRR
//
