ID A0A101JCV2_9ACTN Unreviewed; 690 AA.
AC A0A101JCV2;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Pectate lyase {ECO:0000313|EMBL:KUL24455.1};
GN ORFNames=ADL12_37090 {ECO:0000313|EMBL:KUL24455.1};
OS Streptomyces regalis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=68262 {ECO:0000313|EMBL:KUL24455.1, ECO:0000313|Proteomes:UP000053923};
RN [1] {ECO:0000313|Proteomes:UP000053923}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 3151 {ECO:0000313|Proteomes:UP000053923};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL Submitted (OCT-2015) 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:KUL24455.1}.
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DR EMBL; LLZG01000376; KUL24455.1; -; Genomic_DNA.
DR RefSeq; WP_062711029.1; NZ_LLZG01000376.1.
DR AlphaFoldDB; A0A101JCV2; -.
DR OrthoDB; 112037at2; -.
DR Proteomes; UP000053923; 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:UP000053923};
KW Secreted {ECO:0000256|RuleBase:RU361173}.
FT DOMAIN 81..300
FT /note="Pectate lyase"
FT /evidence="ECO:0000259|SMART:SM00656"
FT REGION 654..690
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 656..670
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 690 AA; 72861 MW; 0A2C7D30F3E0117D CRC64;
MTETRNRPRH RRSRTALAVG VPLALTAAGT LAYGTDLGLF GADAQQKASA ATAAAPAWAT
AAADGFASLN SRGQNGTYGG RDGQIVTVKT QADLEKYATA AEPYVIVVAG TINMNPVGKE
IKVQSDKTIV GSGTSGHIVG GGFFLGSGVH NVIIRNLTIR DAYQGVWNDK DHDFDAVQMD
GAHHVWIDHN DLRHMADGLI DVRKDSTNVT VSWNRLSNDN KAFGIGWTDN VVTDITIHHN
WIRETEQRNP STDNAAHAHL YNNFLEDVAG TDIKSSYGNY SRGKTKMVLE NSYFQGINNP
VIKDGTATLV QRGSVFSGTS GRNESGGTAF DPKAYYSYTL DAAANVPSLL KSGAGPRSSI
GTTTAAAVGT KAATTLTVAK DGNGQYTSVQ AAVNAVPANN ASRVVIAVKP GTYREVVKVP
ANKPHVTIQG TGGSRKDTVI VYNNASGTPK PGGGTYGTGG SATVAVEADD FQARNLTINN
DFDEKANQNL SGHQAVALRT AADKVFLDGV IVGGDQDTLL VDTASKDKLG RVYMKNSYVI
GNVDFIFGRA TAVIDRSVIT LKKRWDGTSA GYVTAPSTAA NRKGILIANS TVNGDVSDRS
FFLGRNWHAG GDATLDPQTT VRNTTLSAAI KTTPWSDMGG FSWKDDRFAE YKNTGAGAGS
ASSDRPQLTD AQAGGQEVAD WLGDWTPTAS
//
