ID A0A0J7Z8Z3_STRVR Unreviewed; 663 AA.
AC A0A0J7Z8Z3;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Pectate lyase {ECO:0000313|EMBL:KMS71947.1};
GN ORFNames=ACM01_25350 {ECO:0000313|EMBL:KMS71947.1};
OS Streptomyces viridochromogenes.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1938 {ECO:0000313|EMBL:KMS71947.1, ECO:0000313|Proteomes:UP000037432};
RN [1] {ECO:0000313|EMBL:KMS71947.1, ECO:0000313|Proteomes:UP000037432}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 3414 {ECO:0000313|EMBL:KMS71947.1,
RC ECO:0000313|Proteomes:UP000037432};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL Submitted (JUN-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:KMS71947.1}.
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DR EMBL; LFNT01000031; KMS71947.1; -; Genomic_DNA.
DR RefSeq; WP_048583659.1; NZ_LGUR01000184.1.
DR AlphaFoldDB; A0A0J7Z8Z3; -.
DR PATRIC; fig|1938.3.peg.4390; -.
DR OrthoDB; 112037at2; -.
DR Proteomes; UP000037432; 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 Secreted {ECO:0000256|RuleBase:RU361173}.
FT DOMAIN 75..292
FT /note="Pectate lyase"
FT /evidence="ECO:0000259|SMART:SM00656"
SQ SEQUENCE 663 AA; 71549 MW; 0DA4FCC871233C02 CRC64;
MTHLRSKRLP ISGPGSGRTL TAVVGLVAAL GLGTLGEANA AAPATTTKTP AARWSDQPHG
FASVAGGTTG GAGGKVVTVT DQASLARYAA APEPYVIRVQ GAITAQPFGA SINVASDKTI
IGVGTSGELV QGEFHLAPGT HNVIIRNMTI RDSAIAGNWD CKDTDFDGIQ MDTVHHVWVD
HNRFSNICDG QLDVRKDSEY VTVSYNRFEN NNKTFGLGWT TNVKTQITID HNWFAGTKQR
NPSVDNAAYA HLYNNYLTAQ ADPGDPVWTY GNWSRGRTKM VIENSYYRDV QHPYQADATA
ELVQRGSILK NTTGRHDEWG AAFEPRDFYD YRLDPAAAVP ALVKRFSGPQ ERIGVVLNVP
AAYPTVQAAV DAVPEGNASA VTIAVAPGTY REKVLIPAKK PNIVLQGTGR DRSDTLIVFD
TPAEYGGSTG SATVRIAAND VTARNLTFSN DFDEAAHELK GEQALAMKTT GDRIVFENTG
FLGNQDTLMT DSPKLTTLSR VYLRDCYIEG DVDFIYGRAS TVIEHSLIKA LNRGSTTNNG
WITAASTWTG NPYGFLITRS KIVSDAPAGS FHLGRPWHPG GEPAAVAQVL IRDTLLPAAI
KASPWTDMSE FSWKDARFTE YGNYGPGAAV TADRPQMSDE AARSHTVSDY LKGTDGWAPH
VRH
//
