ID C9Z544_STRSW Unreviewed; 371 AA.
AC C9Z544;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=Putative secreted protein {ECO:0000313|EMBL:CBG68348.1};
GN OrderedLocusNames=SCAB_11801 {ECO:0000313|EMBL:CBG68348.1};
OS Streptomyces scabiei (strain 87.22).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=680198 {ECO:0000313|EMBL:CBG68348.1, ECO:0000313|Proteomes:UP000001444};
RN [1] {ECO:0000313|EMBL:CBG68348.1, ECO:0000313|Proteomes:UP000001444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=87.22 {ECO:0000313|EMBL:CBG68348.1,
RC ECO:0000313|Proteomes:UP000001444};
RX PubMed=20064060; DOI=10.1094/MPMI-23-2-0161;
RA Bignell D.R., Seipke R.F., Huguet-Tapia J.C., Chambers A.H., Parry R.J.,
RA Loria R.;
RT "Streptomyces scabies 87-22 contains a coronafacic acid-like biosynthetic
RT cluster that contributes to plant-microbe interactions.";
RL Mol. Plant Microbe Interact. 23:161-175(2010).
CC -!- SIMILARITY: Belongs to the transglycosylase family. Rpf subfamily.
CC {ECO:0000256|ARBA:ARBA00010830}.
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DR EMBL; FN554889; CBG68348.1; -; Genomic_DNA.
DR RefSeq; WP_012999078.1; NC_013929.1.
DR AlphaFoldDB; C9Z544; -.
DR STRING; 680198.SCAB_11801; -.
DR CAZy; CBM50; Carbohydrate-Binding Module Family 50.
DR CAZy; GH23; Glycoside Hydrolase Family 23.
DR GeneID; 24310728; -.
DR KEGG; scb:SCAB_11801; -.
DR eggNOG; COG0739; Bacteria.
DR eggNOG; COG1652; Bacteria.
DR HOGENOM; CLU_029425_12_1_11; -.
DR Proteomes; UP000001444; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR CDD; cd00118; LysM; 1.
DR CDD; cd12797; M23_peptidase; 1.
DR CDD; cd13925; RPF; 1.
DR Gene3D; 1.10.530.10; -; 1.
DR Gene3D; 2.70.70.10; Glucose Permease (Domain IIA); 1.
DR Gene3D; 3.10.350.10; LysM domain; 1.
DR InterPro; IPR011055; Dup_hybrid_motif.
DR InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR016047; Peptidase_M23.
DR InterPro; IPR010618; RPF.
DR PANTHER; PTHR21666:SF286; BLR0433 PROTEIN; 1.
DR PANTHER; PTHR21666; PEPTIDASE-RELATED; 1.
DR Pfam; PF01476; LysM; 1.
DR Pfam; PF01551; Peptidase_M23; 1.
DR Pfam; PF06737; Transglycosylas; 1.
DR SMART; SM00257; LysM; 1.
DR SUPFAM; SSF51261; Duplicated hybrid motif; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
DR PROSITE; PS51782; LYSM; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000001444}.
FT DOMAIN 142..191
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT REGION 176..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..230
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 371 AA; 39311 MW; EE4244F8DA149E29 CRC64;
MAASGRHRRY QPNRINRASL TVTAGGAGMA LPLIGTGAAE AADVETWDKV AACESTNDWN
INSGNGYYGG LQFSQSTWEA FGGTAYAARA DLATKEQQIA IAEKVLDGQG PDAWPVCSGR
AGLTIGDVKP QTTPQSQAGK VEMYTVVRGD TLSGIADAED VRGGWRRLYE NNRRTIGSDP
DVIIPGQRLS LHAAGRKEES KKERKPEKRQ ESRQEKKPVH KEHKGGKQQT SEKRQQSASL
VAPVGASLGT PYRASGSSWS KGYHTGVDFP VSTGSSVKSV AAGQVVSAGW GGSFGYEVVI
RHADGRYTQY AHLSAISVKA GQGVSTGQRI GRSGSTGNSS GPHLHFEVRT GPGFGSDIDP
IAYLRAGGVR I
//
