ID A0A0N1GF40_9ACTN Unreviewed; 411 AA.
AC A0A0N1GF40;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Transglycosylase-like domain protein {ECO:0000313|EMBL:KPI18476.1};
DE Flags: Precursor;
GN ORFNames=OK074_7959 {ECO:0000313|EMBL:KPI18476.1};
OS Actinobacteria bacterium OK074.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1592327 {ECO:0000313|EMBL:KPI18476.1, ECO:0000313|Proteomes:UP000037991};
RN [1] {ECO:0000313|EMBL:KPI18476.1, ECO:0000313|Proteomes:UP000037991}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK074 {ECO:0000313|EMBL:KPI18476.1,
RC ECO:0000313|Proteomes:UP000037991};
RA Brown S.D., Utturkar S.M., Klingeman D.M., Pelletier D.;
RT "Draft genome sequences for four actinobacteria strains OK006 OK074 OV450
RT and OV320.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the transglycosylase family. Rpf subfamily.
CC {ECO:0000256|ARBA:ARBA00010830}.
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:KPI18476.1}.
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DR EMBL; LJCV01000065; KPI18476.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N1GF40; -.
DR PATRIC; fig|1592327.3.peg.2255; -.
DR OrthoDB; 5244067at2; -.
DR Proteomes; UP000037991; Unassembled WGS sequence.
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; SSF54106; LysM domain; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
DR PROSITE; PS51782; LYSM; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000037991};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..41
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 42..411
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005872267"
FT DOMAIN 189..238
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT REGION 128..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 240..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..174
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..257
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 411 AA; 42715 MW; 4365B9E0811E7455 CRC64;
MADRGRHRRY QPNRINRASL TVTAGGAGMA IPLAAAGVAH AADVSTWDKV AACESSGDWS
IDTGNGYYGG LQFTQSTWEA YGGRAYAPRA DLATKDQQIA VAEKVLAGQG PGAWPVCSVR
AGLTRGGATA DVDTSSGTHA QTAKTEATAT KKTAEPKKTA EPKKTTENKR TVRDVKPQTT
PQSQAGTTRM YTVVPGDALS RIADSHDVKG GWPDLYAANR KTVGTDPDLI LPGQRLTLDG
RTAAQSTKST KSATSAADTA KKAEPKAEKA AVEKATTTSM VAPVNARIGT PYHATGSEWS
RGYHTGVDFL APTGTSVKAV AAGTVVTAGW GGSYGYQVVI KHADGRYTEY AHLSAISVKA
GQSVTTGQRI GRSGATGNAT GPHLHFEVRT GPGFGTDVDP LAYLRAGGVK I
//
