ID A0A2Z4USB7_9ACTN Unreviewed; 434 AA.
AC A0A2Z4USB7;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Peptidase {ECO:0000313|EMBL:AWZ11857.1};
GN ORFNames=DRB96_05485 {ECO:0000313|EMBL:AWZ11857.1};
OS Streptomyces sp. ICC1.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2099583 {ECO:0000313|EMBL:AWZ11857.1, ECO:0000313|Proteomes:UP000250268};
RN [1] {ECO:0000313|EMBL:AWZ11857.1, ECO:0000313|Proteomes:UP000250268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ICC1 {ECO:0000313|EMBL:AWZ11857.1,
RC ECO:0000313|Proteomes:UP000250268};
RA Gosse J.;
RT "Whole genome sequencing and metabolomic study of cave Streptomyces
RT isolates ICC1 and ICC4.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the transglycosylase family. Rpf subfamily.
CC {ECO:0000256|ARBA:ARBA00010830}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP030287; AWZ11857.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Z4USB7; -.
DR Proteomes; UP000250268; 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; 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:UP000250268}.
FT DOMAIN 180..229
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT REGION 117..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 234..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..256
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..280
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..405
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 434 AA; 44573 MW; A37FC1E1CF48F449 CRC64;
MGVRGRHRRY QPSSINRASL VVTAGGAGIA LPLIGAGTAH AASVDTWSKV AACESTGNWH
INTGNGYYGG LQFSQSTWRA FGGAAYASRA DLATREQQIA VAEKVLKGQG PQAWPVCGKK
AGLSRSGPAP ALPAQAKPVT PVQQTKAQLQ EKKAAAPPST PRSTPPKSAP RPTGTSVLPN
PYVVAPGDSL SAIATEQHVE GGWQALYETN RATVGGDPDL IFPGQRLTLR VTAAPAAPAA
PPSQNPEKPP RTAEPVKPVA PVSEKPAEKP AEKPADKPAA KPAEKPAAQP ASAQKDETAS
GGFSAPVDAG LGTAYRVAGS SWSSGYHTGV DFPVATGTTV KAVSDGQVVS AGWAGAYGYQ
VVIRHSDGRY SQYAHLSALA VKAGSPVSGG QRIGRSGSTG NTTGPHLHFE VRGGPGYGTD
IDPLKYLRAH GVHI
//