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Database: UniProt
Entry: A0A2Z4USB7_9ACTN
LinkDB: A0A2Z4USB7_9ACTN
Original site: A0A2Z4USB7_9ACTN 
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}.
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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
//
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