ID   B5MA92_9NOCA            Unreviewed;       479 AA.
AC   B5MA92;
DT   14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2008, sequence version 1.
DT   28-JUN-2023, entry version 36.
DE   SubName: Full=Putative secreted transglycosylase {ECO:0000313|EMBL:CAR47820.1};
OS   Rhodococcus sp. PY11.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=551544 {ECO:0000313|EMBL:CAR47820.1};
RN   [1] {ECO:0000313|EMBL:CAR47820.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PY11 {ECO:0000313|EMBL:CAR47820.1};
RA   Gasparaviciute R., Rutkiene R., Casaite V., Meskiene R., Kutanovas S.,
RA   Meskys R.;
RT   "Cloning and characterization of genes for the degradation of 2-
RT   hydroxypyridine of Rhodococcus sp. strain PY11.";
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CAR47820.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PY11 {ECO:0000313|EMBL:CAR47820.1};
RA   Gasparaviciute R.;
RT   "Analysis of genes encoding degradation of pyridine and pyridinols.";
RL   Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase C40 family.
CC       {ECO:0000256|ARBA:ARBA00007074}.
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DR   EMBL; FM202432; CAR47820.1; -; Genomic_DNA.
DR   AlphaFoldDB; B5MA92; -.
DR   CAZy; GH23; Glycoside Hydrolase Family 23.
DR   CDD; cd12797; M23_peptidase; 1.
DR   CDD; cd13399; Slt35-like; 1.
DR   Gene3D; 1.10.530.10; -; 1.
DR   Gene3D; 3.90.1720.10; endopeptidase domain like (from Nostoc punctiforme); 1.
DR   Gene3D; 2.70.70.10; Glucose Permease (Domain IIA); 1.
DR   InterPro; IPR011055; Dup_hybrid_motif.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   InterPro; IPR000064; NLP_P60_dom.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR016047; Peptidase_M23.
DR   InterPro; IPR031304; SLT_2.
DR   PANTHER; PTHR47359:SF3; NLPC_P60 DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR47359; PEPTIDOGLYCAN DL-ENDOPEPTIDASE CWLO; 1.
DR   Pfam; PF00877; NLPC_P60; 1.
DR   Pfam; PF01551; Peptidase_M23; 1.
DR   Pfam; PF13406; SLT_2; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF51261; Duplicated hybrid motif; 1.
DR   SUPFAM; SSF53955; Lysozyme-like; 1.
DR   PROSITE; PS51935; NLPC_P60; 1.
PE   3: Inferred from homology;
FT   DOMAIN          355..479
FT                   /note="NlpC/P60"
FT                   /evidence="ECO:0000259|PROSITE:PS51935"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          144..169
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..23
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   479 AA;  49141 MW;  E0584326D4B299B0 CRC64;
     MHLSGPIQLP VQPGTTTHTS GFGPRWGTHH HGDDLAGPVG TPILAALDGV VVAAGATGEG
     PGVGFENWVI IDSNVDGSPV STVYGHMFAD GIHVTAGQQV TAGDHIADMG NAGSSTGAHL
     HFEYWQGGRL QGGTPIDPVT VLPEITRQSG GTPPSVGDRH DSDSHGDQGS NVWLVAASRS
     TADCSGFGIA GGGDLAFKAV PTEFEPWLRR AGGVCPEIDS PLLAAQLQQE NNFRYGPNAP
     VSPSGAIGPA QFMPGTWATW GKDHDGNGTA DPNSIGDAVM SQAHFMCALR HDISEIPGDP
     IELTLAAYNA GPGAVLLHRG IPPYAETQNY IAKITAARAA FTNPNSRGRF TPKASGDNSQ
     AVAAAREYLG TPYVWGGGGI GGPSGGGFDC SGLTSFAVHA ASAGTVTLPR TSEQQWDVGV
     EVPIAQAQPG DLVFGNWGPN GPGHVGIYSG NGQMVHAPTT GGVVEETPLQ AGMKARRVM
//