ID   Q0SD38_RHOJR            Unreviewed;       436 AA.
AC   Q0SD38;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   27-MAR-2024, entry version 99.
DE   RecName: Full=NlpC/P60 domain-containing protein {ECO:0000259|PROSITE:PS51935};
GN   OrderedLocusNames=RHA1_ro02743 {ECO:0000313|EMBL:ABG94548.1};
OS   Rhodococcus jostii (strain RHA1).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=101510 {ECO:0000313|EMBL:ABG94548.1, ECO:0000313|Proteomes:UP000008710};
RN   [1] {ECO:0000313|Proteomes:UP000008710}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RHA1 {ECO:0000313|Proteomes:UP000008710};
RX   PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA   McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA   Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA   Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA   Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA   Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA   Eltis L.D.;
RT   "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT   catabolic powerhouse.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
CC   -!- SIMILARITY: Belongs to the peptidase C40 family.
CC       {ECO:0000256|ARBA:ARBA00007074}.
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DR   EMBL; CP000431; ABG94548.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q0SD38; -.
DR   CAZy; GH23; Glycoside Hydrolase Family 23.
DR   KEGG; rha:RHA1_ro02743; -.
DR   eggNOG; COG0741; Bacteria.
DR   eggNOG; COG0791; Bacteria.
DR   HOGENOM; CLU_619451_0_0_11; -.
DR   Proteomes; UP000008710; Chromosome.
DR   Gene3D; 1.10.530.10; -; 1.
DR   Gene3D; 3.90.1720.10; endopeptidase domain like (from Nostoc punctiforme); 1.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   InterPro; IPR000064; NLP_P60_dom.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
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; PF13406; SLT_2; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF53955; Lysozyme-like; 1.
DR   PROSITE; PS51935; NLPC_P60; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000008710}.
FT   DOMAIN          321..436
FT                   /note="NlpC/P60"
FT                   /evidence="ECO:0000259|PROSITE:PS51935"
FT   REGION          85..113
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        86..113
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   436 AA;  44600 MW;  FBB80D90BD4DE524 CRC64;
     MSVDPSTLIV AVVAAAGAFV QGMDAPPEVE DQATQILESY PAPAVDQQVS DVIAALPEPV
     RVPAQQAVDD VTAAAAAVLE PHLPAGALAP PAPEPGPQTP PEPVAPQSVP EPVPPASVFL
     SSPPVYDDAP SVGTSTVLQP IPATFPRASL APVGAIALFA PWLRKAGAIC DGIKPATLAA
     LYAAENGFRY GPTAPVSPSG ALGPGQFMPG TWAIYGKDAD DDGKADVLGI ADPVMASGHL
     LCDTYEQIDA WKRQGRVSGN TLDLTIAAYN AGAGAVLRSG GMPSGSPDYE NQTKPYVAKI
     RGSEPSFAEL LAPLIGLPLA DGVGGRVVES AIRYLGAPYV WGGGNVDGPS GGGFDCSGLT
     SFAVHAATGI TLPRTSETQW TIGQEIPMDQ ARPGDLLFGN WQSEGPGHVA IYIGNGQMIH
     APPRVTSCAS RTSFPK
//