ID A0A0W7WXV8_9ACTN Unreviewed; 355 AA.
AC A0A0W7WXV8;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 08-OCT-2025, entry version 28.
DE RecName: Full=NlpC/P60 domain-containing protein {ECO:0000259|PROSITE:PS51935};
GN ORFNames=AT728_30025 {ECO:0000313|EMBL:KUF15390.1};
OS Streptomyces silvensis.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1765722 {ECO:0000313|EMBL:KUF15390.1, ECO:0000313|Proteomes:UP000054804};
RN [1] {ECO:0000313|EMBL:KUF15390.1, ECO:0000313|Proteomes:UP000054804}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 53525 {ECO:0000313|EMBL:KUF15390.1,
RC ECO:0000313|Proteomes:UP000054804};
RA Johnston C.W., Li Y., Magarvey N.A.;
RT "Draft genome sequence of Streptomyces silvensis ATCC 53525, a producer of
RT novel hormone antagonists.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase C40 family.
CC {ECO:0000256|ARBA:ARBA00007074}.
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:KUF15390.1}.
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DR EMBL; LOCL01000045; KUF15390.1; -; Genomic_DNA.
DR RefSeq; WP_058850485.1; NZ_LOCL01000045.1.
DR AlphaFoldDB; A0A0W7WXV8; -.
DR STRING; 1765722.AT728_30025; -.
DR OrthoDB; 5177647at2; -.
DR Proteomes; UP000054804; Unassembled WGS sequence.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.90.1720.10; endopeptidase domain like (from Nostoc punctiforme); 1.
DR InterPro; IPR000064; NLP_P60_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR051794; PG_Endopeptidase_C40.
DR PANTHER; PTHR47359:SF3; NLP_P60 DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR47359; PEPTIDOGLYCAN DL-ENDOPEPTIDASE CWLO; 1.
DR Pfam; PF00877; NLPC_P60; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS51935; NLPC_P60; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000054804};
KW Signal {ECO:0000256|SAM:SignalP};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807}.
FT SIGNAL 1..35
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 36..355
FT /note="NlpC/P60 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006936799"
FT DOMAIN 240..355
FT /note="NlpC/P60"
FT /evidence="ECO:0000259|PROSITE:PS51935"
FT REGION 204..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 43..91
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 134..168
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 204..221
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 355 AA; 38245 MW; 39B189317DB3E4EB CRC64;
MASHRRPKQP GRARVTVLTA TAAAAVALTS QAANAAPSEK PSKDEVKSKV DKLYEEAEKA
TEKFNGAKEK QQKLEKQVDT LQDKVARGQD DLNELRSGVG SLASAQYRSG GIDPSLQLFL
SSDPDNYLDK ASALDQLSTK QAEALKKIQA KQRTLAQQRK EAADKLEDLA TTRTELGKKK
REVQGKLGEA QRLLNTLTAA ERAALKDKEE RASRASERQA LDKQGQASQG EAPKSNAKGS
GRAASAYAAA QSKIGSPYVY GATGPSSFDC SGLTSWAYAQ AGMNIPRTSQ AQANYGTRIA
SQSDLRVGDL VIFYGDLHHV GFYAGNGQVL HAPRTGTVVR YESINNMPFQ FGVRI
//
