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Database: UniProt
Entry: A0A919U5K8_9CELL
LinkDB: A0A919U5K8_9CELL
Original site: A0A919U5K8_9CELL 
ID   A0A919U5K8_9CELL        Unreviewed;       464 AA.
AC   A0A919U5K8;
DT   22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2023, sequence version 1.
DT   08-OCT-2025, entry version 9.
DE   RecName: Full=NlpC/P60 domain-containing protein {ECO:0000259|PROSITE:PS51935};
GN   ORFNames=Cpa01nite_07610 {ECO:0000313|EMBL:GIG35380.1};
OS   Cellulomonas pakistanensis.
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
OC   Cellulomonadaceae; Cellulomonas.
OX   NCBI_TaxID=992287 {ECO:0000313|EMBL:GIG35380.1, ECO:0000313|Proteomes:UP000642125};
RN   [1] {ECO:0000313|EMBL:GIG35380.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NBRC 110800 {ECO:0000313|EMBL:GIG35380.1};
RA   Komaki H., Tamura T.;
RT   "Whole genome shotgun sequence of Cellulomonas pakistanensis NBRC 110800.";
RL   Submitted (JAN-2021) 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:GIG35380.1}.
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DR   EMBL; BONO01000004; GIG35380.1; -; Genomic_DNA.
DR   Proteomes; UP000642125; Unassembled WGS sequence.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR   Gene3D; 6.10.250.3150; -; 1.
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:UP000642125};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Thiol protease {ECO:0000256|ARBA:ARBA00022807}.
FT   SIGNAL          1..34
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           35..464
FT                   /note="NlpC/P60 domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5036814089"
FT   DOMAIN          342..464
FT                   /note="NlpC/P60"
FT                   /evidence="ECO:0000259|PROSITE:PS51935"
FT   REGION          241..341
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          64..126
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        241..255
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        256..314
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        315..340
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   464 AA;  47286 MW;  14BD01BA0210A1F8 CRC64;
     MDVVRMGRTR AVRGAAAVIT AAVLLVPAGG AALADPDVTD QDVRDARRAV TSASGAVAGI
     EVRLAELATE ADAAQVAVQQ AGEDVAQAQA DLASAQQEAR EASAQYDQAQ EQLEDARSTL
     VAIARQAARS GGSMDTVQAL LSADGFEDVV ERSEALSRVS SRADQAVQGY LAAEQVATTL
     KGKADAAAEA QETAAADSQA ALDAAEQAQS DADAAVASAQ TERAGLIQQL AVARNTSAEV
     EQARQDQVDA ERQARAEAAA QAEREATPAP SAPAAGGGSA APSTPSTPST PAAPSTPSTP
     STPSTPSTPS TPSTPSNPAP TTPKPTTPVV TPPAATPPPV SASKAETAIA WARTKIGLPY
     VWGGTGPHGY DCSGLTQGAW KAAGVSLNRT SRDQYRQVTK IAYSQLQPGD LVFWGNNPND
     ASSVYHVAIY IGGGQILEAP KPGTPVKISP MRYFNSMAYA GRVG
//
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