ID   P54_ENTFC               Reviewed;         516 AA.
AC   P13692;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 2.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Protein P54;
DE   Flags: Precursor;
OS   Enterococcus faecium (Streptococcus faecium).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=1352;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2780297; DOI=10.1093/nar/17.16.6724;
RA   Fuerst P., Moesch H.-U., Solioz M.;
RT   "A protein of unusual composition from Enterococcus faecium.";
RL   Nucleic Acids Res. 17:6724-6724(1989).
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall.
CC   -!- SIMILARITY: Belongs to the peptidase C40 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01284, ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA34442.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; X16421; CAA34442.1; ALT_INIT; Genomic_DNA.
DR   PIR; S05542; S05542.
DR   AlphaFoldDB; P13692; -.
DR   SMR; P13692; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR000064; NLP_P60_dom.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   Pfam; PF00877; NLPC_P60; 1.
DR   SUPFAM; SSF54001; SSF54001; 1.
DR   PROSITE; PS51935; NLPC_P60; 1.
PE   3: Inferred from homology;
KW   Cell wall; Hydrolase; Protease; Secreted; Signal; Thiol protease.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..516
FT                   /note="Protein P54"
FT                   /id="PRO_0000026544"
FT   DOMAIN          399..516
FT                   /note="NlpC/P60"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
FT   REGION          208..397
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        208..237
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        259..380
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        381..395
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        429
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
FT   ACT_SITE        480
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
FT   ACT_SITE        492
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
SQ   SEQUENCE   516 AA;  54596 MW;  402ECAA439846D26 CRC64;
     MKKSLLSAVM LSSIALTAVG SPIAAAADDF DSQIQQQDKK IADLQNQQAS AQSQIEALEG
     QVSAINTKAQ DLLTKQDTLR KESAQLKQEI KDLQERIEKR EATIQKQARE TQVKNTSSNY
     IDAVLNADSL ADAVGRIQAM STIVKANQDL VQQQKEDKQA VEAKKAENEA KQKELADNQA
     ALESQKGDLL AKQADLNVLK TSLAAEQATA EDKKADLNRK KAEAEAEQAR IREQARLAEQ
     ARQQAAQEKA EKEAREQAAA QAAQTQALSS ASTTTESSSA AQSSSEESKA PESSTTEEST
     STESSTTTEN SSTGSSSTES SSTEESTVPE SSTQESTPAN TESSSSSSNT NVNNNTNNST
     NNSTNNSTTN NNNNNNTVTP APTPTPTPAP APAPNPSGSV NGAAIVAEAY KYIGTPYVWG
     GKDPSGFDCS GFTRYVYLQV TGRDIGGWTV PQESAGTKIS VSQAKAGDLL FWGSAGGTYH
     VAISLGGGQY IHAPQPGENV KVGSVQWYTP DFAVSM