ID   A0A238X8I7_9PSEU        Unreviewed;       447 AA.
AC   A0A238X8I7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=Cell wall-associated hydrolase, NlpC family {ECO:0000313|EMBL:SNR55020.1};
GN   ORFNames=SAMN06265360_109161 {ECO:0000313|EMBL:SNR55020.1};
OS   Haloechinothrix alba.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Haloechinothrix.
OX   NCBI_TaxID=664784 {ECO:0000313|EMBL:SNR55020.1, ECO:0000313|Proteomes:UP000198348};
RN   [1] {ECO:0000313|EMBL:SNR55020.1, ECO:0000313|Proteomes:UP000198348}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45207 {ECO:0000313|EMBL:SNR55020.1,
RC   ECO:0000313|Proteomes:UP000198348};
RA   Kim H.J., Triplett B.A.;
RL   Submitted (JUN-2017) 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; FZNW01000009; SNR55020.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A238X8I7; -.
DR   Proteomes; UP000198348; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase 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   PANTHER; PTHR47053; MUREIN DD-ENDOPEPTIDASE MEPH-RELATED; 1.
DR   PANTHER; PTHR47053:SF1; MUREIN DD-ENDOPEPTIDASE MEPH-RELATED; 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   Hydrolase {ECO:0000313|EMBL:SNR55020.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198348}.
FT   DOMAIN          309..447
FT                   /note="NlpC/P60"
FT                   /evidence="ECO:0000259|PROSITE:PS51935"
FT   REGION          34..76
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          100..150
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          188..309
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        50..76
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        105..134
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        188..284
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        288..309
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   447 AA;  48334 MW;  87968CA3CCD8310B CRC64;
     MLVAKRSRGE RGRSVRGLVA AAATALVVAV GMPATAGAVP PPPPNPSDSE LEQSRERERE
     HAGEVGELTN ELAEAEDRLS QARAEVARKE ELVNKAQVDL ASAEEAAAEA ERAAERAQRD
     SERAAEDLEA ARQRADEFIS GSYQQGSTVG SVTAYVGSSS REELLAREQL LGAMGDSEGE
     ALEGVRAARV DKSNADAAAR EAAEIAEQRQ REAEEAAHAA EAAYEDAVEA RSSQAERTER
     LEAERDEVAE RLYEAQSRVS DLEGQRQRYE DWREEKRREE EKQAQQAALA AAESSGSSGG
     QAQQAQSSNV SVETVVQRAK SQLGVPYAWG GGNTQGPTRG VRDGGVADAH GDYKKIGFDC
     SGLMVYAFAP HRTLAKYSGY QYDEGRKVPL SQKRRGDLLF WGTQGIHHVA MYLGNGQMIE
     APQSGGHVRI VPVRYGDILP YATRVIE
//