ID A0AB94IRI7_9BACI Unreviewed; 268 AA.
AC A0AB94IRI7;
DT 02-APR-2025, integrated into UniProtKB/TrEMBL.
DT 02-APR-2025, sequence version 1.
DT 08-OCT-2025, entry version 3.
DE SubName: Full=NLP/P60 protein {ECO:0000313|EMBL:ETI69664.1};
GN ORFNames=BAVI_06359 {ECO:0000313|EMBL:ETI69664.1};
OS Neobacillus vireti LMG 21834.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC Neobacillus.
OX NCBI_TaxID=1131730 {ECO:0000313|EMBL:ETI69664.1, ECO:0000313|Proteomes:UP000018877};
RN [1] {ECO:0000313|EMBL:ETI69664.1, ECO:0000313|Proteomes:UP000018877}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 21834 {ECO:0000313|EMBL:ETI69664.1,
RC ECO:0000313|Proteomes:UP000018877};
RX PubMed=24708037; DOI=10.1111/1462-2920.12478;
RA Mania D., Heylen K., van Spanning R.J., Frostegard A.;
RT "The nitrate-ammonifying and nosZ-carrying bacterium Bacillus vireti is a
RT potent source and sink for nitric and nitrous oxide under high nitrate
RT conditions.";
RL Environ. Microbiol. 16:3196-3210(2014).
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:ETI69664.1}.
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DR EMBL; ALAN01000045; ETI69664.1; -; Genomic_DNA.
DR RefSeq; WP_024027484.1; NZ_ALAN01000045.1.
DR Proteomes; UP000018877; Unassembled WGS sequence.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR Gene3D; 2.10.270.10; Cholin Binding; 1.
DR Gene3D; 3.90.1720.10; endopeptidase domain like (from Nostoc punctiforme); 1.
DR Gene3D; 2.20.120.10; Multimodular pneumococcal cell wall endolysin, domain 3; 1.
DR InterPro; IPR018337; Cell_wall/Cho-bd_repeat.
DR InterPro; IPR000064; NLP_P60_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR051202; Peptidase_C40.
DR PANTHER; PTHR47053; MUREIN DD-ENDOPEPTIDASE MEPH-RELATED; 1.
DR PANTHER; PTHR47053:SF1; MUREIN DD-ENDOPEPTIDASE MEPH-RELATED; 1.
DR Pfam; PF01473; Choline_bind_1; 1.
DR Pfam; PF19085; Choline_bind_2; 1.
DR Pfam; PF19127; Choline_bind_3; 1.
DR Pfam; PF00877; NLPC_P60; 1.
DR SUPFAM; SSF69360; Cell wall binding repeat; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS51170; CW; 2.
DR PROSITE; PS51935; NLPC_P60; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000018877};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807}.
FT DOMAIN 28..148
FT /note="NlpC/P60"
FT /evidence="ECO:0000259|PROSITE:PS51935"
FT REPEAT 170..189
FT /note="Cell wall-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT REPEAT 190..209
FT /note="Cell wall-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
SQ SEQUENCE 268 AA; 29170 MW; 4CD8FE9625ED4829 CRC64;
MKKLVISGLL SCSLLLSGLI GGQKTEAASV GDKVADIALD YIGVPYEWGG SSPSGFDCSG
FTSYTYKQAG FTLPRTAADQ YTKGQAVSKG NLTKGDLVFF STYKAGASHV GISLGGEKFV
HASSNGVKIS SLSESYYTST YIGSKRIDNG KTGWVLSGGK WYYYNAGAMK TGWQKDGNTW
YYMNSNGVMQ IDWIKSGGTW YYLNSNGAMK TGWLFWKNQW YHLGASGAMT TDWLYSGSQW
YFLNSDGSMA KDTTIDGYVI GSDGVWIK
//
