ID A0A0Q3WNT7_BRECH Unreviewed; 498 AA.
AC A0A0Q3WNT7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Peptidase S41 {ECO:0000313|EMBL:KQL48989.1};
GN ORFNames=AN963_04140 {ECO:0000313|EMBL:KQL48989.1};
OS Brevibacillus choshinensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX NCBI_TaxID=54911 {ECO:0000313|EMBL:KQL48989.1, ECO:0000313|Proteomes:UP000051063};
RN [1] {ECO:0000313|EMBL:KQL48989.1, ECO:0000313|Proteomes:UP000051063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8552 {ECO:0000313|EMBL:KQL48989.1,
RC ECO:0000313|Proteomes:UP000051063};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA Shi H., Pan Z., Liu X.;
RT "Genome sequencing project for genomic taxonomy and phylogenomics of
RT Bacillus-like bacteria.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S41A family.
CC {ECO:0000256|ARBA:ARBA00009179, ECO:0000256|RuleBase:RU004404}.
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:KQL48989.1}.
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DR EMBL; LJJB01000007; KQL48989.1; -; Genomic_DNA.
DR RefSeq; WP_055743285.1; NZ_LJJB01000007.1.
DR AlphaFoldDB; A0A0Q3WNT7; -.
DR STRING; 54911.AN963_04140; -.
DR PATRIC; fig|54911.3.peg.4947; -.
DR OrthoDB; 9812068at2; -.
DR Proteomes; UP000051063; Unassembled WGS sequence.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00988; PDZ_CTP_protease; 1.
DR CDD; cd07560; Peptidase_S41_CPP; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 3.30.750.44; -; 1.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR004447; Peptidase_S41A.
DR InterPro; IPR005151; Tail-specific_protease.
DR NCBIfam; TIGR00225; prc; 1.
DR PANTHER; PTHR32060:SF22; CARBOXYL-TERMINAL-PROCESSING PEPTIDASE 2, CHLOROPLASTIC-RELATED; 1.
DR PANTHER; PTHR32060; TAIL-SPECIFIC PROTEASE; 1.
DR Pfam; PF13180; PDZ_2; 1.
DR Pfam; PF03572; Peptidase_S41; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00245; TSPc; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU004404};
KW Protease {ECO:0000256|RuleBase:RU004404};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU004404}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..498
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006209190"
FT DOMAIN 124..207
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 498 AA; 54716 MW; ED3105F6CB8E73BC CRC64;
MKRLSQWVLA ALLFATAIPV QAAERPYLET EEVFLHVMES HLSKPEAKQL VKGALQAISD
QAEKKQHLSL TVSPEDDTLG EMEQRMAEWQ TKGKWDALTI NTWAIDGMLS TLSDPHSVFF
TSDELRLFQS DVENQFVGFG FRMRMQNNEL ILREIVPGSP AAATVLKRGD QLLKVGEVSL
VGKSFEEAYA YLKGGEGSEA VLTVYRPSEK REFQVKLKRA MLQLPEAEGQ LFSKGSIGYI
SLETFGSDGA IQMRDKLAQF AGSGQPLKGI VLDLRDNGGG YLSTARDIAS LFMEEGLLMY
TTNRNGVEVE TWVRNGHDIG VPVRILVNGG TASASELLSG ALRDHGIAKL VGTKTYGKGS
AQQVIPLSEG DALKLTLNEY FTPKHTVVNH IGLTPDMQVE DYAAQVVEAL HSLNVQTWEL
NDENGDTEIN GVPFPTVDPL FKQAPDGLQI KAAVLQHLLG DSTIGEKDYV ALAPYLKSHP
TLQLQNKNGV NTLTYQTK
//
