ID A0A135L7X9_9BACI Unreviewed; 475 AA.
AC A0A135L7X9;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Peptidase S41 {ECO:0000313|EMBL:KXG45079.1};
GN ORFNames=U473_10690 {ECO:0000313|EMBL:KXG45079.1};
OS Tepidibacillus decaturensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Tepidibacillus.
OX NCBI_TaxID=1413211 {ECO:0000313|EMBL:KXG45079.1, ECO:0000313|Proteomes:UP000070352};
RN [1] {ECO:0000313|EMBL:KXG45079.1, ECO:0000313|Proteomes:UP000070352}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Z9 {ECO:0000313|EMBL:KXG45079.1,
RC ECO:0000313|Proteomes:UP000070352};
RA Dong Y., Chang J.Y., Sanford R., Fouke B.W.;
RT "Draft Genome for Tepidibacillus decaturensis nov. sp. Strain Z9, an
RT Anaerobic, Moderately Thermophilic and Heterotrophic Bacterium from Deep
RT Subsurface of the Illinois Basin, USA.";
RL Submitted (FEB-2016) 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:KXG45079.1}.
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DR EMBL; LSKU01000001; KXG45079.1; -; Genomic_DNA.
DR RefSeq; WP_068727634.1; NZ_LSKU01000001.1.
DR AlphaFoldDB; A0A135L7X9; -.
DR STRING; 1413211.U473_10690; -.
DR OrthoDB; 9812068at2; -.
DR Proteomes; UP000070352; 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 Gene3D; 1.10.101.10; PGBD-like superfamily/PGBD; 1.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR004447; Peptidase_S41A.
DR InterPro; IPR002477; Peptidoglycan-bd-like.
DR InterPro; IPR036365; PGBD-like_sf.
DR InterPro; IPR036366; PGBDSf.
DR InterPro; IPR005151; Tail-specific_protease.
DR NCBIfam; TIGR00225; prc; 1.
DR PANTHER; PTHR32060:SF29; CARBOXY-TERMINAL PROCESSING PROTEASE CTPB; 1.
DR PANTHER; PTHR32060; TAIL-SPECIFIC PROTEASE; 1.
DR Pfam; PF17820; PDZ_6; 1.
DR Pfam; PF03572; Peptidase_S41; 1.
DR Pfam; PF01471; PG_binding_1; 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 SUPFAM; SSF47090; PGBD-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 Reference proteome {ECO:0000313|Proteomes:UP000070352};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU004404}.
FT DOMAIN 98..162
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 475 AA; 51687 MW; C892B87191CD0074 CRC64;
MVKGRTLLIL LVLSIVLSSL VTAMVVDGNG IVINQPSGTE SVPKEMNKLV DVYQTILQSY
VEKKNGNELI DGAIRGMVQS LNDPHSTYMD AKESKDFFGS LNDSFEGIGT EVTIENGKIT
VIAPIKGSPS EKAGIRPRDQ IIKVNGESLE GLNLIEAVSK IRGPKGTKAV LEIVRPGIEA
PIEITVIRDE IPIETVYSST ISSKKGTLGK IEITNFGENT AAEFKKALKD LESKGIKGLI
IDVRGNPGGY LQSVLEIGNL VVPNKGIIVQ VEDRNKKREQ YHSEMEQPSY PIVSLINGGS
ASAAEILVAA LQEAGHYPVV GEPSFGKGTV QNPFELSDGS NVKLTVAKWL TPNGNWIHQK
GIQPDVKMEQ PEYFHAAPFP EDIQLKRDTN SNDVKNLQII LNGLGYKTGR TDGYFDQETV
LAVQAFQKAN GLKASGVVDQ VTANKLQDKI IERIRDPKND LQLQVAIETL LKAIK
//
