ID A0A150M2C1_9BACI Unreviewed; 485 AA.
AC A0A150M2C1;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Carboxyl-terminal protease {ECO:0000313|EMBL:KYD18566.1};
DE EC=3.4.21.102 {ECO:0000313|EMBL:KYD18566.1};
GN ORFNames=B4135_2335 {ECO:0000313|EMBL:KYD18566.1};
OS Caldibacillus debilis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Caldibacillus.
OX NCBI_TaxID=301148 {ECO:0000313|EMBL:KYD18566.1, ECO:0000313|Proteomes:UP000075683};
RN [1] {ECO:0000313|EMBL:KYD18566.1, ECO:0000313|Proteomes:UP000075683}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4135 {ECO:0000313|EMBL:KYD18566.1,
RC ECO:0000313|Proteomes:UP000075683};
RA Berendsen E.M., Wells-Bennik M.H., Krawcyk A.O., De Jong A., Holsappel S.,
RA Eijlander R.T., Kuipers O.P.;
RT "Draft Genome Sequences of Seven Thermophilic Sporeformers Isolated from
RT Foods.";
RL Submitted (JAN-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:KYD18566.1}.
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DR EMBL; LQYT01000050; KYD18566.1; -; Genomic_DNA.
DR RefSeq; WP_061569073.1; NZ_LQYT01000050.1.
DR AlphaFoldDB; A0A150M2C1; -.
DR STRING; 301148.B4135_2335; -.
DR PATRIC; fig|301148.3.peg.3839; -.
DR OrthoDB; 9812068at2; -.
DR Proteomes; UP000075683; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
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; 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; PF13180; PDZ_2; 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, ECO:0000313|EMBL:KYD18566.1};
KW Protease {ECO:0000256|RuleBase:RU004404, ECO:0000313|EMBL:KYD18566.1};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU004404}.
FT DOMAIN 94..170
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 485 AA; 54242 MW; BCFE0EA15B774D1E CRC64;
MSKRKVLILL LISMVLSASA TYFFLNWRWE ERVREQQDLL EIPEGGAQEN QDHLEKIGNA
FHLIKTQYVG EVNEEKLTEG AIQGMLTVLN DPYSVYMNRE EASRFSESLD SSFEGIGAEI
TKIDGKIIIV SPLKNSPAEK AGLKPYDQIL KVDGADVTNK ELNEVTLKIR GKKGTKVVLE
ILRNGLEKPI SVEVKRDTIP IETVYSSLEE ANGKKIGYIE ITSFSRDTGE EFADHLKKLE
RKKIAGLIID VRGNPGGLLT SVEEIASQLI TGDKPIVQIE KKDGERETIF SKLKKRKGYP
IAVLTDEGSA SASEILAAAL KEGEGYPVIG ERTFGKGTVQ QQISLGDGSN MKLTMYKWLT
PNGNWIHGKG IEPDVEVEQP ALFHLQPLQL KGILKRDMND EQIKQAQFIL KELGYEPGRT
DGYFDETTEA AVKVFQHDNR LPETGVIDGK TAKAMEKVIL EEKENKANDR QLKTSLKYLS
YMAEK
//
