ID A0A3D9IEW2_9BACL Unreviewed; 474 AA.
AC A0A3D9IEW2;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Carboxyl-terminal processing protease {ECO:0000313|EMBL:RED60322.1};
GN ORFNames=DFP95_106111 {ECO:0000313|EMBL:RED60322.1};
OS Cohnella lupini.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Cohnella.
OX NCBI_TaxID=1294267 {ECO:0000313|EMBL:RED60322.1, ECO:0000313|Proteomes:UP000256869};
RN [1] {ECO:0000313|EMBL:RED60322.1, ECO:0000313|Proteomes:UP000256869}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8236 {ECO:0000313|EMBL:RED60322.1,
RC ECO:0000313|Proteomes:UP000256869};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (JUL-2018) 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:RED60322.1}.
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DR EMBL; QRDY01000006; RED60322.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3D9IEW2; -.
DR Proteomes; UP000256869; 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; IPR041489; PDZ_6.
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; PF17820; PDZ_6; 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, ECO:0000313|EMBL:RED60322.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000256869};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU004404}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..474
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038907244"
FT DOMAIN 84..148
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 474 AA; 50919 MW; 5BC30B3F8176D0B3 CRC64;
MNPFKRFKFI LSLLLALALL GAYAPNVLGA SADQVEEVRE LLEQYHLSKP DDDDLNEPEI
DAMVDSLHDP YTQYFDNEEW DSFNSVLEQK FVGVGIVMAD ADGSVYVDEV ITGSPAEAAG
ILSGDKVVGA NGNSLKGKSV TDIQEALRGL EGTSVTLSVS RNGSDLEFEM KRRAVQIPVV
TTRMLSEGIG YLALSGFTSD SANEVERQLA KLEENGLKSL VFDLRDNGGG YVDAAQAIAN
LFVEKGVLAH MRDRDGNDHP LELDGSTKPY SLYMLVNKNS ASASELLSGA LQDYGVAKLV
GTRTYGKGVV QSLLAVKSGG MLKVTVQEYY TPTGRKVDKI GLVPDLYING AGEQLIGAYR
MAGGNAVTVT SDKGAVAING VRVSLTDALW KDRTIWFVNL KLAASALGAK LTYDSKSRSY
TLARGSEVLA LPTNDYHVRI KDGVSSIDVR MLKKSFSGVA YTASSVGLKL VTAI
//