ID A0A1G5AIS2_9CLOT Unreviewed; 466 AA.
AC A0A1G5AIS2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Carboxyl-terminal processing protease {ECO:0000313|EMBL:SCX77798.1};
GN ORFNames=SAMN03080606_00156 {ECO:0000313|EMBL:SCX77798.1};
OS Alkaliphilus peptidifermentans DSM 18978.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Alkaliphilus.
OX NCBI_TaxID=1120976 {ECO:0000313|EMBL:SCX77798.1, ECO:0000313|Proteomes:UP000198636};
RN [1] {ECO:0000313|EMBL:SCX77798.1, ECO:0000313|Proteomes:UP000198636}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18978 {ECO:0000313|EMBL:SCX77798.1,
RC ECO:0000313|Proteomes:UP000198636};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S41A family.
CC {ECO:0000256|ARBA:ARBA00009179, ECO:0000256|RuleBase:RU004404}.
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DR EMBL; FMUS01000001; SCX77798.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G5AIS2; -.
DR STRING; 1120976.SAMN03080606_00156; -.
DR OrthoDB; 9812068at2; -.
DR Proteomes; UP000198636; 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: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 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, ECO:0000313|EMBL:SCX77798.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198636};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU004404}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..466
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011443076"
FT DOMAIN 92..151
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 466 AA; 52458 MW; 33E3A37EA0CA7205 CRC64;
MTRPSNWKKQ LAVIAAMVMV MVFLTTPFTY ADDYGDYILE GLKDVILQKF VDPLKYEDLK
GDTPQEIFDN LDIHSEYYTR EEFDAFLDQI MGEFSGIGAY IEEKEGKVYI DETIDDSPAK
KAGLKAGDEI YTVDSIPTKG MTVQEAVNLI RGEEGTKVTL EIKRAGIDKI LKYTITRAVI
ESNPIQWETI DGIGYIKIDS FNEKASNNFS KAVTNMKEEK IDKIIVDVRD NPGGSLDEVV
NISRLLVPKG PVVFVDFRSY KLTYSSFLSK PIFEDIVVLT SEGSASASEI LAAAVQDTKA
GVVVGKTTYG KGSVQRLYGM FNGDGYKITE ARYLSPNKTI IDGVGVIPDY EVERYPEEFH
VEKLLPLSLV ETLNKEDNND TVLAIQQRLR IIGYEITDED GWYGESTQKA VEAFAKGHGI
KTTQLTPEMQ FDIDFVFRLT VSNKKMTNSY NLHWTTLKIK ILKQQQ
//
