ID A0A1M5D896_9FLAO Unreviewed; 523 AA.
AC A0A1M5D896;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Carboxyl-terminal processing protease {ECO:0000313|EMBL:SHF63238.1};
GN ORFNames=SAMN05444344_0884 {ECO:0000313|EMBL:SHF63238.1};
OS Tenacibaculum mesophilum.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Tenacibaculum.
OX NCBI_TaxID=104268 {ECO:0000313|EMBL:SHF63238.1, ECO:0000313|Proteomes:UP000183998};
RN [1] {ECO:0000313|EMBL:SHF63238.1, ECO:0000313|Proteomes:UP000183998}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13764 {ECO:0000313|EMBL:SHF63238.1,
RC ECO:0000313|Proteomes:UP000183998};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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; FQVV01000001; SHF63238.1; -; Genomic_DNA.
DR RefSeq; WP_073182162.1; NZ_FQVV01000001.1.
DR AlphaFoldDB; A0A1M5D896; -.
DR STRING; 104268.SAMN05444344_0884; -.
DR OrthoDB; 9812068at2; -.
DR Proteomes; UP000183998; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU004404};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|RuleBase:RU004404, ECO:0000313|EMBL:SHF63238.1};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU004404}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 99..172
FT /note="PDZ"
FT /evidence="ECO:0000259|SMART:SM00228"
FT DOMAIN 161..363
FT /note="Tail specific protease"
FT /evidence="ECO:0000259|SMART:SM00245"
SQ SEQUENCE 523 AA; 58662 MW; 6D7B4722E87055E5 CRC64;
MNKNNLPIYL SIAVIFGILI GTFFSNGKSS NLIGKSSSSE RKIKRLIDYI QSDYVDAVNT
DDLLDGAIAE MLGKLDPHSV YIPKENLQLV TENMQGNFVG IGVQFRMIGD TITVIEPIKG
GPSIEAGIKA GDRILLADKD TLYGKKLQTS QIMKALKGKP NTKVDLQIYR KTNDSIFNTT
INRGKVNIKS VDIAYMLNDS IGYIKLDRFA RNTYIEFKSS LNKLLTKGMT DLVLDLRGNG
GGFIDIANDI VDEFLEDEKL IVFTKNNKGD IVKSFATDKG DFEHGGLYVL IDENSASASE
IVAGALQDND KGIIIGRRSF GKGLVQQEMD LGDGSAVRLT TARYYTPTGR SIQKPYKKDA
DSEEYSHDFE HRLENGELFT KDSIKTIDSL KYTTPKGKVV YGGGGIIPDY FVAVDTSAYI
PTIFFRPLND FAFSYVDDNR KKLASLTVED FINNFDKDNK ISNKFLAELK DFRLPERTKN
QLRNNLKVLI ARELFSDEGL YKVDQRDDKM LQKVFELEQK QNE
//
