ID A0A1L3JJQ0_9FLAO Unreviewed; 706 AA.
AC A0A1L3JJQ0;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Tail-specific protease {ECO:0000313|EMBL:APG65337.1};
GN ORFNames=LPB136_08225 {ECO:0000313|EMBL:APG65337.1};
OS Tenacibaculum todarodis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Tenacibaculum.
OX NCBI_TaxID=1850252 {ECO:0000313|EMBL:APG65337.1, ECO:0000313|Proteomes:UP000181898};
RN [1] {ECO:0000313|EMBL:APG65337.1, ECO:0000313|Proteomes:UP000181898}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LPB0136 {ECO:0000313|EMBL:APG65337.1,
RC ECO:0000313|Proteomes:UP000181898};
RA Kim E., Yi H.;
RT "Tenacibaculum sp. LPB0136, isolated from marine environment.";
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; CP018155; APG65337.1; -; Genomic_DNA.
DR RefSeq; WP_072555863.1; NZ_CP018155.1.
DR AlphaFoldDB; A0A1L3JJQ0; -.
DR STRING; 1850252.LPB136_08225; -.
DR KEGG; ten:LPB136_08225; -.
DR OrthoDB; 9812068at2; -.
DR Proteomes; UP000181898; Chromosome.
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 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 InterPro; IPR020992; Tail_Prtase_C.
DR InterPro; IPR040573; TSP_N.
DR NCBIfam; TIGR00225; prc; 1.
DR PANTHER; PTHR32060:SF22; CARBOXYL-TERMINAL-PROCESSING PEPTIDASE 3, CHLOROPLASTIC; 1.
DR PANTHER; PTHR32060; TAIL-SPECIFIC PROTEASE; 1.
DR Pfam; PF11818; DUF3340; 1.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF03572; Peptidase_S41; 1.
DR Pfam; PF17804; TSP_NTD; 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|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU004404};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU004404};
KW Reference proteome {ECO:0000313|Proteomes:UP000181898};
KW Serine protease {ECO:0000256|RuleBase:RU004404};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..706
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011978560"
FT DOMAIN 246..320
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 706 AA; 81250 MW; 52D1ACC7C395162A CRC64;
MKTKLTTIYI LLLTVFASSF TTNANTKKDP DKDKVIIYVL KNILTRGHYV QKELNDDFSE
HVYNSFIDGL DPSKRYFTQD DLKEFSQFKY EIDNQLLDNK IDFYKLVYGR FLEKMKSAKT
YYGVLLTQSF DFSKKESIDI DYDKMPFAKN ENELVDYWRK QLKLQVLSNI ENLQDLQVEK
TKKDPKTVQK TFEDFEHEAR TKVLKNMDDL YLRIEELEHA DWYSTFLNSV VSGFGPHTTY
MSPRSKSRFD QDMSGKLEGI GARLQKKGIY THIFELVSGG PAWKQGELEA GDIILKVAQG
EEEPLDIVGM RLDDAIKFIK GPKGTEVRLT VKKKIDGSTK VISITRDVVE LEETFVKSSI
VEKDGKKYGI INLPKFYIDF SDTNGRDSAK DMEQEIARLQ SEGVEGLIVD LRNNGGGSLK
TAIEIGGLFI NEGPIVQVKY RGEQPIIKKD TDPKIQWNGP LVVMVNEFSA SASEIFAAAM
QDYKRGVILG GKQTYGKGTV QNILPINRFA QNYPDDLGAI KMTIQKFYRI NGGSTQIEGV
YSDIAMPDRY SYMEVGERDL EGALPWDKVA QAKYTQTNSY ENFNDVLYNS KNRINSDSKF
KMINEYAKWL KANQERTTYS LNYKDFLAES KKQDKSGDQF KEVFKFDSNL KFLSPKYEFD
LFKKDSVLED KRMAWHKNLS KDIYVNEALN VLSELKMNRN LEPVKN
//