ID A0A269PTX2_9GAMM Unreviewed; 403 AA.
AC A0A269PTX2;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Peptidase S41 {ECO:0000313|EMBL:PAJ75852.1};
GN ORFNames=CJF42_03170 {ECO:0000313|EMBL:PAJ75852.1};
OS Pseudoalteromonas sp. NBT06-2.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=2025950 {ECO:0000313|EMBL:PAJ75852.1, ECO:0000313|Proteomes:UP000215836};
RN [1] {ECO:0000313|EMBL:PAJ75852.1, ECO:0000313|Proteomes:UP000215836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBT06-2 {ECO:0000313|EMBL:PAJ75852.1,
RC ECO:0000313|Proteomes:UP000215836};
RA Wei Y.;
RT "Pseudoalteromonas hadalis sp. nov., a facultative psychrophile isolated
RT from New Britain Trench.";
RL Submitted (AUG-2017) 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:PAJ75852.1}.
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DR EMBL; NQMR01000007; PAJ75852.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A269PTX2; -.
DR OrthoDB; 9812068at2; -.
DR Proteomes; UP000215836; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000215836};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU004404}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..403
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013057612"
FT DOMAIN 86..166
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 403 AA; 43890 MW; DBA6243915BE73C3 CRC64;
MRISLKFNQF LSFCIICLSL SFSPICLAEV SSKLNNVNMK HILEHIQTFY VDEVNTNKLN
SSAVDSVLKQ LDPYSEYLNE QELEDLFNIT NGQYTGLGIE VEMRDEHIVI IASLNNSPAA
QAGLQQGDIL LSINGQTVIN EPIKQVANLI SKTKNTTVSL SIARSGFSTP LRFEVERQLI
ELETVTSKVD CAGYAYLRII SFNNHTLHDV ARHIAKLKTE NGQPLKGLLI DLRDNPGGIL
DSAVAISDLF LKDGIIVSTK GRFYDANKIF TANNSDILNG APMVVLINKG SASAAEILAG
ALKDNKRATV VGTRSYGKGS VQSLIPLGNG QTALKLTTAK YYTPSGTSID GIGITPDIPI
TQSSIPKSDK IAIMNLNKGI ENQVFTSTFK DVQLAKAQKI LEQ
//
