ID A0A1V9US78_9PSED Unreviewed; 704 AA.
AC A0A1V9US78;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Tail-specific protease {ECO:0000313|EMBL:OQR32803.1};
GN ORFNames=BWR59_12685 {ECO:0000313|EMBL:OQR32803.1};
OS Pseudomonas sp. Bc-h.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1943632 {ECO:0000313|EMBL:OQR32803.1, ECO:0000313|Proteomes:UP000192462};
RN [1] {ECO:0000313|EMBL:OQR32803.1, ECO:0000313|Proteomes:UP000192462}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bc-h {ECO:0000313|EMBL:OQR32803.1,
RC ECO:0000313|Proteomes:UP000192462};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-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:OQR32803.1}.
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DR EMBL; MUIN01000006; OQR32803.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V9US78; -.
DR STRING; 1943632.BWR59_12685; -.
DR OrthoDB; 9812068at2; -.
DR Proteomes; UP000192462; 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; 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 InterPro; IPR020992; Tail_Prtase_C.
DR InterPro; IPR040573; TSP_N.
DR NCBIfam; TIGR00225; prc; 1.
DR PANTHER; PTHR32060; TAIL-SPECIFIC PROTEASE; 1.
DR PANTHER; PTHR32060:SF32; 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|RuleBase:RU004404};
KW Protease {ECO:0000256|RuleBase:RU004404, ECO:0000313|EMBL:OQR32803.1};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU004404}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..38
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 39..704
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013320328"
FT DOMAIN 251..327
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 628..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 704 AA; 78703 MW; C8CF526D3423E474 CRC64;
MRYQLSPRRI SMKQILPSTT LALLIGLAAL PMSSSSFAAN SWDNLQPDRD EVIASLNVVE
LLKRHHYSKP PLDDKRSEII YQSYLKLLDP ARSYFLASDI AEFDKWRFQF DDFLKSGDLN
PGFTIYKRYL DRIKSRLDFA LAQLSKGVDK IDLNTQETLL VDRKDAPWPK NEAELDDLWR
KRVKDEVLRL KIAGKDPAKI QETLTKRYKN QLARLGQTRS EDIFQAYLNT FAMSYDPHTN
YLSPDSAENF DINMSLSLEG IGAVLQSDND NVKIVRLVPA GPAAKTKQVA TADKIIGVAQ
GDKEMVDVIG WRLDEVVKLI RGPKGSVVRL EIIPASNAPN DQTTKIVSIT REAVKLEEQA
AKKSVLHLNQ DGKDYKLGVI EIPAFYLDFK AYRAGDPEYK STTRDVKKLL TELQSEKVDG
VVIDLRNNGG GSLQEATELT SLFIDKGPTV LVRNADGKVD VLEDENSGAF YKGPMALLVN
RLSASASEIF AGAMQDYHRA LIIGGQTFGK GTVQTIQPLN HGELKLTLAK FYRVSGQSTQ
HQGVLPDIAY PSIIDTKEIG ESALPEAMTY DTIKPAIKPA VDPFKPFLAQ LQSRHDVRSA
KDAEFVFVEQ KLALAKKLMS EKTVSLNEAE RRTEHADVES KQLVMENTRR KAKGEEPLKE
LKKEDEDALP VDDDKTKPED DAYLSETGRI LIDYLGLSGS VAKK
//
