ID A0A3R8ZMW4_9GAMM Unreviewed; 467 AA.
AC A0A3R8ZMW4;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=S41 family peptidase {ECO:0000313|EMBL:RRU15136.1};
GN ORFNames=EGJ34_09680 {ECO:0000313|EMBL:RRU15136.1};
OS Stenotrophomonas sp. 278.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas.
OX NCBI_TaxID=2479851 {ECO:0000313|EMBL:RRU15136.1, ECO:0000313|Proteomes:UP000274083};
RN [1] {ECO:0000313|EMBL:RRU15136.1, ECO:0000313|Proteomes:UP000274083}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=278 {ECO:0000313|EMBL:RRU15136.1,
RC ECO:0000313|Proteomes:UP000274083};
RA D'Souza A.W., Potter R.F., Wallace M., Shupe A., Patel S., Sun S., Gul D.,
RA Kwon J.H., Andleeb S., Burnham C.-A.D., Dantas G.;
RT "Transmission dynamics of multidrug resistant bacteria on intensive care
RT unit surfaces.";
RL Submitted (OCT-2018) 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:RRU15136.1}.
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DR EMBL; RHPP01000045; RRU15136.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3R8ZMW4; -.
DR OrthoDB; 9812068at2; -.
DR Proteomes; UP000274083; 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; 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.
DR PROSITE; PS50106; PDZ; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU004404};
KW Protease {ECO:0000256|RuleBase:RU004404};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU004404}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..467
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018582484"
FT DOMAIN 96..163
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 374..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 467 AA; 48873 MW; A45A783AA6A66DE2 CRC64;
MRVARSATLL LALLPALTWA QQTAPAAQSG SDAATSEEAV TSRIPLEEIR RYVGVYNAVR
AAYVDPVDDK KLMQSAIRGL LLDLDPHSTY FDKEDAEAFD EQAEGAYEGI GVELQQQPDN
ASLKVIAPID DTPASKAGIL AGDLIIAIDG KPISAIEATE PLRGKAGSKV VLTIVREGKA
KPFDVPITRQ TIRVTSVRSR LLEPGYGYVR LSTFQADTGA DFQKHVTQLQ KQSGGQLKGL
VLDLRSNPGG LLTAAVQVAD DLLEKGNIVS TRGRISISDA RFDATPGDLL KGAPVVVLTD
AGSASASEVL AGALRDNGRA RVVGSRTFGK GSVQTVLPLD NGDSVKLTTA RYYTPSGKSI
QATGIVPDVV LLPEKKDGDD DLPASLSDYS EATLPGHLRG DDEGGEGYAA GDVLPGDGPI
NDALAELKQP GSVAAKQKAE AAKKPAVEAK PAVEPKPAAE PKPAPNP
//
