ID A0A1W2C5H1_9SPHI Unreviewed; 526 AA.
AC A0A1W2C5H1;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Carboxyl-terminal processing protease {ECO:0000313|EMBL:SMC80459.1};
GN ORFNames=SAMN04488101_103155 {ECO:0000313|EMBL:SMC80459.1};
OS Pedobacter nyackensis.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=475255 {ECO:0000313|EMBL:SMC80459.1, ECO:0000313|Proteomes:UP000192678};
RN [1] {ECO:0000313|EMBL:SMC80459.1, ECO:0000313|Proteomes:UP000192678}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19625 {ECO:0000313|EMBL:SMC80459.1,
RC ECO:0000313|Proteomes:UP000192678};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) 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; FWYB01000003; SMC80459.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W2C5H1; -.
DR STRING; 475255.SAMN04488101_103155; -.
DR OrthoDB; 9812068at2; -.
DR Proteomes; UP000192678; 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.
DR PROSITE; PS50106; PDZ; 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:SMC80459.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000192678};
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 9..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 96..147
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 526 AA; 58737 MW; C79F93F46EBB92B5 CRC64;
MKKSTCHNLL IALTYSVTLI GGMFFGYKFL KDQGFQFQRP VQFASNEHTE KVDEIIHIIN
RNYVDDVNAD SLNHLPIDSL LHELDPHSIY LPPAKANEMT ENLEGNFEGI GIEYYILKDT
LLVTNVVKGG PAHMAGIKQG DKILKIDTLM VSGKALPREQ MIGRIRGRKG TAVKLTIVHP
RDSQQVVFIV NRSRVKVSSI DVAYLLNPET AYIRISKFGA DTDKDFIEAI RSLKSKGMKK
LILDLRDNGG GYLNAATGLA NQILEENKLI VYTEGKHEPR TDYTSSGGGE FEQGKLAVLI
NENSASASEI LAGAVQDWGR GVIIGRRSFG KGLVQEQFPF GDGSALNLTI ARYYTPSGRS
IQKSYKKGYT AYKNEIDDRF NDGELTGDNA SVKDTLKNKN IVRGGIQPDV YVKLDTAGYN
KFYSTLVSKK ILFDFVYDVL ANRYNPVMLN QSIASFSITD TDYKDLLRYA QNRNVVIDQK
QLSVSKSLIY NDVKLLLYKY HLGDAGYYKA LNLSDPMIKQ AVSSLQ
//
