ID A0A2S2DWF9_9BACT Unreviewed; 709 AA.
AC A0A2S2DWF9;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=C-terminal processing peptidase {ECO:0000313|EMBL:AWL09706.1};
DE EC=3.4.21.102 {ECO:0000313|EMBL:AWL09706.1};
GN Name=ctpA {ECO:0000313|EMBL:AWL09706.1};
GN ORFNames=HME7025_01855 {ECO:0000313|EMBL:AWL09706.1};
OS Aquirufa nivalisilvae.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae; Aquirufa.
OX NCBI_TaxID=2516557 {ECO:0000313|EMBL:AWL09706.1, ECO:0000313|Proteomes:UP000245468};
RN [1] {ECO:0000313|Proteomes:UP000245468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HME7025 {ECO:0000313|Proteomes:UP000245468};
RA Kim H., Kang H., Joh K.;
RT "Pseudarcicella sp. HME7025 Genome sequencing and assembly.";
RL Submitted (MAY-2018) 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; CP029346; AWL09706.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S2DWF9; -.
DR KEGG; psez:HME7025_01855; -.
DR OrthoDB; 9812068at2; -.
DR Proteomes; UP000245468; Chromosome.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
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; 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, ECO:0000313|EMBL:AWL09706.1};
KW Protease {ECO:0000256|RuleBase:RU004404};
KW Reference proteome {ECO:0000313|Proteomes:UP000245468};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU004404}.
FT DOMAIN 243..320
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 634..677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..648
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 661..677
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 709 AA; 80129 MW; 80F51C2DAE133BDE CRC64;
MKKILPILIP LSLLVVLFLH GKNQTSFPST KSVVYQEGDL QPTETQRKVE RLVFGILSNY
HYRKIPVNDS LSSKIYDAYL KELDPNKVFF LASDIDELEK YRLTIDDQLN DGDLTSAFAI
YNRYQQRMKE RYAYIDQILQ KIPDFTVDET YQPGREKVKY AASKEELNDF WRKDVKRQLL
DWRISGKADT TALRELKERY KRSEKYLART RSEDVFQVFM NAYTESIDPH TSYMIPRTAQ
AFNTDMAQSF EGIGATLRLE GDYVTIQDLI PGGPAFRSKQ INPKDRIIGV AQGDDGSYVD
VIGWFTDDAV KLIRGPKNTV VRLKLLPAGA GTGSPGTEVR LVREKIKLEE QTAKKEILTY
NQGDKKIKLG LITIPMFYRD FEGARKRESD FKSTSADVKK FLTEFKTEGV DGLIIDLRNN
GGGSLIEAVD LTGLFIPKGP VVQRKQSDGK ITQEVDRDPE QFYDGPMAVL INRFSASASE
IFAAAIQDYK RGIIVGEQSY GKGTVQSVVD LDNYMNNEKE PVGQLKITLE KFYRINGSST
QHKGVSPDFA LPSAFSAEEF GESSQPSALP WDMISPTNYQ ITSNINPGLI NKMQTSFQAR
LKSKPDLIKL KDDFERWKKI KELNSISLQI DKRKKELDDQ KKKPDESQAV MDNIAGSAAD
TPEGDKDKKA STADKHAKDV YLKETQQLLA DWVLGPLPTK VAAKPSAKK
//
