ID   A0A127VIT0_9SPHI        Unreviewed;       567 AA.
AC   A0A127VIT0;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Carboxyl-terminal protease {ECO:0000313|EMBL:AMQ01234.1};
GN   ORFNames=AY601_4391 {ECO:0000313|EMBL:AMQ01234.1};
OS   Pedobacter cryoconitis.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pedobacter.
OX   NCBI_TaxID=188932 {ECO:0000313|EMBL:AMQ01234.1, ECO:0000313|Proteomes:UP000071561};
RN   [1] {ECO:0000313|EMBL:AMQ01234.1, ECO:0000313|Proteomes:UP000071561}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PAMC 27485 {ECO:0000313|EMBL:AMQ01234.1,
RC   ECO:0000313|Proteomes:UP000071561};
RA   Lee J., Kim O.-S.;
RT   "Complete genome sequence of Pedobacter cryoconitis PAMC 27485.";
RL   Submitted (MAR-2016) 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; CP014504; AMQ01234.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A127VIT0; -.
DR   KEGG; pcm:AY601_4391; -.
DR   PATRIC; fig|188932.3.peg.4551; -.
DR   Proteomes; UP000071561; Chromosome.
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, ECO:0000313|EMBL:AMQ01234.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000071561};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW   ECO:0000256|RuleBase:RU004404}.
FT   DOMAIN          86..151
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
SQ   SEQUENCE   567 AA;  62792 MW;  4563EA88D4C48176 CRC64;
     MPMKRNKFAL LFALIAFASF TWSFKEDLFL VSKNMDIFAS LYREININYV DETNAGDLMK
     TGIDAMLDTL DPYTTYIPES EVEDYKLKYV STQFGGIGVS TVFIEGKLFV NEVSADYPAF
     KLGVQPGDQL VKINGIEVKG KERAEVSRLL RGPRGSAVDL LLVRAGTVIQ KQLVRDEIKQ
     LNVSYSGMIG DLAYIRLDKF LENSAQEVQD AAVELNKQHP KGMILDLRYN GGGILQEAVK
     IVNLFVNKDL VVVTQKGRNP EKTINYKTSN LPLLPDLPLV VLINGSSASA SEIVAGALQD
     LDRGVIIGQR SYGKGLVQQT FNLPYNSLVK VTVAKYFTPS GRCIQAVDYA HKNKEGKNVK
     IADSLIAKYK TKTGRSVYNG SGVYPDVEVG TIKLSPITIS LISKSMFFDF ANAYKKSHAT
     ISAASDFRVS EEDYTAFANS LDGKDYAYTS TAERLLSELR TEAEKEQKLG LVKTDLEDLK
     AKMLVAKKTE IFTHKAEIKR MLETQIVSRY YFEKGKIVQA FQYDKELEAA KSVLGNSTKM
     LAILKGEGTY KTIGDPAKVI ATPADSN
//