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Database: UniProt
Entry: A0A069RPS9_PEPLI
LinkDB: A0A069RPS9_PEPLI
Original site: A0A069RPS9_PEPLI 
ID   A0A069RPS9_PEPLI        Unreviewed;       464 AA.
AC   A0A069RPS9;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Carboxy-terminal processing protease CtpB {ECO:0000313|EMBL:KDR96172.1};
DE            EC=3.4.21.102 {ECO:0000313|EMBL:KDR96172.1};
GN   Name=ctpB {ECO:0000313|EMBL:KDR96172.1};
GN   ORFNames=CLIT_4c00090 {ECO:0000313|EMBL:KDR96172.1};
OS   Peptoclostridium litorale DSM 5388.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Peptoclostridium.
OX   NCBI_TaxID=1121324 {ECO:0000313|EMBL:KDR96172.1, ECO:0000313|Proteomes:UP000027946};
RN   [1] {ECO:0000313|EMBL:KDR96172.1, ECO:0000313|Proteomes:UP000027946}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W6 {ECO:0000313|EMBL:KDR96172.1,
RC   ECO:0000313|Proteomes:UP000027946};
RA   Poehlein A., Jagirdar A., Khonsari B., Chibani C.M.,
RA   Gutierrez Gutierrez D.A., Davydova E., Alghaithi H.S., Nair K.P.,
RA   Dhamotharan K., Chandran L., G W., Daniel R.;
RT   "Genome sequence of Clostridium litorale W6, DSM 5388.";
RL   Submitted (MAR-2014) 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:KDR96172.1}.
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DR   EMBL; JJMM01000004; KDR96172.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A069RPS9; -.
DR   STRING; 1121324.CLIT_4c00090; -.
DR   eggNOG; COG0793; Bacteria.
DR   Proteomes; UP000027946; Unassembled WGS sequence.
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   Gene3D; 3.30.750.44; -; 1.
DR   Gene3D; 1.10.101.10; PGBD-like superfamily/PGBD; 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; IPR002477; Peptidoglycan-bd-like.
DR   InterPro; IPR036365; PGBD-like_sf.
DR   InterPro; IPR036366; PGBDSf.
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   Pfam; PF01471; PG_binding_1; 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   SUPFAM; SSF47090; PGBD-like; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|RuleBase:RU004404, ECO:0000313|EMBL:KDR96172.1};
KW   Protease {ECO:0000256|RuleBase:RU004404, ECO:0000313|EMBL:KDR96172.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027946};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW   ECO:0000256|RuleBase:RU004404}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           31..464
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5039220342"
FT   DOMAIN          98..170
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|SMART:SM00228"
FT   DOMAIN          170..356
FT                   /note="Tail specific protease"
FT                   /evidence="ECO:0000259|SMART:SM00245"
SQ   SEQUENCE   464 AA;  49923 MW;  5C56807C50AFF1DE CRC64;
     MQNMKVNKMI SKCTAFAVAA VMAASGISYA QQDIEKDMEF FNATKNYIIK NYAADEISEE
     ELIDAAVKGM FDALDKHSVY LDAEQNQQFS EEVEGSFTGI GALIGVRDGN VTILEPIEDS
     PAVEAGLLPG DIIRAIEGEE ITDTENLKEI VDRIRGEEGT SVNLTIERRG RRFDVSVKRG
     QVELNPVKYR ELGNGIGYIK LSEFSKVSIK NMGKAVNELK SQGNNKLVLD LRGNPGGGLV
     DVVAIAQDFV PKGKVVTIKY KNGSESSYPS YGTPVFSKVA VLVDRGSASA SEILAGAIQD
     SKSGVLIGEN TYGKGTVQKL LPLKNGEAIK LTIAKYVLPS GRSIDQTGLV PDIEAGRFAD
     EVVDIGEMTP FETDHAMKKG DAGLDVLALQ ERLQLLGYEI SDPQGIYGDS TAAGVVAYQG
     KVEMPQSGEA SAETLSSLSG DFSKFMLSDD MDNQLKAALE YLGK
//
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