ID A0A1T4X9K4_9BACT Unreviewed; 461 AA.
AC A0A1T4X9K4;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Carboxyl-terminal processing protease {ECO:0000313|EMBL:SKA86270.1};
GN ORFNames=SAMN02745166_01273 {ECO:0000313|EMBL:SKA86270.1};
OS Prosthecobacter debontii.
OC Bacteria; Verrucomicrobiota; Verrucomicrobiae; Verrucomicrobiales;
OC Verrucomicrobiaceae; Prosthecobacter.
OX NCBI_TaxID=48467 {ECO:0000313|EMBL:SKA86270.1, ECO:0000313|Proteomes:UP000190774};
RN [1] {ECO:0000313|EMBL:SKA86270.1, ECO:0000313|Proteomes:UP000190774}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700200 {ECO:0000313|EMBL:SKA86270.1,
RC ECO:0000313|Proteomes:UP000190774};
RA Peterson S.W.;
RL Submitted (FEB-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; FUYE01000003; SKA86270.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T4X9K4; -.
DR STRING; 48467.SAMN02745166_01273; -.
DR OrthoDB; 9812068at2; -.
DR Proteomes; UP000190774; 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, ECO:0000313|EMBL:SKA86270.1};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU004404}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..461
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013092110"
FT DOMAIN 105..185
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 19..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 461 AA; 49777 MW; B750DCB08E301F20 CRC64;
MRFVLVLSLC LAVGHGLRAA PPDESGAAPD KTAAKSKATP PALKPPPEDA YRQMELLTRA
METIRQNYVD ESKITYEELV EGALEGMLRR LDPHCEYMGR SLFEDMQREQ ADTSEGVGIT
VALREGTLTI ITVREDGPAA RAGVLAGDQM VRIGEVLTDS VGVAEAIQLL QGRSGETMKL
TVRRPGTKQF LEFSIVRETL TETSVHDSML LVPKLAGDYK IGYARISQYT HSTAKDLSES
LDELEKAGMQ AFVLDLRNNP GGLLDSAVAV CGEFLPEGTV VVTTEGRIAS QNPPPYRTPV
RDGKKPRRYP MAVLVNHGSA SAAEITAGAL QDLKRAIVVG TTSFGKGSVQ SILPMKNGAA
MRLTTAKYYT PSHRTIHEHG VEPNIVSVLT TDEEMKVAKW RNSHGTGEAA AIEIANLGDK
QLERAVDALK GVLVFDTFQA KAAPVAPPDV PRALPLKEDA N
//
