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Database: UniProt
Entry: A0A1M4SJ16_9GAMM
LinkDB: A0A1M4SJ16_9GAMM
Original site: A0A1M4SJ16_9GAMM 
ID   A0A1M4SJ16_9GAMM        Unreviewed;       477 AA.
AC   A0A1M4SJ16;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Carboxyl-terminal processing protease {ECO:0000313|EMBL:SHE32201.1};
GN   ORFNames=SAMN02745204_00215 {ECO:0000313|EMBL:SHE32201.1};
OS   Thermomonas hydrothermalis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Thermomonas.
OX   NCBI_TaxID=213588 {ECO:0000313|EMBL:SHE32201.1, ECO:0000313|Proteomes:UP000242857};
RN   [1] {ECO:0000313|Proteomes:UP000242857}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14834 {ECO:0000313|Proteomes:UP000242857};
RA   Varghese N., Submissions S.;
RL   Submitted (NOV-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; FQUK01000002; SHE32201.1; -; Genomic_DNA.
DR   RefSeq; WP_072754786.1; NZ_JAILZK010000016.1.
DR   AlphaFoldDB; A0A1M4SJ16; -.
DR   STRING; 213588.SAMN02745204_00215; -.
DR   Proteomes; UP000242857; 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; 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:SHE32201.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000242857};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW   ECO:0000256|RuleBase:RU004404}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..477
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013245663"
FT   DOMAIN          126..209
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   REGION          28..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          458..477
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   477 AA;  49532 MW;  339BFE91F426483D CRC64;
     MPRNPLSLCI ALALAVMPGL LAAQTPPAQT TVQGQAAPVA TPAPPDADTQ DADGEPQAQD
     DDGEDVAALA AAKVPLAEIR RYVTVYNAIK QAYVDPVDDH RLMQMAVRGL LFDLDPHSAY
     LEKDDAQEFD EQTRGSYDGV GVELQQLPDG TLRVIAPLDD SPAARAGLRS GDRIVAIDGK
     LLIPGQNDAS APLRGKAGTK VVVRVLREGV REPIELTLVR DTIRTTSVRG RLLEPGFGYL
     RIASFQADTA AQFVKQLDAL QASGPLRGLV IDLRSNPGGL LIGAVEIADE LLDHGNIVST
     RGRAAIGTTR FEATPGDRLH GAPVVVLVDA GSASAAEVLA GALQDNRRAR VVGSRTFGKG
     SVQTLLPLDN GDAVKLTTAR YYTPSGHSIQ ARGIQPDVVL HPQGGKPAPA PVSEAELPGH
     LAAEAGALEG DNAGEVLPGT APITAALREL KAMAGVPVAS GGKHAGPAKK PAKPAGQ
//
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