ID A0A1I0FIF4_9FIRM Unreviewed; 555 AA.
AC A0A1I0FIF4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Carboxyl-terminal processing protease {ECO:0000313|EMBL:SET57000.1};
GN ORFNames=SAMN04487771_102526 {ECO:0000313|EMBL:SET57000.1};
OS [Clostridium] aminophilum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1526 {ECO:0000313|EMBL:SET57000.1, ECO:0000313|Proteomes:UP000199820};
RN [1] {ECO:0000313|EMBL:SET57000.1, ECO:0000313|Proteomes:UP000199820}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KH1P1 {ECO:0000313|EMBL:SET57000.1,
RC ECO:0000313|Proteomes:UP000199820};
RA de Groot N.N.;
RL Submitted (OCT-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; FOIL01000025; SET57000.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0FIF4; -.
DR OrthoDB; 9812068at2; -.
DR Proteomes; UP000199820; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|RuleBase:RU004404, ECO:0000313|EMBL:SET57000.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199820};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU004404}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 87..111
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 191..250
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 1..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 499..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..81
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..533
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 555 AA; 59733 MW; E9536C9712D70138 CRC64;
MEHLEDRNTD PVTGEQEAQN TAPVQECAEM PGRENAETAG QEETDMPGRE NAETAGQEET
DIPGRKNTET EGQTEPSGKK QKKKHPVIRG IVIGVCGTLC VLTAAVGVFV YNGYRRMKAQ
LSLAGQSAEG GKEGINLDNV RDKLSVLDYL VNNKFLFQEN LDAQLQEDYL YYGYVASLGD
PYSRYYSKAD FRKMQESQNG EYVGIGATVT TNPNTGNVEV ISLTPGGPAE KGGILPGDIF
YKVDEEYVTG KDLDLLIIEN IRGKEGTPLT VTVYRPSEKK YIPIAMTREK IVTETIKASM
KDDIGLIRLT EFDEVTTGQF KNAVDTLLAQ GANKLIFDLR NNPGGNLSAV LPCMDYILPD
GGLMLKFKGL GDTHEEFRCE DGHEVSVPMA VLVNGNSASA AEAFSGALQD YGKAVLVGTK
TFGKGIVQTT FPLGDGSAVN LTTQRYYTPK DQDIHGKGLT PDVECELAEG LIAGTQIPEA
QDNQLQKAVE VVNQKAAEDA LTERAAENST AKTAGTQTEA EPSAESEAQE TAGAQTEAEA
EPVSEAGAKE TTAAN
//
