ID A0A1M5Z8C6_BUTFI Unreviewed; 448 AA.
AC A0A1M5Z8C6;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Carboxyl-terminal processing protease {ECO:0000313|EMBL:SHI20497.1};
GN ORFNames=SAMN02745229_02061 {ECO:0000313|EMBL:SHI20497.1};
OS Butyrivibrio fibrisolvens DSM 3071.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Butyrivibrio.
OX NCBI_TaxID=1121131 {ECO:0000313|EMBL:SHI20497.1, ECO:0000313|Proteomes:UP000184278};
RN [1] {ECO:0000313|EMBL:SHI20497.1, ECO:0000313|Proteomes:UP000184278}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 3071 {ECO:0000313|EMBL:SHI20497.1,
RC ECO:0000313|Proteomes:UP000184278};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
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; FQXK01000016; SHI20497.1; -; Genomic_DNA.
DR RefSeq; WP_073387499.1; NZ_FQXK01000016.1.
DR AlphaFoldDB; A0A1M5Z8C6; -.
DR STRING; 1121131.SAMN02745229_02061; -.
DR GeneID; 40457643; -.
DR Proteomes; UP000184278; 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; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|RuleBase:RU004404, ECO:0000313|EMBL:SHI20497.1};
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 25..50
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 148..232
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 61..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..89
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 448 AA; 49273 MW; CA701FBCB7E628FC CRC64;
MDNENEMINQ MVNENPPEPG KKFNWGTFFL GVVAGAFLST VVFSVSFALV KHESAPYTVT
TTKVDNNDSK SAKEDDTEEQ DEDSKTDEYE SVVNDETMAK LQLLEQTIDE YYIDSENVST
KTLTDGMYEG MLDSLGDVYS VYYTEEELTA LMEDTNGIYY GIGAYISTDD TTGLPVIAGV
MDGSPAQEAG LKEGDVCYKV DGKLTESMTL EEFIRNVKGE EHTKVLLTIV REGESDYLEI
EVERRQIQTP TVKYEMKEGN IGYIQITEFD TVTSDQFTEA LVTLKGQGMK GLVIDLRSNP
GGNLDTVCEI ASQLLPKGTI VYTVDKDGNR VDYNCDGKNE FDMPMVVLVN GYSASASEIL
AGAIKDYEMG TLVGTTTYGK GIVQRIIPFS DGTAVKLTVS KYYTPNGINI HGTGIDPDVE
IEYDPEAAEN GVDNQLDKAL EIIAEEIG
//
