ID A0LVP1_ACIC1 Unreviewed; 396 AA.
AC A0LVP1;
DT 12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT 12-DEC-2006, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE SubName: Full=C-terminal processing peptidase-3 {ECO:0000313|EMBL:ABK53501.1};
DE EC=3.4.21.102 {ECO:0000313|EMBL:ABK53501.1};
GN OrderedLocusNames=Acel_1729 {ECO:0000313|EMBL:ABK53501.1};
OS Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B).
OC Bacteria; Actinomycetota; Actinomycetes; Acidothermales; Acidothermaceae;
OC Acidothermus.
OX NCBI_TaxID=351607 {ECO:0000313|EMBL:ABK53501.1, ECO:0000313|Proteomes:UP000008221};
RN [1] {ECO:0000313|EMBL:ABK53501.1, ECO:0000313|Proteomes:UP000008221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43068 / DSM 8971 / 11B
RC {ECO:0000313|Proteomes:UP000008221};
RX PubMed=19270083; DOI=10.1101/gr.084848.108;
RA Barabote R.D., Xie G., Leu D.H., Normand P., Necsulea A., Daubin V.,
RA Medigue C., Adney W.S., Xu X.C., Lapidus A., Parales R.E., Detter C.,
RA Pujic P., Bruce D., Lavire C., Challacombe J.F., Brettin T.S., Berry A.M.;
RT "Complete genome of the cellulolytic thermophile Acidothermus
RT cellulolyticus 11B provides insights into its ecophysiological and
RT evolutionary adaptations.";
RL Genome Res. 19:1033-1043(2009).
CC -!- SIMILARITY: Belongs to the peptidase S41A family.
CC {ECO:0000256|ARBA:ARBA00009179, ECO:0000256|RuleBase:RU004404}.
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DR EMBL; CP000481; ABK53501.1; -; Genomic_DNA.
DR RefSeq; WP_011720564.1; NC_008578.1.
DR AlphaFoldDB; A0LVP1; -.
DR STRING; 351607.Acel_1729; -.
DR KEGG; ace:Acel_1729; -.
DR eggNOG; COG0793; Bacteria.
DR HOGENOM; CLU_017295_3_2_11; -.
DR InParanoid; A0LVP1; -.
DR OrthoDB; 9812068at2; -.
DR Proteomes; UP000008221; Chromosome.
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 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, ECO:0000313|EMBL:ABK53501.1};
KW Protease {ECO:0000256|RuleBase:RU004404};
KW Reference proteome {ECO:0000313|Proteomes:UP000008221};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU004404}.
FT DOMAIN 97..180
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 396 AA; 40316 MW; 16A4B297B676CFF3 CRC64;
MRISRRSRWV RIGGAVLALA SIYSAGVVTG VLGSSGSAPQ RPAAAPSSPG FLDQVEQTIL
RNAAKPVTAD ELDRSAIRGM LDALDDKWSS YYSAADFASF ENVMNGQYTG VGLWVHRDAS
GAVTVLNVQA GSPADRAGVR SGDVVLAVGG VPVAGRSIAD VVTALRGDAG TTVTLTYRRG
DVVRTVTMRR SAVASEDVTA ATQNGVMIIK VSAFSRGVAN RVRALDSLAR TQRDRGIVLD
LRGNPGGLLE EGVQTASVFL DGGLVATFVR RGAQPVALKA APGGDIATPL AVLVDGGTAS
AAEIVAGALQ DRQRAVVVGS PTFGKGSVQQ PIPLADGSAI EFTVGTYLTP AGRSLDGVGV
QPDVPVAANA PPSLALEEAV DVISGLLANA GTSGHG
//
