ID A0A254SMB8_9BACT Unreviewed; 592 AA.
AC A0A254SMB8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Carboxyl-terminal protease {ECO:0000313|EMBL:OWV21079.1};
GN ORFNames=B7982_12555 {ECO:0000313|EMBL:OWV21079.1};
OS Fibrobacter sp. UWB2.
OC Bacteria; Fibrobacterota; Fibrobacteria; Fibrobacterales; Fibrobacteraceae;
OC Fibrobacter.
OX NCBI_TaxID=1964358 {ECO:0000313|EMBL:OWV21079.1, ECO:0000313|Proteomes:UP000197741};
RN [1] {ECO:0000313|EMBL:OWV21079.1, ECO:0000313|Proteomes:UP000197741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UWB2 {ECO:0000313|EMBL:OWV21079.1,
RC ECO:0000313|Proteomes:UP000197741};
RA Neumann A.P., Suen G.;
RT "Draft genomes of novel Fibrobacter strains.";
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OWV21079.1}.
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DR EMBL; MWQK01000006; OWV21079.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A254SMB8; -.
DR OrthoDB; 9812068at2; -.
DR Proteomes; UP000197741; 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:OWV21079.1};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU004404}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..592
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012671201"
FT DOMAIN 90..154
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 592 AA; 65560 MW; 031AC2212EFB603D CRC64;
MMFKSFCFRS VFMATLSALC IANAATDKKT PPGDFYDEVS RLNKVLSEVN RKYVENVNPT
ELTDAAINGI RNILDPHTTV FAPKDYESLR VSMEGKFGGV GITISLRDNI LTVISPLSGT
PAFKLGIRAG DRIRKIDGKE TKGMSLDDAV NKLRGKIGTD VTVAIEREGV PDLMDYTITR
AEIIVHAVPY YGMVTPEIGY IKLATFSDKT TSDVENAIRG LQKQGMKKLI LDMRYNPGGL
LNQAIEISEL FLKPGNVIVS TRGRTQKTES ASRRNPMLKS DVPMVVLVNQ GSASAAEIVS
GALQDWDRAL IVGKTSFGKG SVQTIFPLDN AGNALKLTTA FYYLPFGRCI NKPENGIKGL
TLQDDEYDDE KEAAKTDSVK ADTAKRDTFY TNNGRMMFGG GGITPDVDVE LDPMPWVVQV
QERMAMYFKF AVKIRPSLEK AGVKVNSEWT VPDSLFTQFK AFCKKDTNFM KVKSNALVGV
DQLEKSIIRE QNYMGDSAKT ISDSTLVKRI TEMRKALEDN RDAQFEANKD YIKDGIKREL
LTAFVNDSVS TAFSLKRDKQ LNEAIKYLSD MNLFKKSISA PAKKKGAAKP KK
//
