ID A0A255TGB5_9BACT Unreviewed; 550 AA.
AC A0A255TGB5;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Peptidase S41 {ECO:0000313|EMBL:OYP64180.1};
GN ORFNames=CIL02_00250 {ECO:0000313|EMBL:OYP64180.1};
OS Prevotella sp. P3-122.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=2024223 {ECO:0000313|EMBL:OYP64180.1, ECO:0000313|Proteomes:UP000215645};
RN [1] {ECO:0000313|EMBL:OYP64180.1, ECO:0000313|Proteomes:UP000215645}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P3-122 {ECO:0000313|EMBL:OYP64180.1,
RC ECO:0000313|Proteomes:UP000215645};
RA Accetto T., Nograsek B., Avgustin G.;
RT "Comparative genomics of non-oral Prevotella species.";
RL Submitted (AUG-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:OYP64180.1}.
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DR EMBL; NPJH01000002; OYP64180.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A255TGB5; -.
DR OrthoDB; 9812068at2; -.
DR Proteomes; UP000215645; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000215645};
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 12..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 90..161
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 550 AA; 61954 MW; D73C263E790838C1 CRC64;
MKQNKSYRYM PLIMATCVVV GIVIGSFFAN RFSGNRLNVI NSGSNRLTNL LRIVDDLYVD
KVDIDSLVEK AIPQILSELD PHSAYISAKD VELTTDDLKG SFSGVGIEFT IRQDTIHVQN
VIKNGPAERA GVLAGDKIVS IDDKPFVGKE VTNEEAMHRL KGPKDTKVKI GVVRYGHKKP
VFMTVTRGEI PTKSVTSVYM LDDDTGYIRI KNFGEKTYTE LLIALAQLSQ ENFSNLVIDL
RFNKGGYLQS AVQMANEFLP KGKIIVYTEG RKSPRQDYIS NGHGSYQDIP LIVLINEGSA
SASEIFAGAI QDNDRGTIIG RRSFGKGLVQ QQIGFPDGSL IRLTIARYYT PSGRCIQKPY
TMGGDREYEQ DLITRYQHGE YFYQDSIKHT GPAYHTALGR SVYGGGGITP DIFIPEDTLG
ITSYYKEAAM SGLILQFAYT YTDDNRQKMQ KFEEMLELVN YLKKQNTVDQ FANYANSHGL
QRRNLMIQKS HSLLERDINS SIIYNMFDEQ AWTEYVNQED RVIKTALEVF RKGEAFPKAP
EKAKEDKKVK
//
