ID A0A1M3BTM3_9BACT Unreviewed; 406 AA.
AC A0A1M3BTM3;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=PDZ domain-containing protein {ECO:0000259|PROSITE:PS50106};
GN ORFNames=BGO17_02820 {ECO:0000313|EMBL:OJU87893.1};
OS Candidatus Saccharibacteria bacterium 49-20.
OC Bacteria; Candidatus Saccharibacteria.
OX NCBI_TaxID=1895829 {ECO:0000313|EMBL:OJU87893.1, ECO:0000313|Proteomes:UP000184370};
RN [1] {ECO:0000313|EMBL:OJU87893.1, ECO:0000313|Proteomes:UP000184370}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=49-20 {ECO:0000313|EMBL:OJU87893.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-2016) 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:OJU87893.1}.
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DR EMBL; MKSN01000001; OJU87893.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M3BTM3; -.
DR STRING; 1895829.BGO17_02820; -.
DR Proteomes; UP000184370; 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 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 24..44
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 106..183
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 406 AA; 42830 MW; 8097D30268B00268 CRC64;
MAEPLTTNTP ITPSPRRAQP QKRIPTTVMI FAFIFVAGIG YVAGGINSGL LSGNINTLLG
KGDIDLASVQ ETYQALESNF DGDLDKQKLI EGANKGLVDA AGDQYTIYMN KKESTSFDDA
LSGNIGGGIG VEVGIRNNVP TVVRVLQDNP AEKSGVMIND IITKVNGEST EGKTLTEVTT
DIRGEVGTTV KLTVLRNGEE KEFNITREQV NNPSAYGEIK DGVGILTITR FDDETGSLAR
AVAMDFKNKG VKGVVVDLRG NGGGYVTAAQ AVAGIWLDRQ LVTTERTNGK VTEELKSTGT
PILNGIKTIV LVNGSSASAS EIVAGALHDH KVATLVGETT FGKGSVQKLV NLSDGATLKV
TIARWYTPAG VNISEKGIVP DTTVVRSVDD INASRDPQLE AALKAI
//
