ID A0A0A7FVZ4_9CLOT Unreviewed; 410 AA.
AC A0A0A7FVZ4;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=PDZ domain-containing protein {ECO:0000259|PROSITE:PS50106};
GN ORFNames=U729_781 {ECO:0000313|EMBL:AIY83016.1};
OS Clostridium baratii str. Sullivan.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1415775 {ECO:0000313|EMBL:AIY83016.1, ECO:0000313|Proteomes:UP000030635};
RN [1] {ECO:0000313|EMBL:AIY83016.1, ECO:0000313|Proteomes:UP000030635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sullivan {ECO:0000313|EMBL:AIY83016.1};
RX PubMed=25489752; DOI=10.1016/j.meegid.2014.12.002;
RA Smith T.J., Hill K.K., Xie G., Foley B.T., Williamson C.H., Foster J.T.,
RA Johnson S.L., Chertkov O., Teshima H., Gibbons H.S., Johnsky L.A.,
RA Karavis M.A., Smith L.A.;
RT "Genomic sequences of six botulinum neurotoxin-producing strains
RT representing three clostridial species illustrate the mobility and
RT diversity of botulinum neurotoxin genes.";
RL Infect. Genet. Evol. 30:102-113(2014).
CC -!- SIMILARITY: Belongs to the peptidase S41A family.
CC {ECO:0000256|ARBA:ARBA00009179, ECO:0000256|RuleBase:RU004404}.
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DR EMBL; CP006905; AIY83016.1; -; Genomic_DNA.
DR RefSeq; WP_039316653.1; NZ_CP006905.1.
DR AlphaFoldDB; A0A0A7FVZ4; -.
DR STRING; 1561.NPD11_2210; -.
DR KEGG; cbv:U729_781; -.
DR eggNOG; COG0793; Bacteria.
DR HOGENOM; CLU_017295_3_2_9; -.
DR OrthoDB; 9812068at2; -.
DR Proteomes; UP000030635; Chromosome.
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:UP000030635};
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 9..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 108..190
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 410 AA; 44574 MW; 67E7577B422AA82F CRC64;
MNNSSNKRFI YIITGVLIVI CLCMGSFVVG NVLATKGVIF TKANSKVENT FKEINDIDKY
KELFEVRDAL IKNYDGEVDD NVLLEGAIKG MTDSLKDPYT VYMNKKEYEK FNEQNSGEYM
GIGVYVGVKN DKVTVISPVE GSPAAKAGLK SDDVIIAVNG QKVGSDVEKT TSLIGGKKKE
EVTLTIERNG GKPFDVKVMR DVIKTQSVKG KMLDGNTGYI QITSFNAGVT EDLKKEIETL
KSKGMKGLII DLRGNPGGYL KEAVGVASQF IPKGKLITYT VDKYDNKSEE VSVGGIAEGM
PLVVLVDNGS ASASEVVTGA LRDYKAATIV GTNTFGKGIV QAPVEFKNGG ALKVTISKYY
TPNGENIHHK GIKPDYEVEP SKEAMSKPYN EKNDNQLKKA IEVLNSKINK
//
