ID A0A151ALX1_9CLOT Unreviewed; 384 AA.
AC A0A151ALX1;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Serine protease Do-like HtrB {ECO:0000313|EMBL:KYH28645.1};
DE EC=3.4.21.107 {ECO:0000313|EMBL:KYH28645.1};
GN Name=htrB_1 {ECO:0000313|EMBL:KYH28645.1};
GN ORFNames=CLCOL_16570 {ECO:0000313|EMBL:KYH28645.1};
OS Clostridium colicanis DSM 13634.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1121305 {ECO:0000313|EMBL:KYH28645.1, ECO:0000313|Proteomes:UP000075374};
RN [1] {ECO:0000313|EMBL:KYH28645.1, ECO:0000313|Proteomes:UP000075374}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13634 {ECO:0000313|EMBL:KYH28645.1,
RC ECO:0000313|Proteomes:UP000075374};
RA Poehlein A., Daniel R.;
RT "Genome sequence of Clostridium colicanis DSM 13634.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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:KYH28645.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LTBB01000008; KYH28645.1; -; Genomic_DNA.
DR RefSeq; WP_061858499.1; NZ_LTBB01000008.1.
DR AlphaFoldDB; A0A151ALX1; -.
DR STRING; 1121305.CLCOL_16570; -.
DR PATRIC; fig|1121305.3.peg.1657; -.
DR Proteomes; UP000075374; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00987; PDZ_serine_protease; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.40.10.120; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR001940; Peptidase_S1C.
DR PANTHER; PTHR43343; PEPTIDASE S12; 1.
DR PANTHER; PTHR43343:SF3; PROTEASE DO-LIKE 8, CHLOROPLASTIC; 1.
DR Pfam; PF13180; PDZ_2; 1.
DR Pfam; PF13365; Trypsin_2; 1.
DR PRINTS; PR00834; PROTEASES2C.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:KYH28645.1};
KW Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:KYH28645.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000075374};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 34..57
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 283..342
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 384 AA; 41708 MW; 8E8B04546D6D421B CRC64;
MQDNHEVKEV NWESISDEKY GAIKFRKRKN NIKSFFRGVA FILIAAVSGA VSSSYMIEKK
YSQKAKVEDK SIDEELQENP YSDIAKVANI VGPTVVGIIK TSPNDSQNVN NSSGSGIIFR
SNGYIVTNYN IIDGAEEINV KLARGQKYLK AKFIGSDPDS GLAIIKVEAQ NLPVAKFGDS
SKMRVGDIAI AIGNPLGEEF TGSVTAGVIS ALNRKIQYGK STYKVLQTDV AMNEGNSGGA
LCNLKGEIIG INNLNLKDTQ FKNEDGMGFA IASNEVKNII NEIMEYGKAA RPDLGIYGRD
AVSNNNDGVK GVYVTSVTKG SGAEKAGIMP TDIIVEIEKK KITKFEDMAG ILGKYKIGDT
VKCKIWRNGN NIDMTIELAD MENK
//