ID F4KP35_PORAD Unreviewed; 506 AA.
AC F4KP35;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Protease Do {ECO:0000313|EMBL:AEE13564.1};
DE EC=3.4.21.108 {ECO:0000313|EMBL:AEE13564.1};
GN OrderedLocusNames=Poras_1633 {ECO:0000313|EMBL:AEE13564.1};
OS Porphyromonas asaccharolytica (strain ATCC 25260 / DSM 20707 / BCRC 10618 /
OS JCM 6326 / LMG 13178 / VPI 4198) (Bacteroides asaccharolyticus).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=879243 {ECO:0000313|EMBL:AEE13564.1, ECO:0000313|Proteomes:UP000006545};
RN [1] {ECO:0000313|Proteomes:UP000006545}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25260 / DSM 20707 / VPI 4198
RC {ECO:0000313|Proteomes:UP000006545};
RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G., Pagani I., Lu M.,
RA Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V.,
RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Gronow S., Wellnitz S.,
RA Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Porphyromonas asaccharolytica DSM 20707.";
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
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; CP002689; AEE13564.1; -; Genomic_DNA.
DR RefSeq; WP_013760886.1; NC_015501.1.
DR AlphaFoldDB; F4KP35; -.
DR STRING; 879243.Poras_1633; -.
DR KEGG; pah:Poras_1633; -.
DR eggNOG; COG0265; Bacteria.
DR HOGENOM; CLU_020120_1_0_10; -.
DR OrthoDB; 9758917at2; -.
DR Proteomes; UP000006545; Chromosome.
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; -; 2.
DR Gene3D; 2.40.10.120; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR011782; Pept_S1C_Do.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR001940; Peptidase_S1C.
DR NCBIfam; TIGR02037; degP_htrA_DO; 1.
DR PANTHER; PTHR22939; SERINE PROTEASE FAMILY S1C HTRA-RELATED; 1.
DR PANTHER; PTHR22939:SF129; SERINE PROTEASE HTRA2, MITOCHONDRIAL; 1.
DR Pfam; PF13180; PDZ_2; 1.
DR Pfam; PF13365; Trypsin_2; 1.
DR PRINTS; PR00834; PROTEASES2C.
DR SMART; SM00228; PDZ; 2.
DR SUPFAM; SSF50156; PDZ domain-like; 2.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AEE13564.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:AEE13564.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006545};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 299..363
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT ACT_SITE 143
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 173
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 252
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
SQ SEQUENCE 506 AA; 53857 MW; 63B012D48E04C657 CRC64;
MNKYLKYLLL TLGIALVSGF VSWGVVRATL GNATSTDGSS YSALSQGNYP SSENDYGFLQ
SDYELTSSRT VGNAPDLSPA AELAVQAVVH IKVEGEQTID YIDPFEFFFG GGRGFDRPQS
RTVTSFGSGV IISTDGYIIT NNHVVEGAKS ISVSLNDSRT FEAKLIGSDP TVDIALLKVD
AKDLPTIPFG DSDKIKLGEW VLAVGNPFNL TGTVTAGIIS AKARSTAVEG PQGTAQIARY
IQTDAAVNRG NSGGALVDAQ GRLIGINTMI FSETGNYSGY SFAVPINTAA KVVSDLKKYG
SVQRAVLGIV GGTVNEDIKK EKKLKVSQGV YVNEFSEVSA AYAAGIEEGD VIIAIDGNKI
TEMGELQERI GRCRPGDTII VTVDRKGTKR DFKVTLKNDE GSTEIVKRDS SSLLGASLRE
ISGDQLRKQG VSYGLEVVKV GKGKLQEAGV KEGFIILSIN NKAVRSVSAA RKLVDAAQKT
RFGDKAILLK GFYPGGSMKY YAIDLS
//