ID F4KN27_PORAD Unreviewed; 720 AA.
AC F4KN27;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Peptidase S46 {ECO:0000313|EMBL:AEE12365.1};
GN OrderedLocusNames=Poras_0411 {ECO:0000313|EMBL:AEE12365.1};
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:AEE12365.1, 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 -!- SIMILARITY: Belongs to the peptidase S46 family.
CC {ECO:0000256|ARBA:ARBA00010491}.
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DR EMBL; CP002689; AEE12365.1; -; Genomic_DNA.
DR RefSeq; WP_013759982.1; NC_015501.1.
DR AlphaFoldDB; F4KN27; -.
DR STRING; 879243.Poras_0411; -.
DR MEROPS; S46.002; -.
DR KEGG; pah:Poras_0411; -.
DR eggNOG; COG3591; Bacteria.
DR HOGENOM; CLU_013776_0_0_10; -.
DR OrthoDB; 9805367at2; -.
DR Proteomes; UP000006545; Chromosome.
DR GO; GO:0008239; F:dipeptidyl-peptidase activity; IEA:InterPro.
DR GO; GO:0070009; F:serine-type aminopeptidase activity; IEA:InterPro.
DR GO; GO:0043171; P:peptide catabolic process; IEA:UniProt.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR InterPro; IPR019500; Pep_S46.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR000126; V8_ser_AS.
DR PANTHER; PTHR38469; -; 1.
DR PANTHER; PTHR38469:SF1; PERIPLASMIC PEPTIDASE SUBFAMILY S1B; 1.
DR Pfam; PF10459; Peptidase_S46; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS00673; V8_SER; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022438};
KW Protease {ECO:0000256|ARBA:ARBA00022438};
KW Reference proteome {ECO:0000313|Proteomes:UP000006545};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..720
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003310138"
SQ SEQUENCE 720 AA; 82182 MW; 5978EA6403DE06D6 CRC64;
MTTHLRRVLL LLLTSLTLSA VALADGGMWL LEQMADQADE LQAKGLQIPV EEIYNPDGPC
LQRAVVMFDG GCSGVFVSNQ GLVLTNHHCG YDQIQSHSAV EHNYLRDGIW TQSMREELPC
PGLEVISIDK ITNVTDQVNK LLKESPYKED PMAAFSIATL TKMIPAIVGE EAMKQPGIRY
ELKPFYGGNR YYLFTKKVFT DVRLVAAPPS AIGKYGSDTD NWMWPRHTGD FSIFRVYVDK
NNNPADYSAD NVPYKPERFA AVSTSGVQRD DFALIMGFPG TTNHFFTEAQ VDEWSEIDNN
IRIEMRGLRQ EVMLRRMLAD EKVNIQYAAK YAYSQNGYKR AQGANWAIRT RNLQATKRAQ
QDELAQWAKA NNRTEVTKAI QTIADCVAAR REARRVQWYL MEGILTPIEF LQIPLVDGKK
LQQWSDPKVR EEIISELRSG YAAFYNKDYD PTVDKEVATV LLQRYTERID EAHWPEALRE
GVAQYHSVQA YVTHLFDSSI FADPARFETF LKTPSREQLL NDPMMQFAVS TINLFVQMRE
QQAAYDDPIK LAHRDYVRGA MDMQGARKVW PDANLTLRFT YGNVRGYTPR DNVYYGHQTT
LTGVMEKEDP TSWEFALPDQ IKEIYKQKDY GVYALPNGEM PVNFCATTHT TGGNSGSPVF
DSKGRLIGLN FDRNWEGVGG DIEYLPDYQR SIILDIRYLL MLVDKYGHCQ RLLDEMNLVK
//
