ID A0A0A2EWS6_9PORP Unreviewed; 949 AA.
AC A0A0A2EWS6;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Peptidase M16 {ECO:0000313|EMBL:KGN81965.1};
GN ORFNames=HQ41_09185 {ECO:0000313|EMBL:KGN81965.1};
OS Porphyromonas sp. COT-290 OH860.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=1515615 {ECO:0000313|EMBL:KGN81965.1, ECO:0000313|Proteomes:UP000030116};
RN [1] {ECO:0000313|EMBL:KGN81965.1, ECO:0000313|Proteomes:UP000030116}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COT-290 OH860 {ECO:0000313|Proteomes:UP000030116};
RA Wallis C., Deusch O., O'Flynn C., Davis I., Jospin G., Darling A.E.,
RA Coil D.A., Alexiev A., Horsfall A., Kirkwood N., Harris S., Eisen J.A.;
RT "Porphyromonas sp. strain:COT-290_OH860 Genome sequencing.";
RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261}.
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:KGN81965.1}.
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DR EMBL; JRAR01000078; KGN81965.1; -; Genomic_DNA.
DR RefSeq; WP_044190623.1; NZ_JRAR01000078.1.
DR AlphaFoldDB; A0A0A2EWS6; -.
DR eggNOG; COG0612; Bacteria.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000030116; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 4.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR007863; Peptidase_M16_C.
DR PANTHER; PTHR43690; NARDILYSIN; 1.
DR PANTHER; PTHR43690:SF34; ZINC PROTEASE PQQL-LIKE; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 2.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000030116};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..949
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001998489"
FT DOMAIN 71..194
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 214..400
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 700..879
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 949 AA; 106104 MW; 9903A63745C294B0 CRC64;
MNVLNKLRRS LVALSTGALL AVTTLASAQQ LPPPLPADTA LRMGQLENGL TYFIRKNALP
EGRADFYIAQ KVGSMQEEDS QSGLAHFLEH IAFNGTKNFP GKGMINWLET IGVRFGFGIN
AYTSFDETVY TLINVPVERQ SVVDSCLLIL HDWSNAISLE DKEIDNERGV IQEEWRSRDS
GNQRIAEKAF EAAFPGNRYG KRMPIGSMDI VRNFKYQELR DYYKKWYRPD LQALIIVGDI
DVDHVEATIK KQFADVPKPV NPAERVYIAV EDNDAPISII ATDPEGVGTR ISIAFKTDVT
PAEIRATAFG VAEHYIKSVI TAMINDRFEE IWKKPNAPFI AASANFGPYF QVAKTKDAWT
FSAVAADGKY EPALQALVAE IERVRQHGFT EGELKRAKKN FMVGMKTTYN ERNKRKNGSF
TSVYVDYFIN GGTLADIDVL YPIYEQFAEL LPLAQINAMA QELLGEKNIA ISLTGPEKPE
FKYPTKDELV SQFLNARKQP VEVYKEPVSD EKLMKKLPKA GKIVKEDKQG QYGSTVWTLS
NGVKVIYKST DFKEDQILMS AVRHGGLASF PKADPTELRM INDISSLGGI AEFDETALGR
VLTGRVVSLN ASLGQITDGL SGNSSKDDLE TLLQLIHLSF TAPRLDNQAY EAFREKMVNL
IETQKSNPMS SVGDSISAAI YPGNKLFQSV TVEELNAMSY ESAMKLYNER MTNAKDFQFF
FVGNVAPEKL RPLVELYIAS LPVKKNLDTK PMESRLPSLR KGVFTNHYTK KQSTPAGLVF
DFISGKLPYS QRNAMIMSIV GEVLNQVYTA TIREEEGGTY GANASASVIR YPEGEAKLQV
TFQTDPAKAH QLNKIVYAEI DRLVQEGAKA ENFDKVLENM KKSHATSLKE NSYWLSQLSN
YYFRGTDNVS QYEATLGSIK REDLAPLVKQ LLDQKNRVEV MLMPEAEAK
//