ID A0A0P0NHM0_9SPHI Unreviewed; 950 AA.
AC A0A0P0NHM0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Peptidase M16 {ECO:0008006|Google:ProtNLM};
GN ORFNames=AQ505_15755 {ECO:0000313|EMBL:ALL06816.1};
OS Pedobacter sp. PACM 27299.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=1727164 {ECO:0000313|EMBL:ALL06816.1, ECO:0000313|Proteomes:UP000062859};
RN [1] {ECO:0000313|EMBL:ALL06816.1, ECO:0000313|Proteomes:UP000062859}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PAMC 27299 {ECO:0000313|EMBL:ALL06816.1,
RC ECO:0000313|Proteomes:UP000062859};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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DR EMBL; CP012996; ALL06816.1; -; Genomic_DNA.
DR RefSeq; WP_062549055.1; NZ_CP012996.1.
DR AlphaFoldDB; A0A0P0NHM0; -.
DR STRING; 1727164.AQ505_15755; -.
DR KEGG; pep:AQ505_15755; -.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000062859; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
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; IPR001431; Pept_M16_Zn_BS.
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.
DR PROSITE; PS00143; INSULINASE; 1.
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:UP000062859};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 75..192
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 231..402
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 703..877
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 950 AA; 107291 MW; CCEBA6A2CA7C64EE CRC64;
MKRSLTSLKV SIRPFKNLLY NRIMFIKYKY LSFLFLAALC IPFACKTSQD GQPLLLDPEL
RMGKLPNGFT YYIRKNKTPE KRVTMYLANK VGSILETDQQ RGIAHFVEHM NFNGTKHFPK
KELSNYLEKS GVRFGADINA NTGFDETVYQ LPLPSDHPEL LANGLQIMRD WAQDANMEAE
DVERERHVIL EEKRFRQGIA QRLQEKSLPF YTNNSRYGSR LPIGIEEVLL KVTPEEIRSF
YKEWYRPDLQ AILVVGDVDV DQMEKDIKAK FSDLKNPEKA TARPAYRVSL TGKNQYMQFI
DSEFSGVSLE IMKKQLADTI RTKADYLGDL KQRLLAELVS IRFRRLPIVG FTPLSGGITS
FSVNLSTKPG ETEQALKSIW LELRQMEEQG FTKSELGRVK KAYQFQMDEA LREKDKTSSE
VLIKPYLQHF LTGNAAPGIV QEAELTKELL PEVSLDEINN LMKAYMKAED RDIIVKSSAY
NKTFLPDEAT LLKWIESVYA QNLPPVEEEE LDLPVLKKEP VPGKITAIEE IKPADLQKIK
LSNGMTVLLK KTDFQNDQIL IKGFAAGGTS LSGDADYESA LNAANIVAAA GAGNYDALQL
GKIMTGRKVQ LSPFILDQYQ GFNGSTTTED LPAALELLHA YFMEPRKDEE SFQTLIGRAK
EQLINKEDNR SQVFMDTVNL VLGNYSSRKK PQSISRLEAI QLDRAFEIYK ARFGNAAAFT
FLFVGNIAAE KLKPLLEKYL GSLPSTRVVE KAKDLGINIP AGRIAKTVYK GTEQKSSVIL
AYSGDFDYNF ENTIKMNAIA DALTISLTQR LRDQEGGTYT PNVQLSLSKY PKSRFALVIS
FDCAPKNVEK LNASVQDELN KMRTSGPSAE NLQKFKAARK VGLETGARNN EFWMDYLASQ
VMNNESLNQF FEYGNALNGI STKSVQEAAA KYIQDKNYVK LVLMPEKTNP
//