ID A0A085ZPL0_9FLAO Unreviewed; 923 AA.
AC A0A085ZPL0;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Peptidase M16 {ECO:0008006|Google:ProtNLM};
GN ORFNames=IW19_13000 {ECO:0000313|EMBL:KFF06374.1};
OS Flavobacterium reichenbachii.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=362418 {ECO:0000313|EMBL:KFF06374.1, ECO:0000313|Proteomes:UP000028715};
RN [1] {ECO:0000313|EMBL:KFF06374.1, ECO:0000313|Proteomes:UP000028715}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 25512 {ECO:0000313|EMBL:KFF06374.1,
RC ECO:0000313|Proteomes:UP000028715};
RA Stropko S.J., Pipes S.E., Newman J.D.;
RT "Genome of Flavobacterium reichenbachii LMG 25512.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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:KFF06374.1}.
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DR EMBL; JPRL01000001; KFF06374.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A085ZPL0; -.
DR STRING; 362418.IW19_13000; -.
DR eggNOG; COG0612; Bacteria.
DR Proteomes; UP000028715; Unassembled WGS sequence.
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 Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 36..156
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 195..375
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 686..852
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 923 AA; 104386 MW; E883CAA0291A70F6 CRC64;
MILGLAQVSA QFKTTIPLRK DVVHGTLNNG MQYFILHNEW PKERADFYFV QNVGAILEDD
NQNGLAHFLE HMAFNGTEHF KGKGIINMLA KHGVTFGRDI NAYTAHDETV YNLSNVPVKN
PALLDSCLYI LHDWSGFLSL KDAEIDAERG VIHEEWRTRR NADLRIGSQL EPVIYNGSKY
SKRDVLGDMD LIENFKYKQL RDYYKKWYLP NHQAVIIVGD IDPAKIEQQV KKIMGSIPMP
SNPAERTYES IPDNDKLLYK LAVDKEAQKT SISLNFKRNK TLVQDPAAFE NSITEQLALQ
MLNNRFREYI VNNETALLSA GVSYSNLTRL SSFFTLEVTP KNGKLLEAFQ QAYTEYERAI
QNGFTKEELG RVKENMLKNF ENQLKNKDKI SNGNWASQLQ NYFLEASPVM SLEDESEFVK
RTLAKVDIEQ INKAFRALPT EKNQILTVSG PEKEGVMYPA EADYTAVIKK VKEQKLAPYT
ETVNNVALVT DKLTVKPITK KFEVNGIKEA KGYVLENGAK VIIYPTTLSQ DQILFAAFSP
GGNSVVAQND LPSAQIATVL AKNSGLGDFK VTDLQKQLAG KSVKVGPYIG EYYEGFSGSA
VKQDLETLLQ LTYLYFKHPR FETQAYKRII DHYSNALENV NDDNGKVYGD TIALLDTNHN
KRTFLLSKEN LADLNFDTAS KIFQSRISNA SDFTFVFVGN IAESDIENIN KYLGNVSGNH
TQEKFIDHKI GTAKGVSKEK LIRKMSVPKT SIYVHYENKD VAFSDKNQIM AYMLSQLLDK
RYLEKIREDE GGSYGVQTQS SLSENPAPVF SLRVSFDCNP EKDSKLLQIV YNELQTITVK
DVDAKDLSDI KEDLVKSNQQ NIKSNSYWLS TITSQLQSGD KYLSSAAYEK LIRSVSVQDI
KKYAGEVLPK ANQVEVLMQP KKD
//
