ID A0A0N0RR06_9FLAO Unreviewed; 440 AA.
AC A0A0N0RR06;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Peptidase M16 {ECO:0000313|EMBL:KOS07656.1};
GN ORFNames=AM493_17610 {ECO:0000313|EMBL:KOS07656.1};
OS Flavobacterium akiainvivens.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1202724 {ECO:0000313|EMBL:KOS07656.1, ECO:0000313|Proteomes:UP000037755};
RN [1] {ECO:0000313|EMBL:KOS07656.1, ECO:0000313|Proteomes:UP000037755}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IK-1 {ECO:0000313|EMBL:KOS07656.1,
RC ECO:0000313|Proteomes:UP000037755};
RA Wan X., Hou S., Saito J., Donachie S.;
RT "Whole genome sequence of Flavobacterium akiainvivens IK-1T, from decaying
RT Wikstroemia oahuensis, an endemic Hawaiian shrub.";
RL Submitted (AUG-2015) 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:KOS07656.1}.
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; LIYD01000005; KOS07656.1; -; Genomic_DNA.
DR RefSeq; WP_054409370.1; NZ_LIYD01000005.1.
DR AlphaFoldDB; A0A0N0RR06; -.
DR STRING; 1202724.AM493_17610; -.
DR PATRIC; fig|1202724.3.peg.3660; -.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000037755; 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; 2.
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:SF17; PROTEIN YHJJ; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
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:UP000037755};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..440
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005857722"
FT DOMAIN 35..177
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 189..366
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 440 AA; 50338 MW; 0AC24C80E589C48E CRC64;
MKKSIMALGS LLVLGAAHAQ KVEFEEFDLS NGLHVILHQD KSAPVVVTAV MYHVGAKDEN
PERTGFAHFF EHLLFEGTEN IERGQWDKIQ AAHGGTGNAN TTDDRTYYYE LFPSNNTELG
LWMESERLLH PVINQIGVDT QNEVVKEEKR MRVDNQPYGN LFAEVKKNMF KVHPYRWATI
GSMEHLDAAT LEEFLAFNKK FYVPNNAVLV VAGDIDTKQT KKWVEQYFGV IKKGEPVVRK
KYEEAPITQE FHASYEDPNV QTPMIVEAYR TPAMTTKDAR VLDLISSILS DGKSSRMYKK
IVDDKKMAMQ VGAFNYSQED YGLYFVYGIP MAGFTTQQIQ KEIDDEIVKL QTELVSEKEF
QKLMNQVESR YVSQNASVDG VAENLATYYM LYGDVNLINT EIDIYRKITR EDIKAVANKY
LKPNQRLILD YLPAQEKAEN
//
