ID I0W5L3_9FLAO Unreviewed; 962 AA.
AC I0W5L3;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Peptidase M16 {ECO:0000313|EMBL:EID71679.1};
GN ORFNames=W5A_13290 {ECO:0000313|EMBL:EID71679.1};
OS Imtechella halotolerans K1.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Imtechella.
OX NCBI_TaxID=946077 {ECO:0000313|EMBL:EID71679.1, ECO:0000313|Proteomes:UP000005938};
RN [1] {ECO:0000313|EMBL:EID71679.1, ECO:0000313|Proteomes:UP000005938}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K1 {ECO:0000313|EMBL:EID71679.1,
RC ECO:0000313|Proteomes:UP000005938};
RX PubMed=22740661; DOI=10.1128/JB.00506-12;
RA Kumar S., Vikram S., Subramanian S., Raghava G.P., Pinnaka A.K.;
RT "Genome Sequence of the Halotolerant Bacterium Imtechella halotolerans
RT K1T.";
RL J. Bacteriol. 194:3731-3731(2012).
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:EID71679.1}.
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DR EMBL; AJJU01000040; EID71679.1; -; Genomic_DNA.
DR AlphaFoldDB; I0W5L3; -.
DR STRING; 946077.W5A_13290; -.
DR eggNOG; COG0612; Bacteria.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000005938; 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; 3.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR007863; Peptidase_M16_C.
DR PANTHER; PTHR43690:SF18; INSULIN-DEGRADING ENZYME-RELATED; 1.
DR PANTHER; PTHR43690; NARDILYSIN; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 2.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 3.
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:UP000005938};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 69..177
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 217..399
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 713..893
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 962 AA; 112248 MW; 548125CF0F6935EF CRC64;
MKVINFNLFK MINKTLKTCI IILVFQLYFF SSPNLYSSNS QDTLLLDPKI RHGKLPNGLT
YYIKPINDSS SKIDIRLFVK AGSSVLDPDQ YEIEHFLEHI AFKAGNNMNI GKANDLGFKL
GEINGGTSFD FTGYYFKGIE TKEKRDIAFQ LIHDIIWDLD FKDSYIVSER SVLINELVVR
GRFHSNSIIN GLENSMLGRN PISKMNVIEH LNTFPNEALI RFYNDWYRPD LMAIVIVGDI
KDLNGLEQEI MERFSKPKNV ENPRSAKIDY SAYRNSPPQF IKKEHPYLLE NSNNKTINLR
LYFRQKEVHE EKGMEMIINE QQRELLFQML EERLKILQKS YCTNYVAFPR SLFPTFTDMK
IQFTIEGGSE RDVIINTIKV VHQVYNDGFL EEEFQESIKR RLEELSKTDT SSAQYWSENI
RNHFVFEKSL PPNKESLIIN MFNNLTLDEF NQFTKGYLSS PFEDIDIIIL APKGNRIFSH
SEDTFRDWIK EASNMPTVPY TKPKVPQDLI DSLTLVNLKE RGVLKETQIL PETTQYVLEN
GIKIVLNSFD QVLSEKTKHS NTLSFHGFTS KGVNYYTSKD YFSALYCIDI VKNSGVGGLD
KFELDRFYED NGFTGQIIPY IEYNESGIRG NINIKDLETA LQLVYLHFKE PNKDELAFED
WKQKTNSSFN LYRLNEKDFE STVKSTLKDI TYLPKGSAAL EGVSLTDLNR SHAIYREIFG
NAGDFTFIFT GNFPKDELLS LCRKYLGNLS REKSKKGTIT EKSLKRYKLP KSISHDVYST
EFMEGVKVQL VYASKLNHKK FDWKDEIRFK LLRQLLKFSM SQKMRFHSDK GGIYTVSVGI
NPKKDRLFNE IFVRFSCSPE DVDRLILEAK EEINSFRNDE ISTEKLEQFK HSLILDLENN
YNERKVVSEK LYHFYKNDLP WYTLHDEKEF INSISRKDIK DAAKKLLQNK PFEFKMIPLP
KL
//
