ID G2E9M3_9FLAO Unreviewed; 943 AA.
AC G2E9M3;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 2.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Insulinase family protein {ECO:0000313|EMBL:EGV44765.2};
GN ORFNames=BZARG_234 {ECO:0000313|EMBL:EGV44765.2};
OS Bizionia argentinensis JUB59.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Bizionia.
OX NCBI_TaxID=1046627 {ECO:0000313|EMBL:EGV44765.2, ECO:0000313|Proteomes:UP000003730};
RN [1] {ECO:0000313|EMBL:EGV44765.2, ECO:0000313|Proteomes:UP000003730}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JUB59 {ECO:0000313|EMBL:EGV44765.2,
RC ECO:0000313|Proteomes:UP000003730};
RX PubMed=18842857; DOI=10.1099/ijs.0.65599-0;
RA Bercovich A., Vazquez S.C., Yankilevich P., Coria S.H., Foti M.,
RA Hernandez E., Vidal A., Ruberto L., Melo C., Marenssi S., Criscuolo M.,
RA Memoli M., Arguelles M., Mac Cormack W.P.;
RT "Bizionia argentinensis sp. nov., isolated from surface marine water in
RT Antarctica.";
RL Int. J. Syst. Evol. Microbiol. 58:2363-2367(2008).
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:EGV44765.2}.
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DR EMBL; AFXZ01000002; EGV44765.2; -; Genomic_DNA.
DR RefSeq; WP_040287874.1; NZ_AFXZ01000002.1.
DR AlphaFoldDB; G2E9M3; -.
DR STRING; 1046627.BZARG_234; -.
DR PATRIC; fig|1046627.3.peg.248; -.
DR eggNOG; COG0612; Bacteria.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000003730; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
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:SF21; PROCESSING PROTEASE; 1.
DR Pfam; PF00675; Peptidase_M16; 2.
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:UP000003730};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 49..170
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 206..384
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 528..648
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 678..852
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 943 AA; 105135 MW; 424844CCA6966DBF CRC64;
MMQPKIYTLL AILLLCMSCE DKPKDQAQIL ENDFAIDYEK FTLDNGLEVI LHQDTSDPIV
AVATIMHVGS NREKPGKTGF AHFFEHMSFN DSENVPVGAN RKMIPEWGGS RNGGTSNDYT
VYYEVVPKDA FEKILWIDSD RFGYMINTVT ESALEREKQV VKNEKRQRVD NAAYGYTDEI
IRSNLYPEGH PYNWTVIGSL PDLQAATIED VKEFYNQFYG ASNATLVIAG DIDFDETKSL
VKKWFGEIPS GPKVEALQPQ PVTLTETKSL YFEDNFAKLP ELRMVFPSVE EYHKDSYALQ
ILGQLLSGSK NAPLYQVVVE EQKLAPNIGT YQSNSELTGE FKFRVRANAQ IDLDLVKKAI
DSGLTRFEEN GVNDRDLKRI KAELETGLYQ GVSTVLSKAF QLGQDNEFGG DPSYITKTAK
LTEAVTADDV MRVYNQYIKN KNYVMTSVVP KGQLDLAVEN AKEATVWIEE VKQNVASEEV
GQGEEADYEK TVSKYDRSEP AFGELPKFKM PTIWTGNLEN GLSIYGIENN ETPLVQFDIT
IPGGQLLDPT NKAGVANFLS DLMMEGTANK TPAELEEAIG LLGASIYMYS TNEDFHISGS
CLAKNFEETI ALVKEIILEP RWDESEFARL KQGLETGLKD RESNPNAIAS IAYSRLLYGQ
NHPFAIPGSG TLETVKDISM ADLKAYYTNL VPKNANFHIA GAMSKSQTLG VLENLNAWKG
EAPQLPEFKL PLEVKKNTVY FIDVPDSKQS VFNIGKLALS AKNEEAENLY FANEILGGGS
SGRLFQTLRI EKGYTYGAYS SIGNSLEVSP FTVSSSVRAN ATLKSLEIIK DMVSNYADDF
TEEDVALTKN KLLKASTRAY ESLGAKLGIL RNISKYGYSN DFIEQNQAEL IAMTLEDYKT
IINSYLQEPD MIYVIVGDKA SQWGEVKKLG KPVVELDIFG NPM
//