ID A0A427U7C9_9VIBR Unreviewed; 917 AA.
AC A0A427U7C9;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Insulinase family protein {ECO:0000313|EMBL:RSD32586.1};
GN ORFNames=EJA03_03175 {ECO:0000313|EMBL:RSD32586.1};
OS Vibrio pectenicida.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=62763 {ECO:0000313|EMBL:RSD32586.1, ECO:0000313|Proteomes:UP000269041};
RN [1] {ECO:0000313|EMBL:RSD32586.1, ECO:0000313|Proteomes:UP000269041}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CAIM 594 {ECO:0000313|EMBL:RSD32586.1,
RC ECO:0000313|Proteomes:UP000269041};
RA Gomez-Gil B., Enciso-Ibarra K.;
RT "Genomic taxonomy of the Vibrionaceae family.";
RL Submitted (DEC-2018) 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:RSD32586.1}.
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DR EMBL; RSFA01000007; RSD32586.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A427U7C9; -.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000269041; 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: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.
DR PROSITE; PS00143; INSULINASE; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670}; Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..917
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019010931"
FT DOMAIN 51..162
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 200..374
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 669..848
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 917 AA; 103876 MW; EA388E5550C91381 CRC64;
MKKLFALCWL LLVGCAQNTP SSPVPIQLNT NWSSGTLKNG LKYHLYPMDS KEVSIRLLVH
VGSTAEESSQ LGYAHYVEHL AFEGSENFTP KEVERLMETT GAKKWHGVNA TTSYDNTTYK
FNLPNLEAFD KAMLWLRDVA SGITFSPEEI EQEKSILLSE NQYRRPEQQS FSDKYYDYAI
KGTIYAQRSP LGTTDAILSA TPESLKAFYN KWYQPQNAEL IIAGNIDRAQ AKVMIEKLFS
DWAATNTEYA PELPLLTAKN DDFIAKVADD EHAILGLRFD RGDSLVSTQE HLLNSELDYI
AAQLIRLRLR TILDEQSIPY QWLYSDVSSF RNLSIYEVSF AFSEPERNLV QPIFLKTLAS
LRDHGVSESE LDIIMADYIS WRKHADEDWE TSKPEYFINE KITQLITGAP TQSRKGYKLS
LDNAIRSSDI NTVNQHLNNM LSSHYGMFVG VGATESIEHI KQALPEWKNM YKITGVVDNK
INFDVNGLVE VKSSSPLPDS VVYENGEELW TLGNGVEVLL DPDVNSDFVN LVYMSAGGKA
ALDRDLLPAA QILFPVIARS GTGNFNGSQM KAYVRKNSIE MQGFIDDTEH GFEMSVPREH
FNQALQFMHT SLVYPKFDPR QVDVIKQEFA EQAMSYLKSP LGQWYDAMDT NTYASSSAYF
PNYARDFNKV TVDQVQQAFE QLFRQSRNNK LVIVADVKSS DITDALNDYV STLPLQQASV
PSYQIDYNPR PDAKINLAIN NEQKGRFILR THNKNAQVQD VRRELIDQII ENILANRLDN
YVREDLSLDY SPASYSAMSY NQTITDWVIE SQVAVSDLTK VEQAVDKVVN DLQTVITEGE
LSVAKKRLDL YLEDVVSNAD SSAWVRSMYM VNGFGKNVLT DAQGIIFDIS IDEVKERIDE
SFGKGTESYK YILSPLD
//
