ID G6EYD8_9PROT Unreviewed; 916 AA.
AC G6EYD8;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Insulinase protein {ECO:0000313|EMBL:EHD14526.1};
GN ORFNames=CIN_04580 {ECO:0000313|EMBL:EHD14526.1};
OS Commensalibacter intestini A911.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae.
OX NCBI_TaxID=1088868 {ECO:0000313|EMBL:EHD14526.1, ECO:0000313|Proteomes:UP000005939};
RN [1] {ECO:0000313|EMBL:EHD14526.1, ECO:0000313|Proteomes:UP000005939}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A911 {ECO:0000313|EMBL:EHD14526.1,
RC ECO:0000313|Proteomes:UP000005939};
RA Lee W.-J., Kim E.-K.;
RT "Genome Sequence of Commensalibacter intestini A911, isolated from
RT Drosophila gut.";
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
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:EHD14526.1}.
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DR EMBL; AGFR01000003; EHD14526.1; -; Genomic_DNA.
DR AlphaFoldDB; G6EYD8; -.
DR STRING; 1088868.CIN_04580; -.
DR PATRIC; fig|1088868.3.peg.458; -.
DR eggNOG; COG0612; Bacteria.
DR Proteomes; UP000005939; 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: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; 4.
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..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..916
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003488453"
FT DOMAIN 70..216
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 225..396
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 668..847
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 916 AA; 99903 MW; 291595F95F1EAF3E CRC64;
MKISLSKATL SLALLTSTPL MGAAFFSQHA FAQKITTDPI TLPTKSPAKA ESSVLIKQDV
VRKTLQNGLR VIVVKDPLAP VITAQISYLV GSNQAPAGFP GTAHALEHMM FRGSTGLDKD
QLAVLGAQLG GSYNAFTTEN VTQYYYTAPA EDLNIMLKIE ALRMGGLSLN AADWEKERGA
IEQEVSRDLS SPIYKYVSEL QKIMFDGTPY EHDALGTRPS FDKTTVAILR KFYETYYAPN
NAILVISGDV DPNKAIAQVE KDFGSIPRKD IPKSKPFTLK PIKAQTLTYP TDFPTSLVTI
AWRMPGERSK NFAVADILSD VISSQRGALY GLVPQGKALM ADFEYVPKGD VGFGVAIAAF
PKGQDYKPVL NEVKQIIQNI HEHGVSPELV EAAKRKEIAS LAFSANSITG LASSWSTALA
FQGLNDPNEM AAAYQAVTPE QVNELAKQIL NPDEAITAIL TPENSGKPIS NKGYGGAESF
ASVPDKPVKL PEWAESALKK LNVPKESAQP TDMTLSNGIR LIVQPIHVSN TISIFGQIRQ
NPSLQEGKGK EGIADITDDM FKYGTKTLDR LAFRKAVDDI AADVSAGSDF SLSVLAPDFD
RGVQLLADNE LNPAFDQKFF DIVKQQTSQS LVGLYQSPGY HFSRAISKAI NPPNDPSLRQ
ANPQQVMKLT VQDLNDFYKK SFRPDLTTIV VAGNITPAQA KATIEKYFGQ WKAEGPKPDL
NMPKRPNSKS SYVHVPDKSA VQNSVALVES INMNVHQPDH YLLNLGNEVL SGGFAGRFYK
DLRVKTGYVY NVNSDFDWSQ TRGAYSITFG ADPDKVSLAR KAALKDLTAM QTTPITEDEL
QLAKASLLRS IPLQEASVNG IADRYLTYTS LGLPLNSSHI AAESYYKATA AEIQKAFQTY
IRPKDLAQII KGPNTP
//
