ID A0A545UCG6_9GAMM Unreviewed; 917 AA.
AC A0A545UCG6;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Insulinase family protein {ECO:0000313|EMBL:TQV87159.1};
GN ORFNames=FLL46_15255 {ECO:0000313|EMBL:TQV87159.1};
OS Aliikangiella coralliicola.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Pleioneaceae; Aliikangiella.
OX NCBI_TaxID=2592383 {ECO:0000313|EMBL:TQV87159.1, ECO:0000313|Proteomes:UP000315439};
RN [1] {ECO:0000313|EMBL:TQV87159.1, ECO:0000313|Proteomes:UP000315439}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M105 {ECO:0000313|EMBL:TQV87159.1,
RC ECO:0000313|Proteomes:UP000315439};
RA Wang G.;
RT "Draft genome for Aliikangiella sp. M105.";
RL Submitted (JUL-2019) 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:TQV87159.1}.
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DR EMBL; VIKS01000009; TQV87159.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A545UCG6; -.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000315439; 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:SF17; PROTEIN YHJJ; 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:UP000315439};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 44..167
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 202..376
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 488..615
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 644..820
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 917 AA; 101933 MW; BF7CAC008550250B CRC64;
MKIIPTVKKS LGIVVLGWLS ISAIAKNVDV DIPYQKYVLD NGLRVIVHED RKAPIVAVSV
WYNVGSKDEP KGRTGFAHLF EHLMFNGSEN YNDEYFKPFH QVGATGMNGT TWFDRTNYFQ
NVPTPALEMA LWMESDRMGH LLGAIDQAKL DEQRGVVQNE KRQGDNQPYG KSEYRILEGL
YPAGHPYRHS TIGSMDDLNA ASLDDVKTWF KDYYGAANAV VVLAGDISPE KGRELVNKYF
GDIPAGPEVT RMNAWIPTRQ HNTLEEMYER VPQARIMKVW ALPGRNEKET ALLNLAARIL
GSGKNSRLYQ ELVYKNQLAS NVSVDVEEHL LTSKFTVDVT LKPGADRQKA EAIMNRVLAD
FKKKAPSKDE LLRAQTGIKA ATIRGLEQVG GFNGKASILA RGELYANDPG FFKKRLGWIA
DATTKSIQKV SNKWLADGFY QLAVLPYPEY KVAKSTVDRS KGLPQIGDLP QLKFPTVQRA
KLKNGIEVVL AESNATPVVN VTLQFDAGYA ADSSGFKLGT ASYTMSMLDE GTDDKNALEI
SAEAEKLGAN IYTSSNLDMS SVNLSALKSN LKDSVELFAE IVREPAFKQG EIDRLRGRWI
AGIKQEKVQP VNIALRNLPP LIYGDKHAYG IPLTGSGTEE SIQSLTREDL QKFYKTWLRP
DNAKLFVVGD TKMDEILPIL NRELGSWKAP KAALPTKNIS DVLVAEKRVI VIDKPGAPQS
LILAGELAPA TGVDNNIAIQ AMNDIIGGQF TSRVNMNLRE DKHWAYGAYT FMFDARGQRP
FMVYAPVQTD KTGASVKELV RELSEFNGDK PATQDEMFKT IKNNVNSLPG AYETSGAVMQ
SLLANDRFNR PDDYVAKLTD KYNNLKLPEI KAAAKQVINP DKLTWMIVGD KKEIVKQLKD
MELGEMIFMD ADGNVLK
//