ID A0A366W9M9_9RHOB Unreviewed; 422 AA.
AC A0A366W9M9;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Insulinase family protein {ECO:0000313|EMBL:RBW45759.1};
GN ORFNames=DS901_01060 {ECO:0000313|EMBL:RBW45759.1};
OS Loktanella sp. D2R18.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Loktanella.
OX NCBI_TaxID=2267230 {ECO:0000313|EMBL:RBW45759.1, ECO:0000313|Proteomes:UP000253154};
RN [1] {ECO:0000313|EMBL:RBW45759.1, ECO:0000313|Proteomes:UP000253154}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D2R18 {ECO:0000313|EMBL:RBW45759.1,
RC ECO:0000313|Proteomes:UP000253154};
RA Enke T.N., Datta M.S., Schwartzman J.A., Cermak N., Schmitz D.A.,
RA Barrere J., Cordero O.X.;
RT "Modular assembly of carbohydrate-degrading microbial communities in the
RT ocean.";
RL Submitted (JUL-2018) 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, 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:RBW45759.1}.
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DR EMBL; QOCG01000004; RBW45759.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A366W9M9; -.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000253154; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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:InterPro.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
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; PTHR11851:SF149; GH01077P; 1.
DR PANTHER; PTHR11851; METALLOPROTEASE; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
DR PROSITE; PS00143; INSULINASE; 1.
PE 3: Inferred from homology;
FT DOMAIN 13..160
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 167..340
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 422 AA; 45855 MW; 6540F4ACCD1004D8 CRC64;
MTIQLHTLSN GFRIVTEHMP TLKSASIGIW VEAGGRHEKP AQNGIAHFLE HMAFKGTQKR
TALQIAECIE DVGGYINAYT SREATAYYVR LLENDVPLGL DVIADILLNP VFAPEDIEIE
RGVILQEIGM TIDTPDEMVF DWLQEVSFPD QALGRTILGP AERVSAFNRD DLQQFVGQHY
GPNQMILAAA GAVDHDAIVA QAEALFGHLP ALDRGTDLIQ PARFGGGEIR NVKDLEQVHF
ALGLEGPNYR DPQIYTAQIY SSVMGGGVSS RLFQEIRENR GLCYSIFAQT GAYEDTGMTT
IYAGTSAEQI AELATVTIDE MKRAADDMTA SEVARARAQM KAGLLMGLES PSNRAERLAR
LLQIWGRIPS LDETIAQIDA VTTGDVKSFA GQMAGQTGMG LALYGPTDAA PTLDALKERL
AA
//