ID A0A515L917_9SPHN Unreviewed; 970 AA.
AC A0A515L917;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Insulinase family protein {ECO:0000313|EMBL:QDM40574.1};
GN ORFNames=C0V74_05610 {ECO:0000313|EMBL:QDM40574.1};
OS Altererythrobacter sp. TH136.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Altererythrobacter.
OX NCBI_TaxID=2067415 {ECO:0000313|EMBL:QDM40574.1, ECO:0000313|Proteomes:UP000315722};
RN [1] {ECO:0000313|EMBL:QDM40574.1, ECO:0000313|Proteomes:UP000315722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TH136 {ECO:0000313|EMBL:QDM40574.1,
RC ECO:0000313|Proteomes:UP000315722};
RA Cai H.;
RT "Genomes of bacteria within cyanobacterial aggregates.";
RL Submitted (DEC-2017) 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}.
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DR EMBL; CP041409; QDM40574.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A515L917; -.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000315722; Chromosome.
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; 2.
DR Pfam; PF05193; Peptidase_M16_C; 2.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000315722};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..970
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5022100293"
FT DOMAIN 70..189
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 223..397
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 533..656
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 687..866
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT REGION 472..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..506
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 970 AA; 102644 MW; C25110BE0FD78195 CRC64;
MHFRFASTSV LALALTACAA APAPQSASSA PVAAAQATAP AAAPLSALVE EVSIPYDSFT
LANGLTTLVH TDRKTPVVGV TLYYRVGSKN EPRGRTGFAH LFEHLMFGGS ENVESFDVPL
EAVGSTSTNG STWYDRTNYV ETVPTGALDR ALMMEADRMG HLLGAVTQDK LDKQRSVVKN
EKRQGDNQPY GLVEYAIGDG LLPVGHPYRH STIGSMADLD AANLTDVRNW FRDHYAPNNV
VLALAGDIDL ATARAKVEKW FGAIPRGPEV KPVDAPVVGP AAPVRREMTD QVPVTRVTRA
WTGPGINHAD APALAVGMYI LGGLASSRLD NALVRGDELA VRVSAGNQQQ ELLSFLQADM
DVKPGTDRAA AEAAFDKVIA DFIARGPTQD EVQRAATKIV SGQIGALEEV GGFGGKGATL
AEGLLYSNDP ADYKKQLEAI AALTPGQVQD ALQRWLSRPA LTVAVVSGER TEDGATMGGW
GDEGTVPAPQ PDAKKPVPPI AKSPPIAIPP VEDVGELTFP AIERATLTNG IPVALARRTA
VPKVMVDLRF NAGYSADGLA RAGTHSLMVS ALDEGTTTRD ATRIAEDQER LGADISTGTS
LDYDDVFLTA LSANLAPSLE LMADIVRNPA FRADDVARLK NQRAADIAQQ LASPQGLASR
ALAPLVYGEG HPYGTVGALG TTAVVAKLTP EDLTAEAQAW LRPENARITV VGDVTMAELL
PQLNQAFGNW SSSEQAPAKK DLPLITPAAE TRLVVIDRPN SPQSVIYAGR LLPVTGATAN
LESLDLANEV LGSGFLSRLN LLIREEKGWS YGVRTGVTAP EGQRLFTFSA PVQADRTGDS
VALALDVIGQ FAGGGKGVDA NEFNRVTDGN IRGLPNRFQT NGQVLRALLD LQARGRPDDY
YTKLPDTYRA IRTNAIDQAA RDYLGAGGLT IVVVGDRDVI DPQLAKLKLP ITYLPADTGA
PVDTDVSSGE
//