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Database: UniProt
Entry: A0A0F6A4T6_9GAMM
LinkDB: A0A0F6A4T6_9GAMM
Original site: A0A0F6A4T6_9GAMM 
ID   A0A0F6A4T6_9GAMM        Unreviewed;       925 AA.
AC   A0A0F6A4T6;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Protease 3 {ECO:0000256|ARBA:ARBA00017565};
DE            EC=3.4.24.55 {ECO:0000256|ARBA:ARBA00012449};
DE   AltName: Full=Pitrilysin {ECO:0000256|ARBA:ARBA00033450};
DE   AltName: Full=Protease III {ECO:0000256|ARBA:ARBA00031184};
DE   AltName: Full=Protease pi {ECO:0000256|ARBA:ARBA00029597};
GN   ORFNames=RN22_02440 {ECO:0000313|EMBL:KKD62200.1};
OS   Grimontia sp. AD028.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Grimontia.
OX   NCBI_TaxID=1581149 {ECO:0000313|EMBL:KKD62200.1, ECO:0000313|Proteomes:UP000033732};
RN   [1] {ECO:0000313|EMBL:KKD62200.1, ECO:0000313|Proteomes:UP000033732}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AD028 {ECO:0000313|EMBL:KKD62200.1,
RC   ECO:0000313|Proteomes:UP000033732};
RA   Adrian T.-G.-S., Chan K.-G.;
RT   "Genome sequencing of Grimontia sp. AD028.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Endopeptidase that degrades small peptides of less than 7
CC       kDa, such as glucagon and insulin. {ECO:0000256|ARBA:ARBA00002184}.
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:KKD62200.1}.
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DR   EMBL; LASY01000008; KKD62200.1; -; Genomic_DNA.
DR   RefSeq; WP_046302940.1; NZ_LASY01000008.1.
DR   AlphaFoldDB; A0A0F6A4T6; -.
DR   MEROPS; M16.008; -.
DR   PATRIC; fig|1581149.3.peg.4562; -.
DR   OrthoDB; 9811314at2; -.
DR   Proteomes; UP000033732; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-EC.
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   InterPro; IPR032632; Peptidase_M16_M.
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   Pfam; PF16187; Peptidase_M16_M; 1.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
DR   PROSITE; PS00143; INSULINASE; 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   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          21..158
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          182..359
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          366..645
FT                   /note="Peptidase M16 middle/third"
FT                   /evidence="ECO:0000259|Pfam:PF16187"
FT   DOMAIN          650..824
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   925 AA;  104918 MW;  1B090924BCE9FE1C CRC64;
     MQISPNDHRS YRLITLANNL RVLLVEDVQA PRSAAALTVN VGHFCDPADR EGLAHFLEHM
     LFLGTEKYPD VGEFQSFISR HGGNNNAWTG TENTTFFFDI RHDHFEEALD RFGQFFSAPL
     FNADAVDKER NAVDSEYRLK LQDDVRRIYQ VQKETINPAH PFSKFSVGSL DTLADREGSS
     VRDELIAFYK AHYSANLMAA SITGPFRLDD LETLANQTFS NIPNLDLSPF VPDVPFVDKA
     QLQQFVCIEP LKDVRKLTLA FSMPATDEHY KIKPLSYIAH LLGYEGTGSV MSLLKAKGLI
     NNLSAGGGIS GSNFREFSVS VSLTEAGLTK IDDIVTYIFQ AISLIREQGL DDWRYAEKRA
     VQEMAFRYQE PSRPIDTVSH MVLNMQHYQD ADVLYGDYIM QEYDEALIRQ MLGYLTPDHL
     RLTLIAKGGN YDRTANWYDT PYSVKPFTEA QLEKWRAAHI SPALALPEPN PFISYELDPA
     DLEAPEQQLP EMIQELPGFR LWHLQDTDFR VPKGVVYVAI DSPHAVQSVE NIVKTRVSVE
     MLMESINETA YPAEVAGLNY NLYAHQGGVT LKLSGFNEKL PLLMDLVLDK FAKRDFNPER
     FEIIKTQLLR SWNNATQNKA INRLYNSMTG ILQPNNPTYE ELIEALEPLQ VTELPDFVHR
     VMSELHVEMF VYGNWQKQQT LDLAEPVKDA LRVHNQRYQE STRPLVLLKG AGSASYHLGC
     DSQDSAVLVY YQSHGTEPQD VALFTFAQHL MSAIFFNELR TKQQLGYMVG SGNMPMNRHP
     GLIFYVQSPQ AGPAKLMEAI DDFLNAFFLV LLELNEAQWQ ASKQGLLGQI EEPDANLRAR
     GQRLWISIGN KDAEFTQRQN VAAAIRDMDR ADMVKFVVEQ LKPRTSDRLI MHSCGGAHPD
     ECSLEGTKEI ESVTAFRRNR TERIN
//
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