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
//