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Database: UniProt
Entry: W7Q057_9GAMM
LinkDB: W7Q057_9GAMM
Original site: W7Q057_9GAMM 
ID   W7Q057_9GAMM            Unreviewed;       956 AA.
AC   W7Q057;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   24-JAN-2024, entry version 29.
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=Q427_10100 {ECO:0000313|EMBL:EWH02185.1};
OS   Halomonas sp. BC04.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=1403540 {ECO:0000313|EMBL:EWH02185.1, ECO:0000313|Proteomes:UP000019279};
RN   [1] {ECO:0000313|EMBL:EWH02185.1, ECO:0000313|Proteomes:UP000019279}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BC04 {ECO:0000313|EMBL:EWH02185.1,
RC   ECO:0000313|Proteomes:UP000019279};
RA   Farooqui S., Greene A.C., Patel B.K.;
RT   "Draft Genome Sequence of Halomonas Strain BC04, an Aromatic-degrading
RT   moderate Halophilic Bacterium.";
RL   Submitted (DEC-2013) 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:EWH02185.1}.
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DR   EMBL; AZQX01000117; EWH02185.1; -; Genomic_DNA.
DR   AlphaFoldDB; W7Q057; -.
DR   PATRIC; fig|1403540.3.peg.1898; -.
DR   Proteomes; UP000019279; 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   Reference proteome {ECO:0000313|Proteomes:UP000019279};
KW   Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           34..956
FT                   /note="Protease 3"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004900330"
FT   DOMAIN          73..188
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          233..409
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          417..688
FT                   /note="Peptidase M16 middle/third"
FT                   /evidence="ECO:0000259|Pfam:PF16187"
FT   DOMAIN          692..867
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   956 AA;  106988 MW;  79B37A22A4A530B4 CRC64;
     MSSLATYRQA QRPWPVPLAG LLLAGALFST AVAAQPTEQS AEAAVDDVVA PRVSPHDTRD
     YRVVTLENGL TALLVSDPDA DRAAASMNVG VGSAQDPDDL AGLAHFVEHM LFLGTEPFPQ
     ADAYQGYLRR HGGSHNAFTA PQDTNYFFDI EPEALTGALD RFSQFFLTPL FNPDQLESER
     NIVHSEYMAR IRDDGRREID VLNQVLNPDN PTVGFSVGSR ETLDPPEGEA TLRQRVIDFY
     ERYYDANVMH LALVAPHSLD ELETMVAERF ADIADRGLER PVIEEPLVLE KDLPLQLEMQ
     SVRDSRHVRF MFPVPDPIQH YTHKPADYLA HLLGHEGEGS LLAVLREAGL ADGLSAGVGR
     SDERDALFTV SISLTPAGAQ RLDEIEATLF AAIDQIRESG LDEWRYDEQA QLAEQQFRFQ
     QHGSPLQGAM RLAMNLARFP VEDVQYAAYR MDGFDRELVM QYLDGLRPDR LLRLYSAPDV
     EGAELSPWFN APWREVSADD PARAEPLAGL ALPEPNPFIA EDLTLLEAQH ERPSQLLDEP
     SFALWHMADA SFNTPKAEWR ISLQHPAANS DPRQAALAHL LAGWLDDSLN EDFYAARLAG
     HHAEAYAHAR GITLSFSGWR DRQDRVMQRT LTQLQQGEID EANFERARYR LQREWRNAPQ
     AALFRQAHRT LTEALVRPQW PTDDLLEASR ALDVEALRDF RDAFLADLHM EALAVGNLDE
     ELAIQEGRLM AEMLQPRAPK EAIPDLTPLR IEEGLPTLHP VTSREESLVL RYLQGSDRSL
     ESQARLAVLG QVIDTPFYQR LRTEEQLGYV VSASYSPLLD APGLSLLVQS PDTPSDEILA
     HIDTFLDAFG EQLAAMDDDD LEAYRQAVHD NLLQRDTSLS GRTNRLWRAL SFGDTDFDRR
     ERLAARVLDV SADELSQAWP ELREAAIATI SFDPGDEPSD VANLTQHLAP MPEADD
//
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