ID   A0A1Q2H338_9GAMM        Unreviewed;       907 AA.
AC   A0A1Q2H338;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 26.
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=B0W48_19665 {ECO:0000313|EMBL:AQQ01797.1};
OS   Pseudoalteromonas aliena.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=247523 {ECO:0000313|EMBL:AQQ01797.1, ECO:0000313|Proteomes:UP000188243};
RN   [1] {ECO:0000313|EMBL:AQQ01797.1, ECO:0000313|Proteomes:UP000188243}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EH1 {ECO:0000313|EMBL:AQQ01797.1,
RC   ECO:0000313|Proteomes:UP000188243};
RA   Kim E., Heo E., Kim H., Kim D.;
RT   "Complete genome sequence of the cold-active Pseudoalteromonas aliena
RT   strain EH1 isolated from Arctic seawater.";
RL   Submitted (FEB-2017) 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}.
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DR   EMBL; CP019628; AQQ01797.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q2H338; -.
DR   STRING; 247523.B0W48_19665; -.
DR   KEGG; paln:B0W48_19665; -.
DR   Proteomes; UP000188243; Chromosome.
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..138
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          182..345
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          367..631
FT                   /note="Peptidase M16 middle/third"
FT                   /evidence="ECO:0000259|Pfam:PF16187"
FT   DOMAIN          651..789
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   907 AA;  104909 MW;  75E3E6277C1C8A84 CRC64;
     MNISRNDNRA YRAFTLDNGL KVLLVQDKDS TKAAASMAVN AGHFDDPVDR QGLAHFLEHM
     VFLGTDQFPE SGSFNNFVSQ AGGNTNAWTG TEHTCYFFDI NNQEFKRALQ QFSRFFIAPL
     LSPAETEKER NAIEAEFKLK IKDDGRRIYQ AHKETVNPAH PFAKFSVGNL QTLADRERCI
     SDELRDFFNT FYQAQWMTLV ICANEELDTL QDWTNTYFNQ VNGHKNLKKP AINEPLYRKQ
     DIGKILHIEP HKHMQKLIVS FAMPNIDDFY RHKTVSFIAH LLGYEGAGSL YSILKEQGWI
     NALSAGGGIN GSNFKDFNIS MALTDEGIEY FEDIIEMVFE YICLINTNTD KLPRLYQDKK
     NLLQIAFDNQ EKSRLIDWVS NLSINMQHYD ECNYVQGDYL MEGFKRATHE MAMQWLTPNN
     MRVVLIHPDV EPEHKTAWYN TPYKVEKVSS SWLDALSDIN EPLNEMLLPT ANPYLTKEVV
     LFDIEKPQTQ PKLLVKENGF DFWFKQDNTF RVAKGHFYLA MDSDFAVKDV KHMALTRLFT
     DLFMDSVGEQ FYPAELAGLS YHLTSHQGGL TLHTAGLSSS QLELVDQLID ALFNVEICAK
     RFAEYKKQLV RHWRNSNQNK PVSELFSILG AKVMPWNPQP GDLASTLKNT SFQQFKEFRR
     DFFKALHVES FLHGNWQQDD AIAFQKKVAA HLKNATTIDD LRRPLFEIKK VTRYELELPC
     NDHAMVIYYQ AQTSSVTEKI KMMALNHLIN QDYFNELRTT QQLGYLVGAG YAPFNTRAGI
     AFYIQSPTFD TTTLIHRHNC FISQYLNTID KIDEHNWQQQ KHGLITHIAE KDKNLRLRSQ
     RLWLAIGNRD HEFNMQQKLL KALNALTLED IKEYAVQLFD EDRPRYELLS SAKVSKSQNM
     PIYSHSL
//