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Database: UniProt
Entry: A0A432ZJP6_9GAMM
LinkDB: A0A432ZJP6_9GAMM
Original site: A0A432ZJP6_9GAMM 
ID   A0A432ZJP6_9GAMM        Unreviewed;       961 AA.
AC   A0A432ZJP6;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 17.
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=CWI83_04160 {ECO:0000313|EMBL:RUO78237.1};
OS   Pseudidiomarina taiwanensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Idiomarinaceae; Pseudidiomarina.
OX   NCBI_TaxID=337250 {ECO:0000313|EMBL:RUO78237.1, ECO:0000313|Proteomes:UP000288279};
RN   [1] {ECO:0000313|EMBL:RUO78237.1, ECO:0000313|Proteomes:UP000288279}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PIT1 {ECO:0000313|EMBL:RUO78237.1,
RC   ECO:0000313|Proteomes:UP000288279};
RX   PubMed=30364313; DOI=.3389/fmicb.2018.02453;
RA   Liu Y., Lai Q., Shao Z.;
RT   "Genome-Based Analysis Reveals the Taxonomy and Diversity of the Family
RT   Idiomarinaceae.";
RL   Front. Microbiol. 9:2453-2453(2018).
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:RUO78237.1}.
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DR   EMBL; PIQG01000002; RUO78237.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A432ZJP6; -.
DR   OrthoDB; 9811314at2; -.
DR   Proteomes; UP000288279; 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:UP000288279};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          76..210
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          235..414
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          420..698
FT                   /note="Peptidase M16 middle/third"
FT                   /evidence="ECO:0000259|Pfam:PF16187"
FT   DOMAIN          703..882
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   961 AA;  108851 MW;  A3E5138E20A58CAD CRC64;
     MTSSYLTKVI SSVLKTSIFR WNSKPSVNQR SNTIRSVMVS PSHGGDSVVH ATDIIQSPAD
     QCHYQALTLA NGLRCCLVHS PEAQHSAAAM AVATGHFDDP EDAQGLAHFL EHMLFLGTEG
     YPAAEDYQNF IANHGGGHNA WTGTELSNYY FHILPEYFGQ ALDRFCRFFY QPLLHPDWVA
     KELESIDAEF HLKRQDELRR LYQVHKSTVN QAHPFAKFSV GNRNTLSDRP DRPLAQQLRD
     FFQSNYQAQW MTLVLVGPHS LAELQQLALQ YGEEIPGQPE RVKPAIDVPL YLPEQLAARI
     QMRPLKDVQR LIISFALPSI DADYAHKTTS FIAHILGYEG PGSLFSLLRE RQWIVSLAAG
     GGISGSNFKD FNINMQLTDE GLAHIDDIIA EVLAYIRLID AMAIEEWRYQ ERQNTIAQAF
     RYQERSRSKD LAPALAVNLQ QYKLEDVVFG DYRMDGLNHS FARQILQLMT PDNMRTTVIH
     KQVETDQIEP IYGSEYSFSP LSNDSLARFR AISASDSQAR LPQANPYTGQ LRPLHPVKRV
     QSVPELTVIN SKLRHWHLQE AEFRVPRAHL YLSFRLPAVT ATARSFALAR LWCELLLDYL
     SESCYDAEVA GLHYNIYPQQ QGITIHISGL SSGVATLSQQ LLITLQNATF SPHRFHVLRQ
     KLAQNWRSAL ASRPLNLLFS KFNVLVQPNT FAVCQLAEEL AEIDLADYQQ WRSQLFNEVA
     IESFSCGDII TEELHPVLEQ IQQLTAAAKL APLAQLDARG LAELQAQDFK VCEGLRQTHP
     DSALILAIQG EQTELREQAL FLLFNHLVNS AFFHQLRTEK QLGYLVGTSY LPIQQRPHLL
     FYVQSSNTDT EQLTTAVEHF LADFQLHLQQ FDADQLASAQ QAIRLQLLEP DTNLRLRAQR
     FWSSITQADT DFARLNQLAE ALEHLTPKDL QQFFNTAVLQ TTSRLYLKSE PTALTAVAEP
     D
//
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