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Database: UniProt
Entry: K2JQ56_9GAMM
LinkDB: K2JQ56_9GAMM
Original site: K2JQ56_9GAMM 
ID   K2JQ56_9GAMM            Unreviewed;       946 AA.
AC   K2JQ56;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 34.
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=B3C1_01415 {ECO:0000313|EMBL:EKE77428.1};
OS   Gallaecimonas xiamenensis 3-C-1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Gallaecimonas.
OX   NCBI_TaxID=745411 {ECO:0000313|EMBL:EKE77428.1, ECO:0000313|Proteomes:UP000006755};
RN   [1] {ECO:0000313|EMBL:EKE77428.1, ECO:0000313|Proteomes:UP000006755}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3-C-1 {ECO:0000313|EMBL:EKE77428.1,
RC   ECO:0000313|Proteomes:UP000006755};
RX   PubMed=23209203; DOI=10.1128/JB.01854-12;
RA   Lai Q., Wang L., Wang W., Shao Z.;
RT   "Genome Sequence of Gallaecimonas xiamenensis Type Strain 3-C-1.";
RL   J. Bacteriol. 194:6937-6937(2012).
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:EKE77428.1}.
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DR   EMBL; AMRI01000002; EKE77428.1; -; Genomic_DNA.
DR   RefSeq; WP_008482418.1; NZ_AMRI01000002.1.
DR   AlphaFoldDB; K2JQ56; -.
DR   STRING; 745411.B3C1_01415; -.
DR   PATRIC; fig|745411.4.peg.274; -.
DR   eggNOG; COG1025; Bacteria.
DR   OrthoDB; 9811314at2; -.
DR   Proteomes; UP000006755; 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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:UP000006755};
KW   Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..946
FT                   /note="Protease 3"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003859379"
FT   DOMAIN          52..189
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          215..390
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          396..669
FT                   /note="Peptidase M16 middle/third"
FT                   /evidence="ECO:0000259|Pfam:PF16187"
FT   DOMAIN          674..850
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   946 AA;  104939 MW;  F00251C156DF6B8C CRC64;
     MLLRTSTLVL ALGLALAGCQ QVSAPQPAPG TIITSPADSL HYRYLALDNG LKVVLASDPD
     ADKAAASLVV HVGHTADPKD RQGLAHFLEH MLFISTDKYP KVDEYRQFIE THGGSSNAGT
     GQVDTTFFFN IAPDQFAPAL DRFAQFFIAP SLDPAYVDRE KHAVYSEFEL KKQDDGRRIN
     EVLKATANPA NPASQFSVGD LETLADRPGD KVWADLKAFH DKYYHAGNMT LALVGKEDLD
     SLEAYARQYF AAIPKGKANP VQPTAAPYLP SQLGVRIDQA PLKDQRTLSL QFPVPNSQAH
     FLAKPLDYIA NMLSNAAPGA LYSELKGKGW VDSLSAYHYG PDDYELFNLD FNLTEAGAEH
     LDDITQATFA YIHKLQAQGV TEAYFDELRK AGNLDFRFQE KASALSLANY LASNLQQVPP
     LHLMDAGFLY QDFEPELIQG YLARLTPDNL RQLVVLPGAN TDKVEPRYQA PYKVSALSPE
     LKDKWASAQA DLALPPDNPY LAEDPRLKAL AENHPLPKKV VEEQGLSIWA LQDPEFRVPK
     VEKRVSLTRP MAGATESAMN SLYADLINEA LESEAYPASQ AGLYFGLSAT SLGLSYSLSG
     YDEKQPLLED KIWTALHLPG LTQAKFNQYR DALVRNWRNL HQEWPVNQVM ARLGSTLVRE
     SYDADSKADA LEKVSFRQFQ GFVAHYPDQL NLRAMAIGNL TDAEVASWGK SLENLLLREA
     KRIDKPLMHL AQLPAGKELG LKLDIDHHDA VLAMIYKGHQ QDATSQARYA LMGQILSAPF
     FGKLRTEQQL GYVVQAGYSS LGRSPALFLL VQSPVADPFA LRQHMDSFSK DFTATLAAMT
     PAQLDEQKAG LINSINQADK QLGDKTDRYW SYLGNGRPFD WRQQLVAAVQ VLTLADLQEF
     YQQQVLDDKD GRLLLWSQGQ QAKSGDMPKA CTNQACLDKL WQYKGE
//
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