ID   B3PDW3_CELJU            Unreviewed;       959 AA.
AC   B3PDW3;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 75.
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   OrderedLocusNames=CJA_3166 {ECO:0000313|EMBL:ACE83881.1};
OS   Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp.
OS   cellulosa).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC   Cellvibrionaceae; Cellvibrio.
OX   NCBI_TaxID=498211 {ECO:0000313|EMBL:ACE83881.1, ECO:0000313|Proteomes:UP000001036};
RN   [1] {ECO:0000313|EMBL:ACE83881.1, ECO:0000313|Proteomes:UP000001036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ueda107 {ECO:0000313|EMBL:ACE83881.1,
RC   ECO:0000313|Proteomes:UP000001036};
RX   PubMed=18556790; DOI=10.1128/JB.01701-07;
RA   Deboy R.T., Mongodin E.F., Fouts D.E., Tailford L.E., Khouri H.,
RA   Emerson J.B., Mohamoud Y., Watkins K., Henrissat B., Gilbert H.J.,
RA   Nelson K.E.;
RT   "Insights into plant cell wall degradation from the genome sequence of the
RT   soil bacterium Cellvibrio japonicus.";
RL   J. Bacteriol. 190:5455-5463(2008).
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; CP000934; ACE83881.1; -; Genomic_DNA.
DR   AlphaFoldDB; B3PDW3; -.
DR   STRING; 498211.CJA_3166; -.
DR   KEGG; cja:CJA_3166; -.
DR   eggNOG; COG1025; Bacteria.
DR   HOGENOM; CLU_004639_1_1_6; -.
DR   OrthoDB; 9811314at2; -.
DR   Proteomes; UP000001036; 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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ACE83881.1};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001036};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          74..191
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          237..413
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          419..697
FT                   /note="Peptidase M16 middle/third"
FT                   /evidence="ECO:0000259|Pfam:PF16187"
FT   DOMAIN          701..878
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   959 AA;  107646 MW;  C40A1B0DACB9349E CRC64;
     MRITSPLPLM HTGNAKIMRA WIAALLLLTL FVAGCQSGQL RQAAPQDPSL VTIIKSPNDD
     RQYQALLLPN GLQVVLVSDP SLENSAASLA VGVGSAHNPV DQLGLAHYLE HMLFLGTEKY
     PEPDGFMKYT QANGGMTNAF TAYDKTNYMF QINAGKFDEA LDRFSDYFKK PTFDPHYSDK
     ERNAVHNEWS LQKAQDGWNL FALMGVTANP ANPSSKFNIG NLDTLVDKPD SKLHATMLAF
     YERYYSANIM KLTLVGKQSL PELKALAEKH FAAIPNKNIE LPHVTEPGLT KAEMGKSLYY
     KPIKDMRALY VDFPVKSNKE QWRLKPNEYV NNLITSEEQG TLGEQLRSKG LVKMVTAFVE
     PDIYGPDGIL RIQAELTDAG LQQQDEIIAA IFAYVDLIKR DGLKQNYFRE LQAMRAKDFD
     NAPKPQPLQQ AVGLTMSQFD LPVENLLNAD YVYERYDPKA IKSLLAQLDK RRARIWYINP
     GVETDKPIPY FDGTYALRET RADEYTRWAS LSAGYRFNLP PLNDLFTDKP APIVESLYLK
     PQAVVSAAGV EAYLVHPEHY REDKGALSVQ INVDFAKSSA RQAVLAELLN EVYNKQNVTL
     VDRAGRASLG VNLYLTVTSS QGISIQGYTT KHEQLLTQLL QSFVALEINE QRFAEAVDTL
     QKNLANRSKD HVFRQLFSHL GRVVTQQSYS PDEQLAALAQ VKREDLLSYY AAVKKDPLLR
     IFAAGNYSEA HVKHLAQTAA QLLPGTRAPR QRALNSYMTP AAGKPLVFSG DVELADSALL
     QAWFRPAKSD AEQAQLAVLN ALYGNAFFMQ LRTHEQLGYA VMSREYPVDD IPGFIMLVQS
     SSVDLPHIKA RIDKFRKDYL ATLKAIEPAE VDLARQALIA NVLQKPTDFY AEMNLYLNEF
     LQGKYRFDAR DRYLASLQQV TKADLVAIYE QLLYGDKGGT ALLQLRGTNF KDKPYAKVK
//