ID   A9KTW1_SHEB9            Unreviewed;       929 AA.
AC   A9KTW1;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 76.
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=Sbal195_2850 {ECO:0000313|EMBL:ABX50016.1};
OS   Shewanella baltica (strain OS195).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=399599 {ECO:0000313|EMBL:ABX50016.1, ECO:0000313|Proteomes:UP000000770};
RN   [1] {ECO:0000313|EMBL:ABX50016.1, ECO:0000313|Proteomes:UP000000770}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OS195 {ECO:0000313|EMBL:ABX50016.1,
RC   ECO:0000313|Proteomes:UP000000770};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Brettar I.,
RA   Rodrigues J., Konstantinidis K., Klappenbach J., Hofle M., Tiedje J.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Shewanella baltica OS195.";
RL   Submitted (NOV-2007) 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; CP000891; ABX50016.1; -; Genomic_DNA.
DR   RefSeq; WP_006085472.1; NC_009997.1.
DR   AlphaFoldDB; A9KTW1; -.
DR   GeneID; 11772936; -.
DR   KEGG; sbn:Sbal195_2850; -.
DR   HOGENOM; CLU_004639_1_1_6; -.
DR   Proteomes; UP000000770; 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          27..143
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          187..360
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          371..647
FT                   /note="Peptidase M16 middle/third"
FT                   /evidence="ECO:0000259|Pfam:PF16187"
FT   DOMAIN          652..827
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   929 AA;  106456 MW;  48353879ED7CD0D4 CRC64;
     MQASQSIYKS PNDHRQYRYL VLDNALRVLL VEDQDASQAA ASMAVGVGHF DDPADRPGMA
     HFLEHMLFLG TEKFPDSGEY HAFINQHGGS NNAWTGTEHT NFFFTINEDV FADSLDRFSQ
     FFIAPKFDLE LVDRERQAIE SEFSLKLKDD IRRTYQVLKE TVNPLHPFSK FSVGNLVTLG
     GEQAQVRSEL LDFYQSHYSA NLMTLCLVAP LSLDELEDLA YHYFSGIQNL NLVKNYPQVP
     LFSENELLTQ IDIVPLKEQK RLSISFNFPG IDHYYKRKPL TYISHILGNE SHGSLLSYLK
     EQGLVNNLSA GGGVNGYNFK DYSIGLQLTD KGLANLDEII SCCFEYIELI KTQGLDEWRY
     LERANLLKMA FRYQEQVKSL DLASHLSINM HHYEVEDLVF GDYRMDGLDI PETIALLELM
     TPHNMRLQLI AQSVKTDRKA NWYHTPYKVR PIAPQSLVRW QVSSIRPELQ LPAANPFIVA
     DSIPRPDKSD VDVPVIVAES TGYRIWHKKD DEFNVPKGHM YLSLDSEQAS KTPKHAALTR
     LYVEMLLDYL TEPTYQAEVA GLSYNIYPHQ GGITLHLSGF TGNQETLLAL LIHKARERNF
     TEERFALIKS QLLRSWQNLA QAKPISQLFT SLTVTLQKSS YEPARMAQML EDISLEDLHN
     HVRAFYEKIY LEGLVYGDWL VSEAQALGKR LEHILSLVST PSAESTRELV NLTGQGTLLR
     ELAIDHQDSA IIVYYQSAVA TPEKMALFSL LNHTMSSTFF HELRTEKQLG YMVGTGYLPL
     NRHPGLIFYI QSPTTGPLHL LEAIDEFIAD FNYAVMQITN EEWESTKVGL ISQIMEHDAN
     LKTRSQRYWV SVGNRDYQFN QRELVVDEIT KLTRTDLLKF MMRKMRTKHS DRLVLFSTGE
     QHRTQAALQS EKMITDLKTF KQTAEKFNF
//