ID   C3SWN0_ECOLX            Unreviewed;       962 AA.
AC   C3SWN0;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   24-JAN-2024, entry version 55.
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=ECs3678 {ECO:0000313|EMBL:ACI78869.1};
OS   Escherichia coli.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562 {ECO:0000313|EMBL:ACI78869.1};
RN   [1] {ECO:0000313|EMBL:ACI78869.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=TB182A {ECO:0000313|EMBL:ACI78869.1};
RX   PubMed=19439656; DOI=10.1073/pnas.0812949106;
RA   Leopold S.R., Magrini V., Holt N.J., Shaikh N., Mardis E.R., Cagno J.,
RA   Ogura Y., Iguchi A., Hayashi T., Mellmann A., Karch H., Besser T.E.,
RA   Sawyer S.A., Whittam T.S., Tarr P.I.;
RT   "A precise reconstruction of the emergence and constrained radiations of
RT   Escherichia coli O157 portrayed by backbone concatenomic analysis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:8713-8718(2009).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; EU896313; ACI78869.1; -; Genomic_DNA.
DR   RefSeq; WP_001138189.1; NZ_WJRH01000004.1.
DR   AlphaFoldDB; C3SWN0; -.
DR   MEROPS; M16.001; -.
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, ECO:0000313|EMBL:ACI78869.1};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          54..191
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          216..394
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          400..675
FT                   /note="Peptidase M16 middle/third"
FT                   /evidence="ECO:0000259|Pfam:PF16187"
FT   DOMAIN          681..857
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   962 AA;  107796 MW;  C98B3D6CDA41E1AC CRC64;
     MPRSTWFKAL LLLVALWAPL SQAETGWQPI QETIRKSDKD NRQYQAIRLD NGMVVLLVSD
     PQAVKSLSAL VVPVGSLEDP EAYQGLAHYL EHMSLMGSKK YPQADSLAEY LKMHGGSHNA
     STAPYRTAFY LEVENDALPG AVDRLADAIA EPLLDKKYAE RERNAVNAEL TMARTRDGMR
     MAQVSAETIN PAHPGSKFSG GNLETLSDKP GNPVQQALKD FHEKYYSANL MKAVIYSNKP
     LPELAKMAAD TFGRVPNKES KKPEITVPVV TDAQKGIIIH YVPALPRKVL RVEFRIDNNS
     AKFRSKTDEL ITYLIGNRSP GTLSDWLQKQ GLVEGISANS DPIVNGNSGV LAISASLTDK
     GLANRDQVVA AIFSYLNLLR EKGIDKQYFD ELANVLDIDF RYPSITRDMD YVEWLADTMI
     RVPVEHTLDA VNIADRYDAK AVKERLAMMT PQNARIWYIS PKEPHNKTAY FIDAPYQVDK
     ISEQTFADWQ QKAANIALSL PELNPYIPDD FSLIKSEKKY DHPELIVDES NLRVVYAPSR
     YFSSEPKADV SLILRNPKAM DSARNQVMFA LNDYLAGLAL DQLSNQASVG GISFSTNANN
     GLMVNANGYT QRLPQLFQAL LEGYFSYTAT EDQLEQAKSW YNQMMDSAEK GKAFEQAIMP
     AQMLSQVPYF SRDERRKILP SITLKEVLAY RDALKSGARP EFMVIGNMTE AQATTLARDV
     QKQLGADGSE WCRNKDVVVD KKQSVIFEKA GNSTDSALAA VFVPTGYDEY TSSAYSSLLG
     QIVQPWFYNQ LRTEEQLGYA VFAFPMSVGR QWGMGFLLQS NDKQPSFLWE RYKAFFPTAE
     AKLRAMKPDE FAQIQQAVIT QMLQAPQTLG EEASKLSKDF DRGNMRFDSR DKIVAQIKLL
     TPQKLADFFH QAVVEPQGMA ILSQISGSQN GKAEYVHPEG WKVWENVSAL QQTMPLMSEK
     NE
//