ID I2B5X8_SHIBC Unreviewed; 962 AA.
AC I2B5X8; K6VY94;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 52.
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 Name=ptr {ECO:0000313|EMBL:AFJ45932.1};
GN OrderedLocusNames=EBL_c08090 {ECO:0000313|EMBL:AFJ45932.1};
OS Shimwellia blattae (strain ATCC 29907 / DSM 4481 / JCM 1650 / NBRC 105725 /
OS CDC 9005-74) (Escherichia blattae).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shimwellia.
OX NCBI_TaxID=630626 {ECO:0000313|EMBL:AFJ45932.1, ECO:0000313|Proteomes:UP000001955};
RN [1] {ECO:0000313|EMBL:AFJ45932.1, ECO:0000313|Proteomes:UP000001955}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29907 / DSM 4481 / JCM 1650 / NBRC 105725 / CDC 9005-74
RC {ECO:0000313|Proteomes:UP000001955};
RX PubMed=22843577; DOI=10.1128/JB.00829-12;
RA Brzuszkiewicz E., Waschkowitz T., Wiezer A., Daniel R.;
RT "Complete genome sequence of the B12-producing Shimwellia blattae strain
RT DSM 4481, isolated from a cockroach.";
RL J. Bacteriol. 194:4436-4436(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 ---------------------------------------------------------------------------
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; CP001560; AFJ45932.1; -; Genomic_DNA.
DR RefSeq; WP_002442347.1; NZ_BAHA01000016.1.
DR AlphaFoldDB; I2B5X8; -.
DR STRING; 630626.EBL_c08090; -.
DR MEROPS; M16.001; -.
DR KEGG; ebt:EBL_c08090; -.
DR PATRIC; fig|630626.3.peg.793; -.
DR eggNOG; COG1025; Bacteria.
DR HOGENOM; CLU_004639_1_3_6; -.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000001955; 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, ECO:0000313|EMBL:AFJ45932.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001955};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..962
FT /note="Protease 3"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003655136"
FT DOMAIN 55..192
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 217..394
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 401..675
FT /note="Peptidase M16 middle/third"
FT /evidence="ECO:0000259|Pfam:PF16187"
FT DOMAIN 682..858
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT REGION 930..962
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 962 AA; 107172 MW; FC92FC19B48F63CA CRC64;
MPTCSTWLKS IFLLAALWAP LIQAKTSWTP LQETIHKSDQ DPRQYQAIRL DNGMVVLLVS
DPQAVKSLSA LVVAVGSLED PDTHLGLAHY LEHMTLMGSR HYPQPDSLSE FLKMHGGSHN
ASTAPYRTAF YLEVENSALA PAVDRLADAI ATPVLSPDYA ERERNAVNAE LTLARSRDGM
RMAQVSAETL NPAHPASRFS GGNLETLRDK PGSKLHDALV AFHDKYYSAG LMKAVIYSNK
PLAELAAIAA RTYGRIPDKK IRRPVIDTPV VTEAQKGILI HYVPALPRKM VRIEFRIANN
SAQFRSKTDE LINYMIGNRS KDTLSDWLQT QGLADSVRAD SDPVVTGNSG VMAISVSLTD
KGLARRDEVV AAVFSYLNML REKGIDKQYF DELAHVLDLD FRYPSITRDM DYVEWLADTM
LRVPVAHTLD VVNIADRYDS KAIGERLAMM TPQNARIWYI SPDEPHNKTA YFVNAPYATQ
KIPAATLEKW RQAAGQIQLQ LPALNPYIPD DFTLTTPGKT YTHPELLVKE PGLRVLYMSG
GRFADEPKAD VTVVLRNPGA MNSAKNQVMF ALNDYLAGLA LDELSNQAAV GGISFSSNAN
SGLMINANGY TQHLPALLSA LLQGYFSYTP TDAQLEQAKS WYLQMLDSAE KGKAYDQAIM
PVQMLSQVPY YSRPERRALL PSITVADLLA YREKLKTGAK PEWLIVGNMG EQQARTMAAD
INAQLGTRGT EWCRNKDILV DKPRKVIFTR TGSSTDSALA AVFVPTGYDE NTSNAYTALL
GQIIQPWFYT RLRTEEQLGY AVFSFPMVIG RQWGLGFLLQ SSDKQPAYLW ARYQAFFPTV
EQRLREMDEK TFARIRQAVI DQMQQPPQTL AQEAIRYSKD FDRANLRFDS RDKVIARLKQ
LTPAGVADFF HQAVIAQQGM AVLSQVSGSH NGKQEFAQPP GWEQAGDVGK LQQSMSLVRE
NQ
//
