ID R8AN55_PLESH Unreviewed; 969 AA.
AC R8AN55;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 36.
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=PLESHI_14176 {ECO:0000313|EMBL:EON87779.1};
OS Plesiomonas shigelloides 302-73.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Plesiomonas.
OX NCBI_TaxID=1315976 {ECO:0000313|EMBL:EON87779.1, ECO:0000313|Proteomes:UP000014012};
RN [1] {ECO:0000313|EMBL:EON87779.1, ECO:0000313|Proteomes:UP000014012}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=302-73 {ECO:0000313|EMBL:EON87779.1,
RC ECO:0000313|Proteomes:UP000014012};
RX PubMed=23814109;
RA Pique N., Aquilini E., Alioto T., Minana-Galbis D., Tomas J.M.;
RT "Genome Sequence of Plesiomonas shigelloides Strain 302-73 (Serotype O1).";
RL Genome Announc. 1:e00404-13(2013).
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:EON87779.1}.
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; AQQO01000358; EON87779.1; -; Genomic_DNA.
DR RefSeq; WP_010864436.1; NZ_KB944511.1.
DR AlphaFoldDB; R8AN55; -.
DR STRING; 703.SAMEA2665130_02427; -.
DR MEROPS; M16.001; -.
DR PATRIC; fig|1315976.3.peg.2710; -.
DR HOGENOM; CLU_004639_1_3_6; -.
DR Proteomes; UP000014012; 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.
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:EON87779.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000014012};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..969
FT /note="Protease 3"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004451932"
FT DOMAIN 61..197
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 222..400
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 406..684
FT /note="Peptidase M16 middle/third"
FT /evidence="ECO:0000259|Pfam:PF16187"
FT DOMAIN 688..865
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT REGION 190..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 969 AA; 108447 MW; B2122960154F05AD CRC64;
MRQLNQPWRW KMWVWSLLVC LPLLWSQQSL AAWQVLPEPV QKSERDSREY QPIRLDNGMT
VLLVSDPKAT KSLAAVTLPV GSMDDPNSQL GLAHYLEHMI LMGSKKYPEA DGFSLFLNKN
GGSHNASTAP YRTSYYLEVE NSAFDPAVDR LADALAEPLL DAKNGDKERH AVNAELVMAR
SRDGMRMAGV DSETLNPKHP TARFSGGNLE TLSDKPNSKL HAELRKFYQR YYSANIMQAV
LYSNQPLEQM AKLADASFGR IADHKINAPQ VTVPLTTEKE EGIILHYVPV QPIKALRIDF
TIPNDSAAFR NKVNTYIGYM LDNRSPGTLA DWLLRQGLAD GIQSNADPML ARNAGTFSIY
ISLTDKGLAH RDEIVASVFR YLRELEQKGI QKSYFDEIAD VLMLDFRYQS ITRDMSYVED
LSDNMLRVPV QNVLNSGVLA DQFDPNAIRE RLASMTPQHA RIWYISPQEP HNKKAYFVNA
PYSVSRITPE QFTLWQQQGA ALNLKLPALN PYIPDDFSLQ KPVKTDNGQP VAVIAKNDLQ
AWLAPSQYFA DEPKGVVTLD LRNPQADNSA RHQVLFALTD YLASLSLDEL SYQAAIGGIS
FNSGNDNGLQ VSASGFTQHL PKLMLALLQG YRDFNPTAAQ LAQAKAWYRD RLDSVEKMRA
YQQAVQPLQS LSAVPYFERS ERLALLDSIT LDELLQYRQQ LLQQSTPALL AVGNFSEEQV
KNLATQIKSQ LQTQGKQPWY GETVVVSRAH HGYLARRISA SDSALAALYV PTGYSERDSQ
AQAALLGQIL QPLFFNQLRT KEQLGYAVFS YAMPVGRQWG LNFVLQTPEK TPAYLFERYQ
AFFKQADARL QSMPAEEFAQ FKNALLNELR QPPQTLDEEA QRLSGDFSRG NAAFNGRAQL
IAALEKLTQS QVYSFYHNAV MRGTGLSLLS QVQGGKGKEG FAHPAEWSAE ASVSALQQAL
DKISNSAAH
//
