ID Q5E3U2_ALIF1 Unreviewed; 925 AA.
AC Q5E3U2;
DT 15-MAR-2005, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2005, sequence version 1.
DT 27-MAR-2024, entry version 94.
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=ptrA {ECO:0000313|EMBL:AAW86304.1};
GN OrderedLocusNames=VF_1809 {ECO:0000313|EMBL:AAW86304.1};
OS Aliivibrio fischeri (strain ATCC 700601 / ES114) (Vibrio fischeri).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Aliivibrio.
OX NCBI_TaxID=312309 {ECO:0000313|EMBL:AAW86304.1, ECO:0000313|Proteomes:UP000000537};
RN [1] {ECO:0000313|EMBL:AAW86304.1, ECO:0000313|Proteomes:UP000000537}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700601 / ES114 {ECO:0000313|Proteomes:UP000000537};
RX PubMed=15703294; DOI=10.1073/pnas.0409900102;
RA Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R.,
RA Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E.,
RA Stevens A., Visick K., Whistler C., Greenberg E.P.;
RT "Complete genome sequence of Vibrio fischeri: a symbiotic bacterium with
RT pathogenic congeners.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(2005).
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; CP000020; AAW86304.1; -; Genomic_DNA.
DR RefSeq; WP_011262338.1; NC_006840.2.
DR RefSeq; YP_205192.1; NC_006840.2.
DR AlphaFoldDB; Q5E3U2; -.
DR STRING; 312309.VF_1809; -.
DR MEROPS; M16.008; -.
DR EnsemblBacteria; AAW86304; AAW86304; VF_1809.
DR KEGG; vfi:VF_1809; -.
DR PATRIC; fig|312309.11.peg.1837; -.
DR eggNOG; COG1025; Bacteria.
DR HOGENOM; CLU_004639_1_1_6; -.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000000537; Chromosome I.
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, ECO:0000313|EMBL:AAW86304.1};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:AAW86304.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000537};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 22..155
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 182..361
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 366..643
FT /note="Peptidase M16 middle/third"
FT /evidence="ECO:0000259|Pfam:PF16187"
FT DOMAIN 647..824
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 925 AA; 106773 MW; 82A33033365B92CC CRC64;
MHISPNDKKH YRLIELDNKL PVLLIQDETA PRSAAALSVN VGHFDDPDDR QGLAHFLEHM
LFLGTQKYPK VGEFHSFINQ QGGSNNAWTG TENTTFFFEV SHSAFEEGLD RFGQFFYASL
FNEEAVDKER NAVDSEYKLK LKDDVRRIYQ VHKETVNQAH PFSKFSVGSI DTLADKESSS
IRDEMLTFYQ THYSADLMTA VVLGNRPLCE LELLATQSFA SIPNQNLGHK EINVSYVTPK
EQSCWINIEP LKEVRKLSLA FHLPNQDRFY KTKPLNYLGH LLGYEGDGSL MLYLKKLGYI
HSLTAGGGVS GSNFREFTLS FNLTEKGMLH LDEIILNTYQ YIELIKQQGL DEWRYNEKKA
VLESAFQFQE KTKPLDLVSH LVMNLQRYHK EDAMYADYMM EGYHEQHVLD LLEQFTPEKM
RVTLVAQDLQ YDRKDKWYHT PYSVQPLSEA QIKSWSHAEL HPELHLPEKN PYICYDLEPQ
ELKETTVLPT LLEDLPGFRL WHKQEEEFRV PKGMVYIAID SPHAISDPRK IVKTRLCVEM
LMDALSEQTY QAEIAGMGYN LYCHQGGVTL TLSGFSQKQP LLLDVILKRF STREFSAERF
DFIKNQLIRH WGNASKERPI SQLFNALSGI LQPNNPPYPV LLEALESIEV DDLPNFVQAM
FAELHVEMFV YGDWTKEQAL ELGRSLKDTL RMQNQTYGES FRPLVMLGES GTFQRELVCD
HSDSALLVYY QSPQEDPRSF ALYTLANHLM SASFFHEIRT KQQLGYMVGT GNLPLNKHPG
LILYVQSPMA PPAILLDAID EFLNAFYMVL LELNEHQWQS SKQGLIDQIS DPDTNLRGRA
QRLWTCIGNK DTNFDHKERV TEELKSLTRI EMIRFVVGIL KPRTANRLIM HSQGTEHQQY
DRLDVGFEID SIDQFQLRKK DINLG
//
