ID A0A0N1MSR5_9GAMM Unreviewed; 959 AA.
AC A0A0N1MSR5;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=ADS77_18415 {ECO:0000313|EMBL:KPH58045.1};
OS Pseudoalteromonas porphyrae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=187330 {ECO:0000313|EMBL:KPH58045.1, ECO:0000313|Proteomes:UP000037848};
RN [1] {ECO:0000313|EMBL:KPH58045.1, ECO:0000313|Proteomes:UP000037848}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCD-SED14 {ECO:0000313|EMBL:KPH58045.1,
RC ECO:0000313|Proteomes:UP000037848};
RA Coil D.A., Jospin G., Lee R.D., Eisen J.A.;
RT "Draft Genome Sequence of Pseudoalteromonas porphyrae UCD-SED14.";
RL Submitted (AUG-2015) 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}.
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:KPH58045.1}.
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DR EMBL; LHPH01000027; KPH58045.1; -; Genomic_DNA.
DR RefSeq; WP_054455760.1; NZ_LHPH01000027.1.
DR AlphaFoldDB; A0A0N1MSR5; -.
DR STRING; 187330.AMS58_15570; -.
DR PATRIC; fig|187330.3.peg.2331; -.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000037848; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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 57..191
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 221..397
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 401..677
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"
SQ SEQUENCE 959 AA; 108355 MW; D9806DB95479C703 CRC64;
MKKIITLSAI ALAVLSGCGT TTTPVQQQTS LLSDTLVVSQ NDNREYKTLK LANEIEVILV
SDPSAEKSAA ALSVGVGLLH DPMSQQGMAH YLEHMLFLGT ERYPDTKGYS DFMTKNGGAH
NAYTWLDITN YMFKVNNDAY DEGLDRFADF FKSPKLYPEY TDKEKNAVNA EWSMRREMDF
FGQFKLARKM MGDHPANRFL IGNLETLGDK EGSSLHKETV DFYNKYYSAN IMKVAMISNL
PLAEMEAKAQ KYFADIEDKK IDKPTVTKKL DFDNVGGKRV HYAPNEDVKQ LQLDFTITDN
SDEFAVKPNR FVAYLLSNEM QGSPAQILRD KGWVSQLSAS SSPTHYGNYG MLSVDIQLTD
EGMKNRETIV ATIMQYIDLI KREGVDSKYF NEIRTSLNNE FKFLEKGDEF GYVSNLAGSM
QDYPLNHAIN APYHYAQFDA DAINEVLAQL NAQTLRIWYT SQQEKTDSKL HFYDGKYRIA
DIGESEIASW NKPSEFALAL PTVNRLLPES FAIKTTQFSE QKHPELTYDK NGVKVWRQAS
QNFAEQPKGL VEVYLNTPDA LADIKAKVLY SVWADLYNLQ QSKLSTEAAV AGMSVGLEDS
NGLILSMSGF TDKQNVLLAQ ALESIDVKVA EQGFAQALDR YQRDLLNAQK QFPYYQAFGE
YSKLVRTGSF DTDALIKTAQ TLTIADFEEL KNQTFSRNEL RVFTFGNYNQ EDVEAIAKEL
TAILPKDHKS TSFTRSKAWL PQVGETIVLQ KDIDVADVAI IDMTVHPIAG YKQKAQAQVL
QDHFRTIAFD KMRTEEQLAY AVGALARSVE DYSAIGLFIQ TPVKGPKEMQ ARFEAFKKQY
AVELEAMSEE TFAQLKNATL VSLKEQPKNL SDEMGPLIGD WYRENFDFNS KQKLISEVEK
VTLADIKDYY KQTMLNPQAA RLNVQLRGSK FADTPFADLP KQTLVTDLKA HFNGIKLQK
//
