ID F7RV22_9GAMM Unreviewed; 919 AA.
AC F7RV22;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 24-JAN-2024, entry version 41.
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=A28LD_0083 {ECO:0000313|EMBL:EGN76347.1};
OS Idiomarina sp. A28L.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae; Idiomarina.
OX NCBI_TaxID=1036674 {ECO:0000313|EMBL:EGN76347.1, ECO:0000313|Proteomes:UP000053031};
RN [1] {ECO:0000313|EMBL:EGN76347.1, ECO:0000313|Proteomes:UP000053031}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A28L {ECO:0000313|EMBL:EGN76347.1,
RC ECO:0000313|Proteomes:UP000053031};
RX PubMed=21742887; DOI=10.1128/JB.05648-11;
RA Gupta H.K., Singh A., Sharma R.;
RT "Genome Sequence of Idiomarina sp. Strain A28L, Isolated from Pangong Lake,
RT India.";
RL J. Bacteriol. 193:5875-5876(2011).
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:EGN76347.1}.
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DR EMBL; AFPO01000001; EGN76347.1; -; Genomic_DNA.
DR RefSeq; WP_007419078.1; NZ_AFPO01000001.1.
DR AlphaFoldDB; F7RV22; -.
DR STRING; 1036674.A28LD_0083; -.
DR PATRIC; fig|1036674.4.peg.80; -.
DR eggNOG; COG1025; Bacteria.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000053031; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000053031};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 30..164
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 191..366
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 375..667
FT /note="Peptidase M16 middle/third"
FT /evidence="ECO:0000259|Pfam:PF16187"
FT DOMAIN 686..839
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 919 AA; 103430 MW; 5F4F37C924D056F0 CRC64;
MNSSNTILTP ESSSADIHTY RSLRLPNGLR VLLVHSPSSQ HSAASFAVNA GHFQDPSSAP
GIAHFLEHLL FLGTKEFPQA DAFATRVNAH GGHFNAWTGT EHSNYYFTTA HPGFAETLMH
FGSLFIEPLL NDEWVEKERQ SIEAEYRLKL KDELRRLYEV NKATANPAHP FSKFSVGNAV
TLADSHAMKV RQRLEDFHQR YYVAQNAALV VAGPNTLDEL QSLAIKSFQG LPAGEVKPNL
PNEPMYLPEQ RGCLIRVRPL KQAARLILTF PLPEINTDYL HKTTSYIAHL LGHEGPGSLC
FFLRRQHWIN ELSAGGGMSG YNFKDFNINM QLTDEGLSHI DEIMQACYQY INIISAEGLT
DALYRERQRM IELAYQFPES MKTVDLVSQL SINMLHYEPE HIVSGDYRMD GLKVELAKQM
LAQMVPENTR ATLIHNDVVT SEKTHFYAAD YAIERFSAEH LNKLKKPLAA TYEAQFSVPQ
ANPYIPKRIT PNPISAPLGK RQVTSCERSG YYPSQLCDGN GVTLWHLQDE HFREPQAHIY
LSLQLPLANA SARNNAISRI WCELGQELLS EQFYDAEVAG MHFNLYPQQS GITLHLAGFS
DRQPTLFKDL MRSLAALRSS QQHFHSVRKQ LHRNWHAIHQ NKPVNHLFSL LHHQLQHGSY
TAEQLAASIE DLDFEHYCNL LPGMLRDAQA KLLIHGDIRA ETALELAQWV EQTLPVVPIQ
KTKALRSVKR LGTGITATHF HNEHSDSAFA FFVQGQSTSL QEKAHFLLLN HIFNPSFFNA
LRTEQQLGYL VGSSYIPMHG LPGLLCYVQS PSHTTEQINA AIQSFIQAFT EQLETIAESV
FEGAQTAVLS HLIDPALSLR VRAQRYWSSI INNHGEFTLA SEVAAVVETA TLSEFIKFCQ
SRLGEQLSAM TLASTKSAH
//
