ID F3LG55_9GAMM Unreviewed; 951 AA.
AC F3LG55;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 45.
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=IMCC1989_299 {ECO:0000313|EMBL:EGG94117.1};
OS gamma proteobacterium IMCC1989.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales.
OX NCBI_TaxID=937772 {ECO:0000313|EMBL:EGG94117.1, ECO:0000313|Proteomes:UP000010300};
RN [1] {ECO:0000313|EMBL:EGG94117.1, ECO:0000313|Proteomes:UP000010300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMCC1989 {ECO:0000313|EMBL:EGG94117.1,
RC ECO:0000313|Proteomes:UP000010300};
RX PubMed=21602334; DOI=10.1128/JB.05202-11;
RA Jang Y., Oh H.M., Kim H., Kang I., Cho J.C.;
RT "Genome sequence of strain IMCC1989, a novel member of the marine
RT gammaproteobacteria.";
RL J. Bacteriol. 193:3672-3673(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:EGG94117.1}.
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DR EMBL; AEVK01000116; EGG94117.1; -; Genomic_DNA.
DR AlphaFoldDB; F3LG55; -.
DR Proteomes; UP000010300; 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:UP000010300};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 57..175
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 218..395
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 402..676
FT /note="Peptidase M16 middle/third"
FT /evidence="ECO:0000259|Pfam:PF16187"
FT DOMAIN 688..848
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 951 AA; 106810 MW; 515FF916D5ADE3D3 CRC64;
MSSSPSDISD VQDINMQTEP NKKNARKINA ENNSVEIEKG QIDDREYHYM VLDNQLKVLL
ISDPQADKAA ASLDVHVGSS DDPADREGLA HFLEHMLFLG TEKYPEAAAY QAFIDNNAGS
HNAYTSAEHT NYFFDIDAEQ LEPALDRFAQ FFIAPLFDQA YVDRERNAVH SEYQAKIKDD
SRRGYDVYRQ QINPQHPYAK FSVGSVETLA NRPNDNVRDD LLEFYQAHYS SHQMALVVLG
KESISDLEKI VNDRFVQIPL RDVKQDDVFI PLFDSARLPF EVISKPIKDT RQMSMVFPLP
SVKAYYGEKP LSYLGSLLGH EGEGSVLSLL KAKGWAEGLS AGGGDAGAGN ATFNVSVSLT
KEGVKHRADI RSVVFHALDV IKQSGIEEWR YAEEQSMANI AFQFREKGRA ISAVSSLADS
LHDYPAAEVI SANYRYTRFD AELIEGLLSR MTPNNLFVST VFPEVETDQI TEKYQVPYTV
QPLRAERVVL PDALIQQYAL PAKNIFIPTN AELFETDKTL SIPKKVVLKT VSDDEAESIL
WIKQDVSFKV PKANAFVRVQ SPLAASSPRS SALNQLLINM INDQLNENSY PASLAGLGYS
LSPNSRGFDV SVQGYNNKMP VLLAMLSAQV QQPVLSVDRF DQLKIELTRQ LNNTQQQTPY
KQLFGQLPVS LFSPYASDSR IVKELETISF QELKDFASRW LQGAQVSALI YGNVNSDDES
LWQSTLQEWV QLGDQALASA EVVKFPVLEE GAKHIPQVSL NVDHGDTAVG LYVQGTSDSL
SNQANMVLLR QVLDSAFYSQ LRTEQQLGYI VFLTSMTIKD VPGSFFIVQS PSASVDEIKQ
AIEAFLNQSE VLIPDDLSGF KRSVSTKLLE TPQTLSAKAS RYWQNVLKSN EDFDYRDSLV
EQINDINSQQ LRAYYKSTLL NSERLMWFVA NKDVASKEII FSEEQEYYRY R
//
