ID W1N9L1_9GAMM Unreviewed; 978 AA.
AC W1N9L1;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 32.
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=BJB45_09540 {ECO:0000313|EMBL:ERL52198.1};
OS Halomonas huangheensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=1178482 {ECO:0000313|EMBL:ERL52198.1, ECO:0000313|Proteomes:UP000019113};
RN [1] {ECO:0000313|EMBL:ERL52198.1, ECO:0000313|Proteomes:UP000019113}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BJGMM-B45 {ECO:0000313|EMBL:ERL52198.1,
RC ECO:0000313|Proteomes:UP000019113};
RA Miao C., Wan Y., Jin W.;
RT "draft genome of Halomonas huanghegensis, strain BJGMM-B45T.";
RL Submitted (AUG-2013) 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:ERL52198.1}.
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DR EMBL; AVBC01000019; ERL52198.1; -; Genomic_DNA.
DR AlphaFoldDB; W1N9L1; -.
DR MEROPS; M16.A01; -.
DR PATRIC; fig|1178482.3.peg.1072; -.
DR eggNOG; COG1025; Bacteria.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000019113; 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:UP000019113};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..978
FT /note="Protease 3"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004807459"
FT DOMAIN 69..205
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 231..406
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 415..685
FT /note="Peptidase M16 middle/third"
FT /evidence="ECO:0000259|Pfam:PF16187"
FT DOMAIN 688..863
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT REGION 946..978
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 978 AA; 108551 MW; 58AD429BF9A1E9B5 CRC64;
MATTPRRRGR VLLVTLCALT LPWQAAGILA AETSDQAIPA EVADVTTPIV SPHDQRDYRV
LTLDNGLEVL LVSDPEADKA AASMNVAVGS SQDPDDLQGL AHLLEHMLFL GTDAWPEPDA
YQGYISRHGG NHNAFTASRD TNYFFDIEPN ALEGALDRFS HFFIDPLFNA DQLGSERTVV
NSEYQARLRD DSRRENEVLD ALLNPENPTV GFSVGSTETL ADRPEGEPSL RDRVMQFYEQ
HYGAGVMHLS VVAPLPLDQL TRMVSEDFSA IPNRDLERAS ITTPLVETDR LPMAAEVQSL
RDERHVTFMF PIEDPILSYR TKPDSYIANL LGHEGPGSLL SELRKEGWAD GLSAGTARSD
GQHALFSVDI SLTPEGAKHI DRIQASLFAA IKQIREDGVS ESRYDEQASL ADQSFQFQQH
GSPIDEVTRL SMNLAYYPLK DVNRAAYRMD GLDRDEAEQW LDALRPERLL RLYSGPDVDS
EQRTRYYDTA WRKVPLKANE AQPVSGLALP APNPFIAEDL ALLDQHQDIP TVLLDSPQAD
IWYKADSEFD TPRVSWRISL QHPESSQSAR QAAMARLLAG WLNDSLNDQL YAARLAGQSY
TAYAHSRGMT LSFTGWRDRQ SLVMQQVIDQ LLNGEIEASN LERVRYGLKR QWSNTPRDPL
YYQAQRTLSE ALIRPQWSTP VLLEALDDIS LDDLRNYRDD FLSQLHVQAL AVGNLDKDLA
NDEAQQVIDK LQPQLSADDI PDLVVLDAND LPALTPESTR EESILLRYLQ GSDQSVTTQA
RLAVLGKLLE TPFYQRLRTE QQLGYVVNAG YSPLLYAPGI SMLVQSPATP SAELRQHVDA
FLNGVPQMLS NLDDEDLTTY RQAVHDELLV RDTSLPERTS RLWGALSWGD LQFDHHQRLA
AAVLEVNASD LSNAWGDLLG HDVVDVTFDP GASPSDVAGL KAGLEVLPGD SNANSTSDAP
HSEIPAANLK DATGSDTH
//
