ID A0A0X8HGV2_9GAMM Unreviewed; 960 AA.
AC A0A0X8HGV2;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
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:AMD02335.1};
GN ORFNames=LOKO_03289 {ECO:0000313|EMBL:AMD02335.1};
OS Halomonas chromatireducens.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=507626 {ECO:0000313|EMBL:AMD02335.1, ECO:0000313|Proteomes:UP000063387};
RN [1] {ECO:0000313|EMBL:AMD02335.1, ECO:0000313|Proteomes:UP000063387}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AGD 8-3 {ECO:0000313|EMBL:AMD02335.1,
RC ECO:0000313|Proteomes:UP000063387};
RX PubMed=26988058;
RA Sharko F.S., Shapovalova A.A., Tsygankova S.V., Komova A.V.,
RA Boulygina E.S., Teslyuk A.B., Gotovtsev P.M., Namsaraev Z.B.,
RA Khijniak T.V., Nedoluzhko A.V., Vasilov R.G.;
RT "Draft Genome Sequence of 'Halomonas chromatireducens' Strain AGD 8-3, a
RT Haloalkaliphilic Chromate- and Selenite-Reducing Gammaproteobacterium.";
RL Genome Announc. 4:0-0(2016).
RN [2] {ECO:0000313|EMBL:AMD02335.1, ECO:0000313|Proteomes:UP000063387}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AGD 8-3 {ECO:0000313|EMBL:AMD02335.1,
RC ECO:0000313|Proteomes:UP000063387};
RA Wen L., He K., Yang H.;
RL Submitted (FEB-2016) 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}.
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DR EMBL; CP014226; AMD02335.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0X8HGV2; -.
DR STRING; 507626.LOKO_03289; -.
DR KEGG; hco:LOKO_03289; -.
DR PATRIC; fig|507626.3.peg.3285; -.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000063387; Chromosome.
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:AMD02335.1};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:AMD02335.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000063387};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 77..192
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 237..413
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 421..692
FT /note="Peptidase M16 middle/third"
FT /evidence="ECO:0000259|Pfam:PF16187"
FT DOMAIN 696..870
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT REGION 930..960
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 940..960
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 960 AA; 107486 MW; F8DCEC5EA70A16A0 CRC64;
MSSLATSPQG QRHWSKPFAG LLLAGALLNG ALLPTAAAET AEQAAEAAID EIVTPRVSPH
DTRDYRVLTL ENGLTALLVS DPDADRAAAS MNVGVGSAQD PDDLAGLAHF LEHMLFLGTE
PFPEADAYQG YLRRHGGSHN AFTAPQDTNY FFDIEPEALT GALDRFSQFF LTPLFNPDQL
ESERNIVHSE YMARIRDDGR RELDVLNQVL NPDNPTVGFS VGSRETLDPP EGEASLRQRV
IDFYERYYDA NVMHLALVAP HSLDELETMV IERFADIADR GLERPVIEEP LVREESLPLK
LEMQSVRNSR HVRFMFPVPD SIQYYEHKPA DYLAHLLGHE GEGSLLAVLR EAGLADGLSA
GVGRSDERDA LFTVSISLTP AGAERLDEIE ATLFAAIDQI RESGLDEWRY DEQAQLAEQQ
FRFQQHGSPL QGAMRLAMNL ARFPVEDVQY AAYRMDGFDR ELVERYLDEL RPDRLLRLYS
APDVEGEQIS PWFNAPWREA SDTGPATAEP LAGLSLPEPN PFIAEDLTLL TEQHERPSQV
LDEPSFALWH MADASFNTPK VEWRISLQHP AANSDPRQAA LAHLLAGWLD DSLNEDFYAA
RLAGHHAEAY AHARGITLSF SGWRDRQDRV MQRTLAQLQQ GEINEASFER ARYRLQREWR
NAPQAALFRQ AHRTLTEALV RPQWPTNDLL EASRDLDVQA LRDFRDALLS DLHMEALAVG
NLDEELAIRE GRQIAELLQP QAAKEAIPDL TPLRIVSDLP PLHPVTSREE SLVLRYLQGS
DRSLTSQARL AVLGQVIDTP FYQRLRTEEQ LGYVVNAGYS PLLDAPGLSL LVQSPDTPSD
EILTHIDAFL DAFGERLGAL EDDELAAYRQ AVHDNLLQRD TSLSGRTNRL WRALSFGDTD
FDRRERLAAR VLDVSADELR QAWPELREGA TATISHDPGD EPSDVADLTR HLEPMPEADD
//
