ID A0A1H6RAX2_9GAMM Unreviewed; 972 AA.
AC A0A1H6RAX2;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
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=SAMN05421831_103226 {ECO:0000313|EMBL:SEI52998.1};
OS Allopseudospirillum japonicum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Allopseudospirillum.
OX NCBI_TaxID=64971 {ECO:0000313|EMBL:SEI52998.1, ECO:0000313|Proteomes:UP000242999};
RN [1] {ECO:0000313|Proteomes:UP000242999}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7165 {ECO:0000313|Proteomes:UP000242999};
RA Varghese N., Submissions S.;
RL Submitted (OCT-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}.
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DR EMBL; FNYH01000003; SEI52998.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H6RAX2; -.
DR STRING; 64971.SAMN05421831_103226; -.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000242999; 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; 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.
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:UP000242999};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 55..176
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 216..394
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 403..685
FT /note="Peptidase M16 middle/third"
FT /evidence="ECO:0000259|Pfam:PF16187"
FT DOMAIN 689..850
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 972 AA; 110094 MW; 093B34A48A9DA162 CRC64;
MLSSRHYKAP IRLFSTLLFC VLSLIMSKLQ AATIHKPLND ARTYHAFTLE NGLQVLAITD
PEAEKAAVAM HIGAGSHHEP KAYPRLAHFL EHMLFLGTRT YPQADAYAAY INQHGGQHNA
MTAHEYTQYF FDVNHKDLEG ALARFAPFFS EPLLDPQYVQ REVKAVDSEY SAKLQQDGRR
ILGALRQAFH PDHPLAHFSA GNAQTLPVDD PQLVPALREF FETYYRAPNM RLVVMGSQSV
EQLTTWVRTY FAQIGANLDK KEESKPSDSL ALWSDQHPLP LRLEVQTLKD ERTLKLYFPV
PHPKTLYPLR PVQFLANFLG HEGEGSLHAH LDALGWITQL GAGLDLPSGE QAFFALTLGL
TPEGAQHQTD ILQKIFSYIQ LVRTQGMAEW RYQEMALLAQ QSFDFQEPLS GIHYVSRLAN
NLYLYPVEDA LQASYRFGTF DVDAIQPYLE ALRPQNLLLL YAAPPQDFTE QTQYPWQKSP
WYPTLYRLAP QTIQTLADIT DASTLGLQLP EANPYIADAL PILARASQEP MHTLLDTPEI
KLWHSLSTLQ TPKANLFIYL KSPVSQRSLR EHMLTALWIN AASDAINTQA YPASLAGLTA
HLYQASEGVT LRTLGYAPKQ IEFALDLLEQ VQTLQITPER FAQLQAEMQR ALSNMQHKPL
TSQMFHALSS ALFDPAWSVQ EQAQALAQLT LADLQNFQTE FFTHLQLEIL SYGNLTTTEA
QHLAEQLKSK LHLDASQVST PRRARLLPTQ TKTYLWKPEI QHNDHAQLLY LQAQQTDVQT
QAQFALLAQM QRADFFHQLR TEQQLGYVVF TQEVSLLDRA GLVYVVQSPH IQPDALAQQI
QNFLQAYQTQ MANLTDDALM RFKEGVIASL RQPYPRLSSR AATRWMDIRL GYIEQARKEA
IADAVDQISL TQMHDFYQQL LTYPKLWLQV TGESATTVEN AANPEIAHPT LSAQVVDLQQ
IRTWASYSPV LP
//