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Database: UniProt
Entry: A0A1F8JQQ7_9BACT
LinkDB: A0A1F8JQQ7_9BACT
Original site: A0A1F8JQQ7_9BACT 
ID   A0A1F8JQQ7_9BACT        Unreviewed;       964 AA.
AC   A0A1F8JQQ7;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
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=A3E26_03285 {ECO:0000313|EMBL:OGN64381.1};
OS   Chlamydiae bacterium RIFCSPHIGHO2_12_FULL_49_32.
OC   Bacteria; Chlamydiota.
OX   NCBI_TaxID=1797604 {ECO:0000313|EMBL:OGN64381.1, ECO:0000313|Proteomes:UP000176567};
RN   [1] {ECO:0000313|EMBL:OGN64381.1, ECO:0000313|Proteomes:UP000176567}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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:OGN64381.1}.
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DR   EMBL; MGLX01000013; OGN64381.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F8JQQ7; -.
DR   Proteomes; UP000176567; 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   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          55..184
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          209..388
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          394..677
FT                   /note="Peptidase M16 middle/third"
FT                   /evidence="ECO:0000259|Pfam:PF16187"
FT   DOMAIN          691..862
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   964 AA;  109645 MW;  0A983C7AAAED6BB5 CRC64;
     MIKSLLFFLF FSSLFASEKG YELIEDRAAL PLLNFSLSEK RVAKLRLDNG LEAYLVSDPG
     TEEAAASLSV EAGSWDDPQE YPGMAHFLEH MLFMGTHAFP DEREYWQYIQ DHGGSANAFT
     APDRTVYLFS IKPYAFEGAV ERFSHFFIDP LFSPACIHRE LHAVDQEHAK NIENDLWREW
     MIFKECGNPD HPNAKFSTGN AKTLSGIPQE ALKKWYQSHY SARVMHLILL SPQPLEQLIS
     LTSRLFSKIP SFPLEKNRID LPLASSKQRG HFTYISPIKD LRRLTLTWEI PSSFVLDEES
     HAPSLISYAL SHGGERGLLQ KLKEENLVED LAIEQNRLGK KEMLFSLILE LTHQGLSQID
     TVIARCFQAI ARLKCSGISP NLFQEMQKIS TLNYQYQSRE NAFAFVNRHG FSIVDESLST
     YPEKSTIPSS YNPAALSLFI EQLTPQNCLF TLHADPSLTG QPTTAKEKWM EAEYALGEIS
     KTKLLSWQEI HPHPHIRLPD ANPYLPENLA LKTPLPNAPS HSAPHLLYAG KDGKIYYAQD
     TKYLVPECGI FFNLKSSQID GSPQRQMLLD LFILALQDQN SQQNFFLKKA GYSLLLFSDQ
     MALKVELSGY SDKAPLILKE LFKKMKSLSI SSPQFIRYKE ELATCYENQS RNLPLMQALD
     FASGLLTNFH PTSAEKLVAL RALTFEESLP IFKELFDTVY AEGMIFGNLT ETEALQLSTT
     LKALFDAKPY LLADQKKREV LLLPKEEGPL LIEQKTERQG SGVLLIIDCG PFALENHAAE
     SLLASLLQEA FFDTLRTKQQ TAYIAKAFKK EIEHHIFQCF AVQSSTHTPT ELLFRFELFL
     EEFLRNFEAN LAPERFRALK EALAASLEMA PENLSSMTTL LHTLAFEHEG DFSFRKKRLE
     GLKELSYEEL HSFARKHLSR HNGGRLAVLM EGAPAKETLF HYRSLTKKEL NEKRTYTAGK
     EKNL
//
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