ID A0A486XQD1_9BACT Unreviewed; 954 AA.
AC A0A486XQD1;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, 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 Name=ptrA_2 {ECO:0000313|EMBL:VHO03896.1};
GN ORFNames=RHT_01101 {ECO:0000313|EMBL:VHO03896.1};
OS Candidatus Rhabdochlamydia sp. T3358.
OC Bacteria; Chlamydiota; Chlamydiia; Parachlamydiales; Rhabdochlamydiaceae;
OC Rhabdochlamydia.
OX NCBI_TaxID=2099795 {ECO:0000313|EMBL:VHO03896.1, ECO:0000313|Proteomes:UP000335940};
RN [1] {ECO:0000313|EMBL:VHO03896.1, ECO:0000313|Proteomes:UP000335940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T3358 {ECO:0000313|EMBL:VHO03896.1};
RA Pillonel T., Pillonel T.;
RL Submitted (APR-2019) 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; CAAJGQ010000014; VHO03896.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A486XQD1; -.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000335940; 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, ECO:0000313|EMBL:VHO03896.1};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:VHO03896.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000335940};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..954
FT /note="Protease 3"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019795171"
FT DOMAIN 56..190
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 211..388
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 395..674
FT /note="Peptidase M16 middle/third"
FT /evidence="ECO:0000259|Pfam:PF16187"
FT DOMAIN 682..859
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 954 AA; 108489 MW; D653807899358F9A CRC64;
MKYFLSLICL SASLCAVDPS ALSYTIIQDQ CRVPILTPSL AERETEKIIL ENGLKILLIS
DKDTPQSSAG VCVGAGSWKD DHPGIAHFLE HMLFMGTEAY PDESEYMQFI KDHGGKVNAY
TAPDRTVYMF SIHNDAYAQA IDRLSHFFID PLFSTSCIQR ELNAVDNEHA KNIEHDGWRQ
YMILKETGNP DHPNCKFSTG NKDTLCEIPQ SDLKNWYSSH YNANCMHLVM ISSLSIAEMR
DLAVTKFSPV TNAPYQKKNP QSSLLSGQQK GSMIFIKPVK DLKTLSLCWE VPKEFAANLE
EKAPEFIAYI LNKEVKGSLF AKLKKGNIAE NFHVCCDRFS KDSLLFCIDI CLTDSGLLQI
DSTISYVFAA LERLRTEKLP DYLFQEFKAM ATIDYQYQSR KDAFEMASET ASDMLYEDLS
SYPIKTKIPT VFSPQRIHSF LNTLKPAECV YFVIAEPSKV GVVTDREEKW MKAKYAIIPI
DQKQLQAWQK PGINPEINLP GQNPYIPNQL TLQDTPLQEI PALIHQDEGS EVYFLADHYY
GTPETVFTFQ LKSPLFNQTP KAQVLADLWS YALQEMLADE LSFAKDAGIQ IELKLKPLEA
IIYIRGLSEK MPLFTKKVFQ ASKQVVCSQE KFQIYVSSLV ASYENVSKEL PVCQALEQMS
GVIFDQPTSQ QKLLALQKTC LKDLCDFSEK FSQCLYMQAL LYGNLNQELA TELCKEIQTI
LATKPYSLQS QAKAKVLLLS DLHGPYKLVF ETNRQGAAAL LLLQEGSFSF ESWAIQQVLS
QALESAFFET LRTKQQTAYI AKAWDDEKEK QLLQYFAVQS STHTPTDLLA RFELFLEDFD
KNLPMEISLE RFEKIRANLI TSLAMRSENM FNKAKETAKL AFYYQDFEWI NKQIDSLKAL
SYDYFCIAAQ KLISRKNSRR LAILVEGVMA DDKNFCYELT SKEDVQALGQ LTSN
//
