ID A0A0P1F5X8_THAGE Unreviewed; 444 AA.
AC A0A0P1F5X8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Protease 3 {ECO:0000313|EMBL:CUH63312.1};
DE EC=3.4.24.55 {ECO:0000313|EMBL:CUH63312.1};
GN Name=ptrA_1 {ECO:0000313|EMBL:CUH63312.1};
GN ORFNames=TG4357_00597 {ECO:0000313|EMBL:CUH63312.1};
OS Thalassovita gelatinovora (Thalassobius gelatinovorus).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Thalassovita.
OX NCBI_TaxID=53501 {ECO:0000313|EMBL:CUH63312.1, ECO:0000313|Proteomes:UP000051587};
RN [1] {ECO:0000313|EMBL:CUH63312.1, ECO:0000313|Proteomes:UP000051587}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 4357 {ECO:0000313|EMBL:CUH63312.1,
RC ECO:0000313|Proteomes:UP000051587};
RG Swine Surveillance;
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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DR EMBL; CYSA01000007; CUH63312.1; -; Genomic_DNA.
DR RefSeq; WP_058261390.1; NZ_FOFW01000007.1.
DR AlphaFoldDB; A0A0P1F5X8; -.
DR STRING; 53501.SAMN04488043_10799; -.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000051587; 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; 2.
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 PANTHER; PTHR43690; NARDILYSIN; 1.
DR PANTHER; PTHR43690:SF17; PROTEIN YHJJ; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
DR PROSITE; PS00143; INSULINASE; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CUH63312.1};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:CUH63312.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051587};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..444
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006062307"
FT DOMAIN 35..172
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 189..372
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 444 AA; 49342 MW; 03D4533684DFB606 CRC64;
MIRFVLGFAA FIATSLPALA DDQVSNFTLN NGMEVVVIED HRAPVVVQMV WYRAGSADEP
VGQSGVAHFL EHLLFKGTET LEPGEFSATV AKNGGRDNAF TSYDYTAYHQ RVAADRLELM
MQMESDRMVN LRLTETEIAT ERDVILEERN MRTENNPSAL FREQKSAVQY LNHRYGVPVI
GWRHEMEDLS LADALSFYGT YYSPNNAILV VAGDVDPEEV RTLATKYYGA IPANPDLPDT
RYRSQEPPQT AERRLTYRDA RVAQPYVSRS YLAPERDHGA QEKAAALTVL AEILGGGQTS
VLAEKLQFES QTAVYVGAYY GGTSLDDTTF DLVVVPAPGV SLQQAEDAMD QTLAEFLETG
IDTEQLTRIK TQIRASEIYA RDDVEGLANR YGRALTQGLT VKDVQEWPDI LQAVSADDIV
AAAKDVLDRR QSVTGWMMAE EVTQ
//
