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Database: UniProt
Entry: A0A085FJA3_9BURK
LinkDB: A0A085FJA3_9BURK
Original site: A0A085FJA3_9BURK 
ID   A0A085FJA3_9BURK        Unreviewed;       945 AA.
AC   A0A085FJA3;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   SubName: Full=Zinc protease-like peptidase {ECO:0000313|EMBL:KFC71548.1};
GN   ORFNames=FG94_02337 {ECO:0000313|EMBL:KFC71548.1};
OS   Massilia sp. LC238.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Telluria group; Massilia.
OX   NCBI_TaxID=1502852 {ECO:0000313|EMBL:KFC71548.1, ECO:0000313|Proteomes:UP000028601};
RN   [1] {ECO:0000313|EMBL:KFC71548.1, ECO:0000313|Proteomes:UP000028601}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LC238 {ECO:0000313|EMBL:KFC71548.1,
RC   ECO:0000313|Proteomes:UP000028601};
RA   Gan H.M., Gan H.Y., Barton H.A., Savka M.A.;
RT   "Genome sequence of acyl-homoserine lactone-producing cave bacterial
RT   isolate.";
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261}.
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:KFC71548.1}.
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DR   EMBL; JNNN01000039; KFC71548.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A085FJA3; -.
DR   STRING; 1502852.FG94_02337; -.
DR   PATRIC; fig|1502852.3.peg.2289; -.
DR   eggNOG; COG0612; Bacteria.
DR   OrthoDB; 9811314at2; -.
DR   Proteomes; UP000028601; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
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   PANTHER; PTHR43690; NARDILYSIN; 1.
DR   PANTHER; PTHR43690:SF21; PROCESSING PROTEASE; 1.
DR   Pfam; PF00675; Peptidase_M16; 2.
DR   Pfam; PF05193; Peptidase_M16_C; 2.
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, ECO:0000313|EMBL:KFC71548.1};
KW   Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..945
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001789953"
FT   DOMAIN          56..140
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          209..387
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          533..657
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          681..856
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   REGION          478..508
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   945 AA;  103649 MW;  5ABE9BC134D557D7 CRC64;
     MKMSPLPLLL AACFTSTALF PAHAAKPAVA SQAAGLKVDY QKFTLPNGLD VIFHIDRSDP
     VVAVNLTAHV GSAREKAGRT GFAHLFEHLL FLESENLGKG GLDKMSARIG GSGANGSTSQ
     DRTNYLQTVP KDALEKMIWA EADKLGWFIN TVTDPVLAKE KQVVKNEKRQ GVDNAPYGHT
     RYVINKALYP LDHPYNWQVI GSLEDLQNAT LDDVKEFFRL WYVPNNVTLV IAGDFDPAQA
     RKWVEKYFSE IKRGAPIEAM AKRPGVVKQT VKLAHEDNFA KLPELTMAWP TVEDLHPDSY
     ALEVLAEYLS QTKRAPFYQV LVEDSKLAPS VQSSNQTGEL AGQFMLRVRA FEGKALDDVA
     GAIGQAFAKF EREGISERDL NRIKAGLETR FYSSVSSVLG KSALLAEYNY LTGNPGYVEE
     GVRKTLAVTT ADVRRVYDTY IKGKPYVATS FVPKGKLDLA LSGSAKADVV EEKVVQGAED
     KVEPSANAEY TRTPSAFDRS KEPPYGAAPS VKVPQVWDTK LANGMRVYGI ENKEVPLVQF
     DIAIDGGLLL DNPDKVGVAN LMARLMTQGT AKKTPQELEE AILQLGASIN VFARTEDVRI
     SVTTLARNYA ATVDLVREIL LEPRWDEKEF ALVKQSVLSQ IRQQEADPNA LASSNFNKLI
     YGKGDIRSRN ILGTSASVNA ISIEDLKAYY RANLSPSNAR MHVIGALPKD AVARPLAALS
     RAWEAKPVAL PAASAARGEA PGKVYFVDVP DAKQSVLHIG YRALAATDPD YYPATVANYI
     LGGGGFASRL TQELREGKGY TYGIRSSFAG SKSAGPFIIA SGVRSNVTLE STQLVKKILQ
     DYAPTYSAAD LETTRNFLVK SNARAFETAE AKLGMLDNIS KYGWRADYVK DRERIVKSMT
     LPQVQALSQK YLDPSKMVWL VVGDAKTQLP RMKELGFDEP VLIER
//
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