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
//