ID   A0A1E3LV92_9SPHN        Unreviewed;       791 AA.
AC   A0A1E3LV92;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Peptidase M16 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=BFL28_19670 {ECO:0000313|EMBL:ODP36750.1};
OS   Sphingomonas turrisvirgatae.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1888892 {ECO:0000313|EMBL:ODP36750.1, ECO:0000313|Proteomes:UP000094487};
RN   [1] {ECO:0000313|EMBL:ODP36750.1, ECO:0000313|Proteomes:UP000094487}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCT13 {ECO:0000313|EMBL:ODP36750.1,
RC   ECO:0000313|Proteomes:UP000094487};
RA   D'Andrea M.M., Rossolini G.M., Thaller M.C.;
RT   "Draft genome of the agarase producing Sphingomonas sp. MCT13.";
RL   Submitted (AUG-2016) 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}.
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:ODP36750.1}.
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DR   EMBL; MDDS01000050; ODP36750.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1E3LV92; -.
DR   STRING; 1888892.BFL28_19670; -.
DR   OrthoDB; 9811314at2; -.
DR   Proteomes; UP000094487; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 3.
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:SF17; PROTEIN YHJJ; 1.
DR   Pfam; PF00675; Peptidase_M16; 2.
DR   Pfam; PF05193; Peptidase_M16_C; 1.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 3.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000094487};
KW   Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..791
FT                   /note="Peptidase M16"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5009132069"
FT   DOMAIN          45..160
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          204..380
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          533..653
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   REGION          480..502
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          688..708
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          726..760
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        736..750
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   791 AA;  84719 MW;  98AAD48C3E152C4B CRC64;
     MKKLLSSAAL AAALLFNASA SAQSAPPAQP ALIPTETFVL ANGLRVVMNV DRSDPVVAVA
     LVAHVGSGRE TKGRTGFAHM FEHLFFLNSE NLGPGGLDKL SARVGGEGAN GYTNLDQTVY
     LQTVPKDALE KMLWAEADKL GYFINTVTPA VVAKEIEVVK NEKRQSYDNQ PYGHLFPIMQ
     AALYPADHPY SWTTIGSLAD LSAATLDDVK QFYRRWYVPN NASLVISGDI DPKQTRAWVE
     KYFGEIPRGA AVDIPQPRGA SLPTTKRLMH LDSFAKLPQL TLVWPTVPEG DKDDAAVELL
     IDALAQGPDG PVYRAVVEQA KVSDAVRGNS WDEQMAGVAM LQVRGFDGVP LDRVASAIDS
     GLARFGTEGL TAARLERLKA VREAALYEWI GSVRGKVEAI GESETLRRKP DPADVMLSQL
     KAVSVDDVMR AYRTYMPGKP RLEVGFVPKA QPQLALSNAE TAKVVEEPIV QGAEAAVDQT
     AGRTQVARTP SRIDRSVEPP AGAEPVVTMP SIWTGALANG LALSGIEDRE LPVARFEIAI
     DGGQLRDDPK KPGAASLVAD MLTRGTRTRT REQFENALKA LGANVSVNVV EERTIISGTT
     LARNFGATAA LVHEMLTAPR WDPAELALAK AAATAGVQAS RAQPAYLGQM VARQAMYGTG
     VLANDPRGTP QSIAALTMED LQRFKAASYS PRAAHPHRRR SEPGGGAGRL CRAGARLAGR
     GPGGAWLGSV RRAGQDSDPV LRRARRQTVS DHAGAPRPGA RRVRLVPGAG EQLHPWRRRL
     CIAPDAGAAR G
//