ID Q0RDT2_FRAAA Unreviewed; 470 AA.
AC Q0RDT2;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE SubName: Full=Putative zinc protease {ECO:0000313|EMBL:CAJ64384.1};
DE EC=3.4.24.- {ECO:0000313|EMBL:CAJ64384.1};
GN OrderedLocusNames=FRAAL5752 {ECO:0000313|EMBL:CAJ64384.1};
OS Frankia alni (strain DSM 45986 / CECT 9034 / ACN14a).
OC Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia.
OX NCBI_TaxID=326424 {ECO:0000313|EMBL:CAJ64384.1, ECO:0000313|Proteomes:UP000000657};
RN [1] {ECO:0000313|EMBL:CAJ64384.1, ECO:0000313|Proteomes:UP000000657}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACN14a {ECO:0000313|Proteomes:UP000000657};
RX PubMed=17151343; DOI=10.1101/gr.5798407;
RA Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N., Couloux A.,
RA Cournoyer B., Cruveiller S., Daubin V., Demange N., Francino M.P.,
RA Goltsman E., Huang Y., Kopp O.R., Labarre L., Lapidus A., Lavire C.,
RA Marechal J., Martinez M., Mastronunzio J.E., Mullin B.C., Niemann J.,
RA Pujic P., Rawnsley T., Rouy Z., Schenowitz C., Sellstedt A., Tavares F.,
RA Tomkins J.P., Vallenet D., Valverde C., Wall L.G., Wang Y., Medigue C.,
RA Benson D.R.;
RT "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT reflect host range and host plant biogeography.";
RL Genome Res. 17:7-15(2007).
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; CT573213; CAJ64384.1; -; Genomic_DNA.
DR RefSeq; WP_011606826.1; NC_008278.1.
DR AlphaFoldDB; Q0RDT2; -.
DR STRING; 326424.FRAAL5752; -.
DR KEGG; fal:FRAAL5752; -.
DR eggNOG; COG0612; Bacteria.
DR HOGENOM; CLU_009902_3_0_11; -.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000000657; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
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; PTHR11851:SF149; GH01077P; 1.
DR PANTHER; PTHR11851; METALLOPROTEASE; 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:0000313|EMBL:CAJ64384.1};
KW Protease {ECO:0000313|EMBL:CAJ64384.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000657}.
FT DOMAIN 61..208
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 217..391
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 470 AA; 49220 MW; B32BCF9020D67D66 CRC64;
MSDTPTPDLT RSTDGAGGTG ASVRGAADAG ERVARLLAGG SGSETLLGGA VRRTVLPGGL
RVITERVPGV RSAAIGVWVG VGSRDETPVT AGCSHYLEHL LFKGTPTRDA LTISASVEAV
GGDLNAFTGK EYTCYYARVL DSDLAMAVGV VADMVTNSLV TADDVEAERG VILEEIAMHE
DDPGDVVHDV FAEAMLGASA LGRPVLGTIE SIEGLGRETI ADYYRSRYVP PAMVVSVAGN
LEHDRVLALV ADAFGDHLTS AGDPSAVRAG RYDYPPAPGI VVSERPTEQA NLVLGTVGVS
RHDPRRFALG VLSTALGGGM SSRLFQEVRE KRGLAYSVYS FASHFADAGL FGVYAGCAPK
RADEVLAIAR DQVRSIAERG ISAEELDRAR GQSHGSLVLG LEDTGSRMSR LGKSELVHGE
LLSVDEIIAR VDAVTLDDVR QVAASLVEQP WALGVIGPFD DHDFGAAVAR
//