ID A0A0K1JVB2_9BURK Unreviewed; 942 AA.
AC A0A0K1JVB2;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Peptidase M16 {ECO:0000313|EMBL:AKU20926.1};
GN ORFNames=ACZ75_04880 {ECO:0000313|EMBL:AKU20926.1};
OS Massilia sp. NR 4-1.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1678028 {ECO:0000313|EMBL:AKU20926.1, ECO:0000313|Proteomes:UP000056897};
RN [1] {ECO:0000313|EMBL:AKU20926.1, ECO:0000313|Proteomes:UP000056897}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NR 4-1 {ECO:0000313|EMBL:AKU20926.1,
RC ECO:0000313|Proteomes:UP000056897};
RA Sul W.J.;
RT "Massilia sp. NR 4-1 isolated from rhizosphere of Torreya nucifera in
RT national heritage Bijarim forest, volcanic Jeju Island, Korea.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261}.
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DR EMBL; CP012201; AKU20926.1; -; Genomic_DNA.
DR RefSeq; WP_050407686.1; NZ_CP012201.1.
DR AlphaFoldDB; A0A0K1JVB2; -.
DR STRING; 1678028.ACZ75_04880; -.
DR KEGG; mnr:ACZ75_04880; -.
DR PATRIC; fig|1678028.3.peg.998; -.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000056897; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
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; PTHR11851:SF149; GH01077P; 1.
DR PANTHER; PTHR11851; METALLOPROTEASE; 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 Reference proteome {ECO:0000313|Proteomes:UP000056897};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..942
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005462470"
FT DOMAIN 55..190
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 208..378
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 480..619
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 626..816
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 942 AA; 104153 MW; 738313E05956801E CRC64;
MSRVLPLLTL ALSAPVFAAP APAAAPDLLP FKATEKVLPN GLKIIVVPTG FPNIVSLQIP
VQTGSRNEVE PGKSGFAHFF EHMMFRGTKE YPPEKYQDII TRAGARQNAY TSDDLTNYHT
TFAKEDLETV LKVEADRFQH LSYGEDVFKT ESRAVLGEYN KNSANPVSKL FEAMRDTAYE
KHTYKHTTMG FLKDIEDMPN QYAYSKVFFD RWYRPERTTI IVAGDVEPQK AVALVEKYWS
KWQRGSYKVD VPVEPAPKAP LYKHVTWATP TLPWVSVAFR APAFSEKQKD QAALSVLLSL
SFGRTSPLYK RLVQDEQKID QLFDSTPNRV DPTLAVIGAR VKKAEDTVYV RNAIMETVAK
LRSEPVGEKA LADAKSALKY GVIRSLDNTE QIAGMLASYV HFNRSYGTLN NYYRVLDSLT
PADLQAAARK YLTDEGLIVT TLSNGALPAD IGELPKLAAL EPKLNTAKID LLVQKSALPQ
IRYKLVFGAG SAHDPQGKEG LAALTAAMVA SAGSSERKID EISKALFPLA GSFSEQTDKE
MSTFTGTIHK DNWSQFQDIV MPQLLAPGFR EDDFRRLKDA QKNALLLDLK DNNEEELGKE
RLQTNVFAGS GYGHPVLGTV AGLDAITLDD VKDFYKKAYT QGALRVGLAG DVSDAMSASL
LKSLSRLPAG AGLAATPIPV GKMPNGLEVE IIEKNTRATA ISFGLPLTVT RSHADFPALW
LAKTWLGEHR ASSSLLYQRI REIRGMNYGD YAYIEAFPRG MFQFFPSANL GRKAQLFEIW
VRPVAPENAH LALRIALAEL DKLVAKGLTK EQFDITRGYL MKNVFVMTST QDQQLGYALD
SQWYGTPEFT KLMRDGLGKL TVDDVNAAIR KHLSSKNLSV VMIAKDAAGL KDKLLSDAFS
PIKYDGNKPK ELLDEDQVIG NMKLNIKPEA VKITPAANVF AN
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