ID A0A1J5MK21_9GAMM Unreviewed; 505 AA.
AC A0A1J5MK21;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Peptidase M16 {ECO:0000313|EMBL:OIQ46909.1};
DE Flags: Fragment;
GN ORFNames=BM565_09370 {ECO:0000313|EMBL:OIQ46909.1};
OS Gammaproteobacteria bacterium MedPE.
OC Bacteria; Pseudomonadota; Gammaproteobacteria.
OX NCBI_TaxID=1860093 {ECO:0000313|EMBL:OIQ46909.1, ECO:0000313|Proteomes:UP000182920};
RN [1] {ECO:0000313|EMBL:OIQ46909.1, ECO:0000313|Proteomes:UP000182920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MedPE {ECO:0000313|EMBL:OIQ46909.1};
RX PubMed=27446036; DOI=10.3389/fmicb.2016.00996;
RA Lopez-Perez M., Kimes N.E., Haro-Moreno J.M., Rodriguez-Valera F.;
RT "Not All Particles Are Equal: The Selective Enrichment of Particle-
RT Associated Bacteria from the Mediterranean Sea.";
RL Front. Microbiol. 7:996-996(2016).
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:OIQ46909.1}.
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DR EMBL; MPDF01000061; OIQ46909.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J5MK21; -.
DR STRING; 1860093.BM565_09370; -.
DR Proteomes; UP000182920; 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; 2.
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:SF35; NON-CATALYTIC MEMBER OF PEPTIDASE SUBFAMILY M16B-RELATED; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 58..174
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 215..393
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT REGION 474..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..492
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 505
FT /evidence="ECO:0000313|EMBL:OIQ46909.1"
SQ SEQUENCE 505 AA; 56150 MW; BA7F89163B073305 CRC64;
MKKWMISAVA LAITACSQSP NTDDVNIAGV KFVEKVSAQP GKTTIPYKKF QLANGLTVIL
HEDKSDPLVH VDVTYHVGSA REDLGMSGFA HFFEHMMFQG SENVGDDEHF KIVTEAGGTM
NGTTNSDRTN YYQTVPVNQL EKMLWLESDR MGYLLDAVTQ EKFEVQRETV KNERGQRVDN
APYGRLGETK ARALYPKGHP YSWPVIGYMA DLNRVNVNDL KAFFLKWYGP NNATLTIGGD
INAAETMALV NKYFGEITPS MTPTPLDKTL INLPRDRYVS FEDNVNLPLV YLSFPTAHAR
HEDEAPLDLL AQILGGGKTS LLYKNLVKSR IAVQTSASHP CQELACTFDL YALPHPASGK
SLGDIEKIIR KTITEFETRG VMDDDLAKAK AQMEASFIFG LQSVQGKVAQ LAAYETFTGD
ANYIEKDIAR YNNVSKVDVM RVFNRYIKNK PSVIVSVVPN GKGDMVAKAD NFEPQVTKLS
GQSTTSEADL KMRDNPNTFD RSKKP
//
