ID A0A2A8I0E0_9SPHN Unreviewed; 977 AA.
AC A0A2A8I0E0;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=Peptidase M16 {ECO:0000313|EMBL:PEQ14768.1};
GN ORFNames=B2G71_03630 {ECO:0000313|EMBL:PEQ14768.1};
OS Novosphingobium sp. PC22D.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1962403 {ECO:0000313|EMBL:PEQ14768.1, ECO:0000313|Proteomes:UP000220675};
RN [1] {ECO:0000313|EMBL:PEQ14768.1, ECO:0000313|Proteomes:UP000220675}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PC22D {ECO:0000313|EMBL:PEQ14768.1,
RC ECO:0000313|Proteomes:UP000220675};
RA Peterson S.W.;
RL Submitted (FEB-2017) 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:PEQ14768.1}.
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DR EMBL; MWMO01000001; PEQ14768.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A8I0E0; -.
DR Proteomes; UP000220675; 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:SF18; INSULIN-DEGRADING ENZYME-RELATED; 1.
DR PANTHER; PTHR43690; NARDILYSIN; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 2.
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:UP000220675};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 63..199
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 213..412
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 713..885
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 977 AA; 105985 MW; 1DF2E3A34FBAB206 CRC64;
MDPVVESSPV PSAVPVATGP DDSAEVPWLY RNSDVPPDRE WQFGELDNGL RYAVRKNGVP
PGQVSIRIRV DAGSLYEKDA ERGYAHFLEH LVFRQSKYIP EGAAIATFQR LGASFGSDTN
AETTTTQTVF KLDLPDATPQ SVDEVMKLVS GMITAPKLSA ANLKSDLPIV LSEMRERGGA
AKRVQDAMQS TFYAGQPLAV RSPIGTIETL DAATPESVRA FYNRWYRPQN VVIIVAGDAE
PAFLEAEVAK WFGEWSPPGE PVPAPSFGDP VAPDEVAAAT TDDGAANAFA QTPVGETKVL
VEPDLPASVT YAILRPWRQV DDTIVYNQGL MTDALAQAII NRRLESKARM GGSFLTAQVN
QDDVARSADA TFVQVTPLTD DWQSALEHVR AVIADALANP PTQAEIDREV AELDVAFQVP
VEQRRLLPGS KLADDLVNAL DIRETVAAPD AVLRIFRESI PLFTPEAILQ HTRGLFEGTV
TRAVFVTPQQ GVASDAALRT ALIEPVAPDD SVRLASSEPV SFDNLPAVGA PGQVLAATPT
GLLDIQQIEF ANGVKALLWP VQEEPGRVTV KVRFGGGYRS IDPKDAPYVT LGEMALVSSG
VATLGQEDLD RISTGRKMGF KFDVEDAAFQ FSAETRPADL ADQLYLFAAK LALPRWDENP
FLRAKAAAKI QYEAYSTSPQ GVLNRDLQYY QRGRDPRFET PTPAEIEKTT PEGFKRVWEK
ALSSGPVEVQ IFGDFDLPST VAALQKTFGA LAPRQPGVTP TQLAEISQPK PSDSPVVLRH
RGDPDQAAAI ISWPTGGGSM GITESRQLEI LTQLFTNRLL DAVREKLGVS YAPYVYSTWP
VDLQAGGAIT AMAQVDPKSV KVFFQTADEI AQDLITNPPT ADELALVTEP LRQQVTRAAS
SSAFFMGQIE GATYDPARIA SVRSVLIDYT ETTPEKMQAL AARYLGKDNS WRLEVLPEET
REAAASDSQK ASKVSLR
//
