ID C3QEY2_9BACE Unreviewed; 412 AA.
AC C3QEY2;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Peptidase M16 inactive domain protein {ECO:0000313|EMBL:EEO50317.1};
DE EC=3.4.24.- {ECO:0000313|EMBL:EEO50317.1};
GN ORFNames=BSAG_02028 {ECO:0000313|EMBL:EEO50317.1};
OS Bacteroides sp. D1.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=556258 {ECO:0000313|EMBL:EEO50317.1, ECO:0000313|Proteomes:UP000003361};
RN [1] {ECO:0000313|EMBL:EEO50317.1, ECO:0000313|Proteomes:UP000003361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D1 {ECO:0000313|EMBL:EEO50317.1,
RC ECO:0000313|Proteomes:UP000003361};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Strauss J., Sibley C.,
RA White A., Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M.,
RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A.,
RA MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C., Neiman D.,
RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Bacteroides sp. D1.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
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:EEO50317.1}.
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DR EMBL; ACAB02000106; EEO50317.1; -; Genomic_DNA.
DR RefSeq; WP_004313042.1; NZ_JH114349.1.
DR AlphaFoldDB; C3QEY2; -.
DR HOGENOM; CLU_009902_1_1_10; -.
DR Proteomes; UP000003361; 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:SF17; PROTEIN YHJJ; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EEO50317.1};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 15..128
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 167..343
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 412 AA; 47452 MW; 3725B95C45B6200D CRC64;
MKINRHILEN GLRLVHSQDE STQMVALNIL YNVGARDEDP EHTGFAHLFE HLMFGGSVNI
PDYDMPLQLA GGENNAWTNN DITNYYLTVP RQNVETGFWL ESDRMLSLDF SERSLEVQRG
VVMEEFKQRC LNQPYGDVGH LLRPLAYQTH PYQWPTIGKE LSHIANATLE EVKAFFFRFY
APNNAILAVT GNISFEEAVA LTEKWFASIP RREVPLRNLP QEQEQTEERW LTVERNVPLD
ALFMAYHMPD HRHPDYYAFD ILSDVLSNGR SSRLNQRLVQ QKQLFSSIDA YISGSVDAGL
FHISGKPSAG VTLEQAEAAV REELELLQQE LVDEQELEKV KNKFESTQIF GNINYLNVAT
NLAWFELLGR AEDMEKEVER YRSVTAEQLR TVAQSAFRKE NGVVLYYKKQ QN
//
