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Database: UniProt
Entry: E5C5G3_9BACE
LinkDB: E5C5G3_9BACE
Original site: E5C5G3_9BACE 
ID   E5C5G3_9BACE            Unreviewed;       945 AA.
AC   E5C5G3;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=Peptidase M16 inactive domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=BSGG_1309 {ECO:0000313|EMBL:EFS30609.1};
OS   Bacteroides sp. D2.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=556259 {ECO:0000313|EMBL:EFS30609.1, ECO:0000313|Proteomes:UP000003135};
RN   [1] {ECO:0000313|EMBL:EFS30609.1, ECO:0000313|Proteomes:UP000003135}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D2 {ECO:0000313|EMBL:EFS30609.1,
RC   ECO:0000313|Proteomes:UP000003135};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Allen-Vercoe E., Strauss J.,
RA   Sibley C., White A., 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., Goldberg J.,
RA   Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A.,
RA   MacDonald P.J.P., Montmayeur A., Murphy C., Neiman D., Pearson M.,
RA   Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C.,
RA   Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Bacteroides sp. D2.";
RL   Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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:EFS30609.1}.
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DR   EMBL; ACGA02000062; EFS30609.1; -; Genomic_DNA.
DR   RefSeq; WP_009000531.1; NZ_JH636026.1.
DR   AlphaFoldDB; E5C5G3; -.
DR   HOGENOM; CLU_008156_0_0_10; -.
DR   OrthoDB; 9811314at2; -.
DR   Proteomes; UP000003135; Unassembled WGS sequence.
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: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; IPR001431; Pept_M16_Zn_BS.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   PANTHER; PTHR43690; NARDILYSIN; 1.
DR   PANTHER; PTHR43690:SF34; ZINC PROTEASE PQQL-LIKE; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 2.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
DR   PROSITE; PS00143; INSULINASE; 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          56..181
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          213..398
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          696..874
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   945 AA;  106557 MW;  3BAA6A5F8193A5D6 CRC64;
     MKHLLRGLFI AVLFICCNFQ LVLAQPMQEL PVDKNVRIGK LDNGLTYYIR HNALPEKRVE
     FYIAQKVGSI LEEPQQRGLA HFLEHMAFNG TKHFPGDETG LGIVPWCETK GIKFGTNLNA
     YTSVDQTVYN ISNVPTENIN VVDSCLLILH DWSSAINLAD KEIDKERGVI REEWRSRNSG
     MLRIMTDAQS TLYPDSKYSD CMPIGSIDVI NNFPYQDIRD YYAKWYRPDL QGIVIVGDIN
     VDEIEAKLKK VFADVKAPVN PAERIYYPVA DNQEPLIYIG TDKEVKNPYV NIFFKQDATP
     DSLKNTIAYY ATQYMVSMAM NMLNNRLNEL RQTANPPFTS ASAEYGNYFL AKTKEALALD
     ASSKIDGIDL AMKTVLEEAE RARRFGFTAS EYERARANYL QAVESAYNER EKTKSGSYVN
     EYINNFLEKE PIPGIEVEYT LVNKLAPNIP VEAVNQVMQQ LITDNNQVVL LAGPEKEGAK
     YPTKEEIAAL LKQMKSFDLK PYEDKVSNEP LISEDIKGGK IVSEKAGEIY GTTKLVLSNG
     VTVYVKPTDF KADQIVMKGV SFGGTSVFPN EEIINISQLN GVALVGGIGN FSKVDLGKAL
     AGKRANVGAG IGNTTETVSG SCAPKDFETM MQLTYLTFTS PRKDNEAFES YKNRLKAELQ
     NADANPMTAF SDTITSVLYG HHPRAIRMKE NMVDQIDYDR ILEMYKDRYK DASDFTFFLV
     GNVDLATMKP LIAKYLGGLP SINRKETFKD NKMDIRKGEI KNVFAKAQET PMATIMFLYS
     GTCKYDLRNN VLLSFLDQAL DLVYTAEIRE KEGGTYGVSC NGSLGKYPKE ELVLQIVFQT
     DPAKKDKLSA VVVEQLHKMA KEGPSAEHMQ KIKEYMLKKY KDAQKENGYW LNNMDEYLYT
     GVDNTKDYEK LVNSITAKEV QDFLAKLLKQ NNEIQVIMTV PEENK
//
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