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Database: UniProt
Entry: B3CD65_9BACE
LinkDB: B3CD65_9BACE
Original site: B3CD65_9BACE 
ID   B3CD65_9BACE            Unreviewed;       429 AA.
AC   B3CD65;
DT   22-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2008, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   SubName: Full=Peptidase M16 inactive domain protein {ECO:0000313|EMBL:EDV03126.1};
DE            EC=3.4.24.- {ECO:0000313|EMBL:EDV03126.1};
GN   ORFNames=BACINT_02240 {ECO:0000313|EMBL:EDV03126.1};
OS   Bacteroides intestinalis DSM 17393.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=471870 {ECO:0000313|EMBL:EDV03126.1, ECO:0000313|Proteomes:UP000004596};
RN   [1] {ECO:0000313|EMBL:EDV03126.1, ECO:0000313|Proteomes:UP000004596}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17393 {ECO:0000313|EMBL:EDV03126.1,
RC   ECO:0000313|Proteomes:UP000004596};
RA   Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA   Gordon J.;
RT   "Draft genome sequence of Bacteroides intestinalis (DSM 17393).";
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EDV03126.1, ECO:0000313|Proteomes:UP000004596}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17393 {ECO:0000313|EMBL:EDV03126.1,
RC   ECO:0000313|Proteomes:UP000004596};
RA   Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA   Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
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:EDV03126.1}.
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DR   EMBL; ABJL02000008; EDV03126.1; -; Genomic_DNA.
DR   RefSeq; WP_007662825.1; NZ_ABJL02000008.1.
DR   AlphaFoldDB; B3CD65; -.
DR   STRING; 471870.BACINT_02240; -.
DR   eggNOG; COG0612; Bacteria.
DR   OrthoDB; 9811314at2; -.
DR   Proteomes; UP000004596; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
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; PTHR11851:SF149; GH01077P; 1.
DR   PANTHER; PTHR11851; METALLOPROTEASE; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 1.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:EDV03126.1}.
FT   DOMAIN          41..134
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          183..358
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   429 AA;  48929 MW;  86F8D0F9222E65BC CRC64;
     MLDRTIQPRI CEPEQLAVPS PECRVMKNGI PLYILNAGDN EVVRIDLLIE GGRWQQSQRL
     QALFTNRMLR EGTRRYSAAA IAEKLDYYGA WLELSSSSEY AYITLYSLNK YLPETLDVFE
     SIVKEPLFPE KELGVIIDSN IQQFLVNCSK VDFLAHRTLI NAVYGDTHPC GQLVQKEDYH
     LINPSVLQSF YDRYYHSGNC SIYLAGKVSE DAIRRIETLF GSEPFGKDFR KPEKLSYVPV
     TSSEKRIFTE RADAMQSAVR MGMLSLDRRH PDYLKVRVLV TLFGGYFGSR LMSNIREDKG
     YTYGISAGIM PYPDSGLLVV NAETANEFVE PLIKEVYHEI DRLQNDLVPV EELAMVRNYM
     LGDMCRSYES AFSLADAWIF IHTSGLPDSY VRDAVEAVKT ITPVEIRELA SRYLCKETLK
     EIVSGKKMS
//
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