ID E1WVM1_BACF6 Unreviewed; 954 AA.
AC E1WVM1;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Putative peptidase {ECO:0000313|EMBL:CBW23930.1};
GN OrderedLocusNames=BF638R_3469 {ECO:0000313|EMBL:CBW23930.1};
OS Bacteroides fragilis (strain 638R).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=862962 {ECO:0000313|EMBL:CBW23930.1, ECO:0000313|Proteomes:UP000008560};
RN [1] {ECO:0000313|EMBL:CBW23930.1, ECO:0000313|Proteomes:UP000008560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=638R {ECO:0000313|EMBL:CBW23930.1,
RC ECO:0000313|Proteomes:UP000008560};
RX PubMed=20829291; DOI=10.1099/mic.0.042978-0;
RA Patrick S., Blakely G.W., Houston S., Moore J., Abratt V.R., Bertalan M.,
RA Cerdeno-Tarraga A.M., Quail M.A., Corton N., Corton C., Bignell A.,
RA Barron A., Clark L., Bentley S.D., Parkhill J.;
RT "Twenty-eight divergent polysaccharide loci specifying within- and amongst-
RT strain capsule diversity in three strains of Bacteroides fragilis.";
RL Microbiology 156:3255-3269(2010).
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261}.
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DR EMBL; FQ312004; CBW23930.1; -; Genomic_DNA.
DR RefSeq; WP_005817299.1; NC_016776.1.
DR AlphaFoldDB; E1WVM1; -.
DR KEGG; bfg:BF638R_3469; -.
DR PATRIC; fig|862962.3.peg.3594; -.
DR HOGENOM; CLU_008156_0_0_10; -.
DR Proteomes; UP000008560; Chromosome.
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; 4.
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; 4.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670}; Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..954
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003154414"
FT DOMAIN 51..179
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 206..380
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 696..875
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 954 AA; 109462 MW; 808F5EE7DD3A58EC CRC64;
MKRNNKNRYL YIAAIFIAAM LPYTACPQST PILLPPGTVE GRLPNGLHYL ILHNASPASR
VEFRLIMRVG SVQETEQEKG CAHFLEHITF GGTRHFPKRS LVEYLESLGM KYGQDINAFT
GFDRTIYMFA VPTDFAKDEA LDRSLLILHD WLDGVTIDPE KVENEKGIIL EELRGFDPED
DFYPLKIGQG IFSHRMPLGT TDDIRKVTPQ VLKNYYHKWY VPSLATLVIV GDISPLEIES
KIKERFKSLP GRPVNDFRNY PLEYTRGIHL ASIRDSLQPR TKVELMIPHP CTVERTMEDA
IAKEKGRLLV SAISSRFRAR KLKTDVTDQW YLSDKNHFVL TVEGENRKEI LTSISTTVSL
LNDLIRNGWQ EDELQDIKNN FCRRMKLSTD APSRPSSMWC DDFADYVISG DRYLTDPSQQ
QQLKEAMSRV SGQSLQTLLK EWMSYREETL LVACSTHPGL GAPLSETEIA SAWAQGEQVE
CTPFLYFRPE KQEEIDIETP PCLAARFPFD PASVLRQTEY PQNRIREVEL KNGIRLVLKP
TLEADSTLLI TSFAPFGTSS LSDEEYPLLE GFAGYIDMGD IAKVDGQVLS DYLFRKEISL
SMAVENHWHG FIGMSPTANA PELFNLIYEK IFDPELKYDE FEEIRQDLLE NQDKETILEK
MLQRSPDRLL SARINELTGT GFARSSQKLS SEQIKNLNLD SIAAFYKKLY TNPQGTTYVI
CGNFNADTLM QQFVSVFGRI PVSSHLSRFS YPHFNFPVRK HIEGFPNDND TQTLFDYLLP
GHYQPGLKNT LTLKLMRDLI RNRLISVLRE QKSLVYSPYI SLMYEGIPQG IFYFDINASA
DNDNMPQIEQ LLKEILHQLK QQEVDNEELN TLKRSFLIAK REALNEESPS AWRTALVGLL
KNGETISDFD HYEQCLDSIT PAMLREAFRR YLDTENYILL YLSKNKLKND TSNH
//