ID W2CJM2_9BACT Unreviewed; 940 AA.
AC W2CJM2;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Peptidase M16 {ECO:0000313|EMBL:ETK06681.1};
GN ORFNames=T230_11015 {ECO:0000313|EMBL:ETK06681.1};
OS Tannerella sp. oral taxon BU063 isolate Cell 1/3.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae;
OC Tannerella.
OX NCBI_TaxID=1411022 {ECO:0000313|EMBL:ETK06681.1, ECO:0000313|Proteomes:UP000034982};
RN [1] {ECO:0000313|EMBL:ETK06681.1, ECO:0000313|Proteomes:UP000034982}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cell 1/3 {ECO:0000313|EMBL:ETK06681.1};
RA Beall C.J., Campbell A.G., Griffen A.L., Podar M., Leys E.J.;
RT "Single cell genomics of uncultured Tannerella BU063 (oral taxon 286).";
RL Submitted (NOV-2013) 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:ETK06681.1}.
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DR EMBL; AYYE01001145; ETK06681.1; -; Genomic_DNA.
DR AlphaFoldDB; W2CJM2; -.
DR PATRIC; fig|1411022.3.peg.1305; -.
DR Proteomes; UP000034982; Unassembled WGS sequence.
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: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; 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}; Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..940
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004813680"
FT DOMAIN 52..173
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 212..395
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 694..873
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 940 AA; 106504 MW; 5DB72BD9C42EA227 CRC64;
MKMQFKHMLL GLAVLCFTAT KAQQMPTVPV DKQVRIGHLE NGLTYYIRAN KLPENRANFY
IVQRVGSILE EENQRGLAHF LEHMAFHGSK HFPEDQTGSG IISYLETIGV KFGRNLNAYT
GMDETVYNID DVPTDRRGAV DSCLLILHDW SNSLFLRDKD IDKERKVIHE EWRTRRSASS
RLIDSIAPVI FAGSKYAERM PIGLMSVVDH FKPKELRDYY HKWYRPDLQA IIIVGDFDAE
QVEKDVKRIF GSIPKPVNPA ERVYEKIPDN EAPAVAVVTD KEQPTGYFMV SYKRDALPKE
QKTVIDYLVY DFATDMIDRM LTDRFQEMMQ NQNPPFAYAR ASNGSFFGVA TTDAMQLAGV
IKPGQADTTL LTLLREAKRV HDFGFTPSEY ERAKADWLSD IEKLYNERDK QKNNYYVQQY
VEHFLLGEPI PSLEEYYQIM SQVVPSVPLE AINQLAAEFI SDNNRAVVLM GNEEQRPTYP
TPDRIRKIIA QVDGEHLTAY ADKSINEPLI ATLPTKGKIT KEKKLTDRGV TVWTLSNGAR
VAVKKTDFKK DEILLSGFAY GGKSLMDPRY AAEQKLMDDA SSVGGLGKFS ATDLKKVLAG
KNADVSASIS EYNQSVGGRS SVKDLETLMQ LLYLQFTAVR KDETAYAALA TRLKGILPML
ANNPDYAFND SVMMAIYKGN PLMRIPTVKE IEAVNYDKLL DLFRARLANA ADYTFTFVGN
VDEAALRPLV EQYVASLPSN GKPSKAFNKD YLPIRKGQFE NHFSRQLETE KATTSIYYSG
DMAYTADNLI RLSALEQLFN MEFVDKIREK LGGTYGVSVS SNAQKLPTEG FSLQFQYDCA
PDRRVELTNA MNQVSERMRK TGPDAVMLSK VKEYMLKQHA DNLKENGYTL RATWRYLVFG
IDINADYEKK VNALTIESVR DFANQLLSQG NRIEVSMSSK
//