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Database: UniProt
Entry: W2CJM2_9BACT
LinkDB: W2CJM2_9BACT
Original site: W2CJM2_9BACT 
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
//
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