ID   R5ANH9_9BACT            Unreviewed;       951 AA.
AC   R5ANH9;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Zinc protease {ECO:0000313|EMBL:CCX43444.1};
GN   ORFNames=BN456_01777 {ECO:0000313|EMBL:CCX43444.1};
OS   Prevotella sp. CAG:1031.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=1262917 {ECO:0000313|EMBL:CCX43444.1, ECO:0000313|Proteomes:UP000018183};
RN   [1] {ECO:0000313|EMBL:CCX43444.1, ECO:0000313|Proteomes:UP000018183}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:1031 {ECO:0000313|Proteomes:UP000018183};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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:CCX43444.1}.
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DR   EMBL; CAWK010000037; CCX43444.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5ANH9; -.
DR   STRING; 1262917.BN456_01777; -.
DR   Proteomes; UP000018183; 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, ECO:0000313|EMBL:CCX43444.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018183};
KW   Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..951
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004375088"
FT   DOMAIN          59..189
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          213..399
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          720..883
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   951 AA;  106092 MW;  D4E2A10E0700BBCD CRC64;
     MKKTLKFLAL AIVSLFVMPA MTALAQEMPQ MPQLPLDPQV RKGVLPNGLT YYIRHNEKPK
     GQADFYIAQK VGSILEEDHQ RGLAHFLEHM CFNGSENFPG NGMISWLETV GVKFGQNLNA
     YTAIDETVYN IANVPVARKS VQDSCLLILH DWADGLLLEP DEIDKERGVI HEEWRSRNKG
     SQRILEQILP ALYPGLKYGY RLPIGTMEVV DNFKPQALRD YYEAWYRPDL QGIVVVGDID
     VDYIEGKIKE IFSPIKMPKN AKERVYPAVP DYNKTVYGIG HDKEMNVNVI EMSWLSDPLP
     QELRNTQIYY MTQYMQSMIS MMLNNRFNEI TSKPDAPFAQ ADVNFGGFLV SSRVKDAFSL
     SVVAKDENLE PAFAAAYREV LRAARGGFNQ SELTRARDEY LSSIERAYNN RASIESGTFV
     NQYVRNFLDG DPAPGIETVY TMMNQMAPMI PLEAMNQALA ETVAGQSRAV LVMQPDNEKN
     VYATEQGIDA AIKKIDAENI EAFVDNAKTE PLIEKLPAPG KIVSESKNDN WGTTEYTLSN
     GVRVILKQTK FKEDEILMEA QALDGYAAMC PRNGEKPAEL ASIKLLPYSA DNFSLGSYTS
     NDLSKYLAGK QVGMGFSMGA YTREINGSTT PKDLKTLMEL VYSAFTGLSY DAEEFKAFQS
     QMSAMLANQT KTPDYKFSKM LMENLFKSPM RQALTAEDVT AATAEGTTKV MKALTNNAAD
     YTFVFVGNID EAAFRPLVEQ YIATLPANPA FSIKQVEEYN AADFITPGDA NVTMATKMEQ
     PTTYVAVFQT ANMPVNPKNQ RMAEIIGQVL TKRLLKTVRE EMGAVYSIGA NGGESSMGPM
     NVNLQSAFPM KPEMKEQVLK VVADEFNAIG NNLTEAELSD IRNFMVKEAK ENLEKNNGWL
     NGITGWLIHG NDAFTTRVAT LEGITVDDVK AYAKAVMAQK NYKVLILEPE K
//