ID   A0A1P9X1E2_9BACT        Unreviewed;       958 AA.
AC   A0A1P9X1E2;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Peptidase M16 {ECO:0000313|EMBL:AQG81440.1};
GN   ORFNames=AWR27_20240 {ECO:0000313|EMBL:AQG81440.1};
OS   Spirosoma montaniterrae.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae; Spirosoma.
OX   NCBI_TaxID=1178516 {ECO:0000313|EMBL:AQG81440.1, ECO:0000313|Proteomes:UP000187941};
RN   [1] {ECO:0000313|EMBL:AQG81440.1, ECO:0000313|Proteomes:UP000187941}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DY10 {ECO:0000313|EMBL:AQG81440.1,
RC   ECO:0000313|Proteomes:UP000187941};
RA   Oliw E.H.;
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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DR   EMBL; CP014263; AQG81440.1; -; Genomic_DNA.
DR   RefSeq; WP_077132901.1; NZ_CP014263.1.
DR   AlphaFoldDB; A0A1P9X1E2; -.
DR   STRING; 1178516.AWR27_20240; -.
DR   KEGG; smon:AWR27_20240; -.
DR   OrthoDB; 9811314at2; -.
DR   Proteomes; UP000187941; Chromosome.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000187941};
KW   Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..958
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013111788"
FT   DOMAIN          69..187
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          226..406
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          706..880
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   REGION          23..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..43
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   958 AA;  107477 MW;  133888FA9B1D1641 CRC64;
     MVRFFSCLSL LLCTTLALSQ PAVQPKQGKS PARSASPASK AINLNAPIPT DPAVKVGKLP
     NGLTYYIRKN AEPKNRAELR LVIRAGSVLE TDEQQGLAHF MEHMAFNGTK NFPKNELVNF
     LQSAGVRFGA DLNAYTGFDE TVYQLPVPTD SARLFERAFQ ILEDWAHNAT IDPAEVEKER
     GVILEERRLG RGAGQRMRDK YFPILLNNSQ YANRLPIGTE QVLTTFKPET LRQFYKDWYR
     PDLMAVIAVG DFNATEVEAM IREKFGRIPV VKNAKPRRDY EIPAHKDTKV VIVTDPEQPN
     TVVQVIYKRP EIKERTLNDL RESIKRGLFN TMLGNRIQEL TQQANPPFLG GYSNYSDFLG
     NLDAFTSIAV AKEGNVERAI RAVLDENARV KQFGFTATEL ARAKQEFYTN VEQSYSERNK
     TRSANFVSEY VQNFTDKEPY TSIDFYFDFT KKVLPGVALD EVNTLVDQFI RNENRAVIVM
     APEKDKAKLP TVEQIIGYVD SAGKDLKPYE DKTLDAPLVA TPPTPSPVSN AREIKEIGVT
     EWTLRNGVRV VLKPTDFKND QILFSGVSFG GTSLYELKDF QSARFSSTLA AMGGTGAYSQ
     VQLGKFLAGK QVNVFPFVSE LNEGVNGSAA PKDLETALQL LYSYFTQPRK DPDVVAGFLS
     NQRNALQNQI NTPTPQRVFQ DTISITLGAN NPRRQPLKPA DLDKIDLDRA ISIYQERFAN
     AGDFTFFFVG NFNEENIKPL IEKYLGGLPA TPGKTEKFTD LGIRIPAGQL SKTVYRGLDP
     KATVQMVYSG DLTWSPETTT QLDALAEVLE IKLIEKLREE ESGVYGVGSN ASYSKYPVPR
     YTFRISFGCA PENVEKLIAK TQEIINTIKQ NGAAPGDIAK FKAETWRETE VQLKDNQFWL
     GYLQSQYFNQ DEPTEILREN EQLNKVTVDS TKAAANKYLA DNVARFVLLP EKKMEIGK
//