ID   A0A1M7LP30_9FLAO        Unreviewed;       944 AA.
AC   A0A1M7LP30;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Zinc protease {ECO:0000313|EMBL:SHM79991.1};
GN   ORFNames=SAMN05720268_0610 {ECO:0000313|EMBL:SHM79991.1};
OS   Polaribacter sp. KT 15.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae.
OX   NCBI_TaxID=1896175 {ECO:0000313|EMBL:SHM79991.1, ECO:0000313|Proteomes:UP000190644};
RN   [1] {ECO:0000313|EMBL:SHM79991.1, ECO:0000313|Proteomes:UP000190644}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KT 15 {ECO:0000313|EMBL:SHM79991.1,
RC   ECO:0000313|Proteomes:UP000190644};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261}.
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DR   EMBL; LT670850; SHM79991.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M7LP30; -.
DR   Proteomes; UP000190644; Chromosome i.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0008233; F:peptidase 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; NARDILYSIN; 1.
DR   PANTHER; PTHR43690:SF21; PROCESSING PROTEASE; 1.
DR   Pfam; PF00675; Peptidase_M16; 2.
DR   Pfam; PF05193; Peptidase_M16_C; 2.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:SHM79991.1};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          48..134
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          201..377
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          526..650
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          672..847
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   944 AA;  105063 MW;  E2C64684BC6347FD CRC64;
     MKKICIAFIA IASFIACNNS SKEKTKELRV NYKKIELDNG LDVIFHVDKS DPVVAVELMV
     HVGSAREKEG RTGFAHLFEH LLFLESENLG KGGLDKMSAR IGGSGANGST SRDRTNYLQT
     VPKDALEKMI WAEADKLGYF INTVTEPVLA KEKQVVKNEK RQSVDNRPYG HNQYVIGKNL
     YPKNHPYNWQ VIGSLEDLQN ATLQDVKDFY KKWYVPNNAT LVLSGDIDIE EATKWVHKYF
     DEIPKGEEIP ALEKKPGEVK ETKFLYYEDN FARVPQLTMV WPSVEMYHED SYALEVLTQY
     LSDGKSAPLN TVLVDDLKLT SNTVMYNYAS ELAGETQLIV RAFNGKNLDE VKAGIEKGFA
     KFESEGISDK DLQRIKAGQE TQFYLGLSSV LGKGSNLASN NTYLGNPGFA TEDIKKTLAV
     TKDDVMRVYN TYIKDKNYIA TSFVPKNSAE LALKGSTLAN VVEEKIVNGA EETFNPKIAA
     TYKKTPSSFD RSIEPEYGKA PSLAVPKVYE ADLENGLKIY GIENNEVPLV RFNLTIDGGQ
     LLESLDKLGV ANLTADLLNK GTKNKSVQQL EEAIQELGAS IYIYATKENI TLSGTTLAKN
     YTKTLALAQE MLLQPRFDET EFALLKKATI SNLRQQEASP NSVARNAYNT LIYGEDNIRS
     KNTLGTISSV ENISIEDLKE YYNNYISPSV AKMLVVGDIT EETVVNSLAS LNTNWHSKAV
     TIPEYKTPNA PNKPVVYFYD IPNAKQSVLQ FGAPALAATD KDYYAASVMN YILGGGGFAS
     RLTQELREGK GYTYGIRSGF SGTKAKGTFT ISSGVRSNVT LESAQAVKKI LEEYPTTFSD
     KDLETTKGFL IKSNARAFET AGAKLRMLSN IANYGMKADY ISDREETVNN MTKERISELA
     NTYVNPNKMI WLIVGDAETQ LNRMKELGYG EPVLLNERQK KIKN
//