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Database: UniProt
Entry: A0A0A6Y357_9FLAO
LinkDB: A0A0A6Y357_9FLAO
Original site: A0A0A6Y357_9FLAO 
ID   A0A0A6Y357_9FLAO        Unreviewed;       981 AA.
AC   A0A0A6Y357;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=Peptidase M16 inactive domain protein {ECO:0000313|EMBL:KHE70029.1};
GN   ORFNames=HMPREF9074_08002 {ECO:0000313|EMBL:KHE70029.1};
OS   Capnocytophaga sp. oral taxon 329 str. F0087.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Capnocytophaga.
OX   NCBI_TaxID=706436 {ECO:0000313|EMBL:KHE70029.1, ECO:0000313|Proteomes:UP000030579};
RN   [1] {ECO:0000313|EMBL:KHE70029.1, ECO:0000313|Proteomes:UP000030579}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0087 {ECO:0000313|EMBL:KHE70029.1,
RC   ECO:0000313|Proteomes:UP000030579};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA   Chinwalla A., Mardis E.R., Wilson R.K.;
RL   Submitted (OCT-2014) 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:KHE70029.1}.
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DR   EMBL; AFHP02000075; KHE70029.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A6Y357; -.
DR   STRING; 706436.HMPREF9074_08002; -.
DR   eggNOG; COG0612; Bacteria.
DR   HOGENOM; CLU_306466_0_0_10; -.
DR   Proteomes; UP000030579; 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:InterPro.
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:SF17; PROTEIN YHJJ; 1.
DR   Pfam; PF00675; Peptidase_M16; 3.
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..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..981
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002035167"
FT   DOMAIN          64..113
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          156..253
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          267..439
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          601..680
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          731..878
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   981 AA;  111415 MW;  9C4806F85A937B2C CRC64;
     MLIHQMMLKR NLFLWLFALA VSFGAQAQNY EWKEAQSGGY KYKYVTHDPT NSRFYTLKNG
     LTVILSPTNK EPRIQCYVAV KAGSKTDPST NTGLAHYLEH LLFKGTDKYG SLDWEKEKVQ
     LDKIDALYEE YNHTKDAEKR KAIYKKIDSV SGVASKYAIA NEYDKMMTAM GAQGTNAFTS
     FEKTVYTDDV PANALNKYIT VQAERFRNPV LRIFHTELEA VYEEKNRSLD SDNSEVFETL
     FASLFKKHNY GLQTTIGTVE HLKNPSLKEI RKYFHTYYVP NNMAVVLSGD FNPDEAIAEI
     DKAFSYMTPK AVPQYTFEKE EPISAPIIKK VVGPDAENVS IAFRLPGNQD KDALLADLVG
     EILTNGKAGL IDLNLVKKQK LLGASAGAYT LIDYGMLYLS GRPLQGQSLE QVKDLILGEI
     ENLKKGNFDD DLIPSIINNM KKYVIQGTES YANRANMLME AFTDNLDWKD RVAYVNSLSK
     ITKADIVAFA NKYLGNNYVV IYKEKGQRTN VEKIEKPAIT PVETNADKQS AFVKMVNEMP
     STPVKPVFLD YSKDLQKGKL GKAEVLYVQN KDNELYRLSF RYKIGTLNDL KLAIAANYSQ
     FLGTDKKSAE QLSKELYKIA SSFNISASGE YTTVNIEGLQ ENFEAAVKLY EDFIANIKVD
     EEALKALKTR VAKTRIDSKA NRGAIMQALT NYALYGAKNP YNYTFSDAEI EAITGKELVE
     KLKKLNNVEQ TVIYYGPLSL NQLTAKLKPL HKVPAKFAQV APKKEFKQVE QTKNQVFFAD
     YEMVQAETRW IRNTVPYNPA ESTVIKAFNN YFGGGMGSLV FQTIRESKAL AYSTYGYYAT
     PSKKTDKYYT LAYVGSQADK FKEAVEAMNE LLNTMPELPA NLELAKQQIK QEIETERITQ
     DGIIYYYLHD QRMGLKEDIR KQIYQNIDNI TMKDIKAFHD KYLSNKPYTY VILASEKKLS
     EDELKKIGDF KKLSLKELFG Y
//
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