ID A0A1N7KS45_9BACT Unreviewed; 932 AA.
AC A0A1N7KS45;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Zinc protease {ECO:0000313|EMBL:SIS64377.1};
GN ORFNames=SAMN05421761_102301 {ECO:0000313|EMBL:SIS64377.1};
OS Belliella pelovolcani.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Belliella.
OX NCBI_TaxID=529505 {ECO:0000313|EMBL:SIS64377.1, ECO:0000313|Proteomes:UP000186026};
RN [1] {ECO:0000313|EMBL:SIS64377.1, ECO:0000313|Proteomes:UP000186026}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 46698 {ECO:0000313|EMBL:SIS64377.1,
RC ECO:0000313|Proteomes:UP000186026};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) 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; FTOP01000002; SIS64377.1; -; Genomic_DNA.
DR RefSeq; WP_076498644.1; NZ_FTOP01000002.1.
DR AlphaFoldDB; A0A1N7KS45; -.
DR STRING; 529505.SAMN05421761_102301; -.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000186026; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0008237; F:metallopeptidase 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: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.
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:SIS64377.1};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..932
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012523625"
FT DOMAIN 49..170
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 206..387
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 694..862
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 932 AA; 104649 MW; 5D18484D18356CB0 CRC64;
MKYTRIIILM AFWLGTTLAL TAQSQEKVPL DSRVRTGKLA NGLTYYVQQN PKPEKKVELR
LAVNAGSILE DDDQAGLAHF TEHMAFNGTK NFEKNELVSY LQSIGVSFGG DLNAYTSFDE
TVYILPIPSD DEEKLKSGFL VLADWAGGVL MNEEDIDGER GIIVEEWRTG QGYSQRVRDQ
FLPVLLHDSK YADRLPIGKM EVVENFEYET IRRFYRDWYR PDLMAVVAVG DEDPDKLEAL
IKEYFSGLEN PANAKPREHF PVPEHKETFV TVVTDPESPG IQIQLYYKHK ALPTSTKEDY
KNILKRRLYS GMLNQRLDEI RQKPDAPFIY AGTGYGNFVR DMDYFSASGA VAPGKTAVAI
KALIEENERV AQFGFTESEL ERVKRSLLNS AERAAKEMDK AESGSLVGKY VSHYLEGSFA
EDQQWRYEFY QDVMPQITVE EINALAKELV RDDNRVVVIS GPEKDKETLP TEQEVLALFT
AVDNMQLTPY EEKLLAEDLI TNLPAAGKVS GMNKISGVDI QEITLSNGAK VFVKQTDFKN
DEILISATGK GGTSLYSDED HLTASNAGVM VNVMGVGDFS PTDLRKVLSG KTVSLTPNIG
TYSQNISGIT SPKDLETAMQ LMHLYFTKPR KDADLYEVYK TNQKTQLAGA QANPDYQFSR
AVNKIVAGGN PRAMGILDPE DYDKIDIDRG LEIFADRFSN AANFEFFFTG NIDMDTFIPL
LEQYIGSLPG DANAKDSFVD LGIRTPRGKK ERIEVGTDEK SQVIMFFSGE TDYDRKKSTD
ISYLGEILTI KLIENLREEI GGVYGVGASG NMSIQPVGNF SFSISFPCSP DMVDKLTEAA
WAEVKKIQEN GPTEDDLNKV KEKRRIAYEE NLKRNNYWNG QMSAVRTYDL PWEVILEGRA
SIDSVTPERI QNAAKAYLVK ENLLEIQRFP AK
//
