ID A0A1N6DGK6_9BACT Unreviewed; 947 AA.
AC A0A1N6DGK6;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Zinc protease {ECO:0000313|EMBL:SIN69794.1};
GN ORFNames=SAMN04488055_0716 {ECO:0000313|EMBL:SIN69794.1};
OS Chitinophaga niabensis.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Chitinophaga.
OX NCBI_TaxID=536979 {ECO:0000313|EMBL:SIN69794.1, ECO:0000313|Proteomes:UP000185003};
RN [1] {ECO:0000313|EMBL:SIN69794.1, ECO:0000313|Proteomes:UP000185003}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24787 {ECO:0000313|EMBL:SIN69794.1,
RC ECO:0000313|Proteomes:UP000185003};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FSRA01000001; SIN69794.1; -; Genomic_DNA.
DR RefSeq; WP_074237908.1; NZ_FSRA01000001.1.
DR AlphaFoldDB; A0A1N6DGK6; -.
DR STRING; 536979.SAMN04488055_0716; -.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000185003; 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:SIN69794.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000185003};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..947
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012116533"
FT DOMAIN 61..191
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 219..405
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 700..877
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 947 AA; 105032 MW; 5537F871099248E0 CRC64;
MKRRVLLLAL ATTSVFSLWE QPALAQKKAA PVVKKTGDVI PDDPDVKIGK LANGLTYYIR
KNTEPKNRAV LYMALKAGSL METDAQQGLA HFTEHMAFNG TKDFPKNELI NYLQKAGVKF
GADLNAFTAF DQTVYQLPIP TDSAALFKNG FKILANWAGY VTMEDSEIDN ERGVIVEEDR
QRGKNAQSRI QKELLPVLLK GSRYAERIPI GKLDIIQNFK HNEIKQFYKD WYRPNLQGVI
AVGDFDVAQV EAMIKENFSP LKNPANPKPV VKYNMPDNKE PLVKIVTDKE FPYNVAVVMI
RHHGSVGKTT AEVKAGIING MINNMMGNRI NELKQKGTAP FVEGQFSYGA YQGGLIPGLE
ATSVVAVAKS GDELTKALGG VMTEAERMSQ FGFTASELDI VKKNLEAGNE KSFREKDKTP
SNSYVQAYLS NFLQGSPIPA ATYRYEMVKR LLGEITLEDV NKKAKEMIKP ENMMIVIQAP
EKEKEKLPTE AQLLATVQGA GKGVTAYVEN KVDKPLLEKK PVAGKVVSEE KIEGIDVTKL
TLSNGVKVYL KPTTFKNDQI LFSSFGEGGT SLADDKEYLA MNYASNIAGD GIGEFDNTQL
RKLLAGSTAS AGAYIGDLHQ GFSGSASPKD LETALQLVYA RATNPRKDPV VFKKNLDDYK
VMLQNADDNP ESVYGDTITA VLSSNSIRER KPTPAELDAI SLDKSFDFYK ARFADASGQT
FVFVGNFEVD KIKPLLETYL GGLPAANHTE KYIDRGIKPL SGKVERTVKK GIEDKAQVKL
YFHNDYQYSP ENNLQLSALS DILEFKVLER LREKESGVYS PNVGVSYEKL PSPYYNLQIS
FSCATANVDK LIAAALDEIE KIKKEGATAV DVEKFKAESR RAMEVSLREN NFWLSYLTSK
FRNNEDPLSV LKQNERLEQV TPESVKAAAQ KYLGGADYFR AVLVPEK
//