ID G8TPY3_NIAKG Unreviewed; 375 AA.
AC G8TPY3;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Cellulase {ECO:0000313|EMBL:AEV99977.1};
DE EC=3.2.1.4 {ECO:0000313|EMBL:AEV99977.1};
GN OrderedLocusNames=Niako_3679 {ECO:0000313|EMBL:AEV99977.1};
OS Niastella koreensis (strain DSM 17620 / KACC 11465 / NBRC 106392 /
OS GR20-10).
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Niastella.
OX NCBI_TaxID=700598 {ECO:0000313|EMBL:AEV99977.1, ECO:0000313|Proteomes:UP000005438};
RN [1] {ECO:0000313|EMBL:AEV99977.1, ECO:0000313|Proteomes:UP000005438}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17620 / KACC 11465 / NBRC 106392 / GR20-10
RC {ECO:0000313|Proteomes:UP000005438};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Davenport K.,
RA Saunders E., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B.,
RA Pomrenke H., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Niastella koreensis GR20-10.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|PIRSR:PIRSR001123-2};
CC Note=Binds 2 divalent metal cations per subunit.
CC {ECO:0000256|PIRSR:PIRSR001123-2};
CC -!- SIMILARITY: Belongs to the peptidase M42 family.
CC {ECO:0000256|ARBA:ARBA00006272, ECO:0000256|PIRNR:PIRNR001123}.
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DR EMBL; CP003178; AEV99977.1; -; Genomic_DNA.
DR RefSeq; WP_014219891.1; NC_016609.1.
DR AlphaFoldDB; G8TPY3; -.
DR STRING; 700598.Niako_3679; -.
DR KEGG; nko:Niako_3679; -.
DR PATRIC; fig|700598.3.peg.3761; -.
DR eggNOG; COG1363; Bacteria.
DR HOGENOM; CLU_047249_1_0_10; -.
DR OrthoDB; 9772053at2; -.
DR Proteomes; UP000005438; Chromosome.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05656; M42_Frv; 1.
DR Gene3D; 2.40.30.40; Peptidase M42, domain 2; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR008007; Peptidase_M42.
DR InterPro; IPR023367; Peptidase_M42_dom2.
DR PANTHER; PTHR32481; AMINOPEPTIDASE; 1.
DR PANTHER; PTHR32481:SF0; AMINOPEPTIDASE YPDE-RELATED; 1.
DR Pfam; PF05343; Peptidase_M42; 1.
DR PIRSF; PIRSF001123; PepA_GA; 1.
DR SUPFAM; SSF101821; Aminopeptidase/glucanase lid domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438};
KW Glycosidase {ECO:0000313|EMBL:AEV99977.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AEV99977.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR001123-2}; Protease {ECO:0000256|ARBA:ARBA00022670}.
FT ACT_SITE 231
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-1"
FT BINDING 82
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 197
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 197
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 232
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 254
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 341
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
SQ SEQUENCE 375 AA; 41420 MW; 2FE2A8C30147B7BD CRC64;
MAKSKTTASA TSAGTYTMTD KAFKFLQSYI NNPSPVGFES SGQKLWLDYI TPLVDTTFVD
PYGTAVGVIN PKAEFKVVIE AHADEISWFV NYVTPEGLIY LKRNGGVDHV IAPGQRVFIH
GKKGPVKAVF GWPAIHTRLH NPDQKDPSPK VENLFLDSGA RNKKEVEDLG IHIGAVVTYQ
DGFDELAHDY YIGRAFDNRV GGFMIAEVAR LLKENKKTLP YGLYVVNAVQ EEIGLRGAEM
IARRIKPNVA IITDVTHDTY TPMINKIIEG DVACGKGPSL AYGPAVHNKL LSLVQDVAEK
NNIPVQNRTV SRSTGTDTDS FAYANDGCPS VLISIPLRYM HTTVEMLHKS DIEQTIRLMY
ETVLTLTPKT NLSYL
//
