ID A0A172TC14_9DEIO Unreviewed; 363 AA.
AC A0A172TC14;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Endoglucanase {ECO:0000313|EMBL:ANE44474.1};
GN ORFNames=SU48_12685 {ECO:0000313|EMBL:ANE44474.1};
OS Deinococcus puniceus.
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=1182568 {ECO:0000313|EMBL:ANE44474.1, ECO:0000313|Proteomes:UP000077363};
RN [1] {ECO:0000313|EMBL:ANE44474.1, ECO:0000313|Proteomes:UP000077363}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY1 {ECO:0000313|EMBL:ANE44474.1,
RC ECO:0000313|Proteomes:UP000077363};
RA Kim M.K., Srinivasan S., Lee J.-J.;
RT "Deinococcus puniceus/DY1/ whole genome sequencing.";
RL Submitted (JAN-2015) 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; CP011387; ANE44474.1; -; Genomic_DNA.
DR RefSeq; WP_064015557.1; NZ_CP011387.1.
DR AlphaFoldDB; A0A172TC14; -.
DR STRING; 1182568.SU48_12685; -.
DR KEGG; dpu:SU48_12685; -.
DR PATRIC; fig|1182568.3.peg.2622; -.
DR OrthoDB; 9772053at2; -.
DR Proteomes; UP000077363; Chromosome.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-UniRule.
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:SF20; AMINOPEPTIDASE YSDC-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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR001123-2}; Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000077363}.
FT ACT_SITE 220
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-1"
FT BINDING 78
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 188
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 188
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 221
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 243
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 330
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
SQ SEQUENCE 363 AA; 38419 MW; 94986A4BE4122F98 CRC64;
MTQAPDSQSA DQQSGPIINL EFLFKLLSVA APSGSERRAA DVWKQEAAAF ARVSEDHFGN
VYAEVGPEGA PTIALMGHLD EIGLIVSHVS DEGFLSVLGV GGWDPQVLVG QRVRLLAPGG
DLLGVIGKKA IHVMEAEERT KASKLEDLWI DVGLDKDTVK ARIPIGTVAV IEQMPMMIGD
KIVSRALDNR VGAFIVLEAL RAVAGHDLKH RVVAVGTSQE EIGAFGAQVG GYLLNPVAGI
AVDVTHETKQ PGVSEKKYGV VPFGSGANLS VNPLSSPALN RALIDAAGAE HIPYTLSAAG
RYSGTDADTL TLVRAGVPTA VVSIPNRYMH SPSEMVDARD VKACTDIIAA WLRRVGTEEN
WGR
//
