ID A0A2N0VGY8_9BACT Unreviewed; 345 AA.
AC A0A2N0VGY8;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE SubName: Full=Endoglucanase {ECO:0000313|EMBL:PKD43459.1};
GN ORFNames=CWD77_07765 {ECO:0000313|EMBL:PKD43459.1};
OS Rhodohalobacter barkolensis.
OC Bacteria; Balneolota; Balneolia; Balneolales; Balneolaceae;
OC Rhodohalobacter.
OX NCBI_TaxID=2053187 {ECO:0000313|EMBL:PKD43459.1, ECO:0000313|Proteomes:UP000233398};
RN [1] {ECO:0000313|EMBL:PKD43459.1, ECO:0000313|Proteomes:UP000233398}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=15182 {ECO:0000313|EMBL:PKD43459.1,
RC ECO:0000313|Proteomes:UP000233398};
RA Han S.;
RT "Rhodohalobacter 15182 sp. nov., isolated from a salt lake.";
RL Submitted (NOV-2017) 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}.
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:PKD43459.1}.
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DR EMBL; PISP01000002; PKD43459.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N0VGY8; -.
DR OrthoDB; 9772053at2; -.
DR Proteomes; UP000233398; Unassembled WGS sequence.
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: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 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:UP000233398}.
FT ACT_SITE 202
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-1"
FT BINDING 63
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 172
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 172
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 203
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 225
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 314
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
SQ SEQUENCE 345 AA; 37462 MW; DBC0597CF6A2B5B2 CRC64;
MKLNFKLLKE IVSTPGAPGH ESPIRSVLIN HIRDHVDEYS VDRMGNLIAR VKGDGPKVMA
AAHMDEISLI TTHVDSKGFI RFSTLGGFDP ETLITQRVLI HGNETIPGVI GSKPIHIQTD
SEKKSKSKLK NLFIDTGLPA DRVKELIPNG TPVTRDKDLL ELGECISSKS LDNRISVYIL
IEALQRAKKS NCDFYAAFTV QEEVGIRGAR VAAQAIQPEI GLNLDVTLAN DLPGVSDHEV
CTLLGEGIGI KIMDKSVICT PTLVRHLEDL ANKNSIKIQR EVLTAGGTDT SAMQYLVGIG
SHVTSISCPV RYIHSTAETC AISDVKAGIK LTTLCIENIG SYSFK
//