ID A0A2I0QV30_9BACI Unreviewed; 352 AA.
AC A0A2I0QV30;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Endoglucanase {ECO:0000313|EMBL:PKR78178.1};
GN ORFNames=CEY16_08330 {ECO:0000313|EMBL:PKR78178.1};
OS Halalkalibacillus sediminis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halalkalibacillus.
OX NCBI_TaxID=2018042 {ECO:0000313|EMBL:PKR78178.1, ECO:0000313|Proteomes:UP000243524};
RN [1] {ECO:0000313|EMBL:PKR78178.1, ECO:0000313|Proteomes:UP000243524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B3227 {ECO:0000313|EMBL:PKR78178.1,
RC ECO:0000313|Proteomes:UP000243524};
RA He R.-H., Du Z.-J.;
RT "the draft geome sequence of Illustriluteabacillus marina B3227.";
RL Submitted (JUN-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:PKR78178.1}.
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DR EMBL; PJNH01000002; PKR78178.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I0QV30; -.
DR OrthoDB; 9772053at2; -.
DR Proteomes; UP000243524; 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:SF9; ENDOGLUCANASE; 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:UP000243524}.
FT ACT_SITE 207
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-1"
FT BINDING 62
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 175
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 175
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 208
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 230
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 317
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
SQ SEQUENCE 352 AA; 38623 MW; 4449E7CE6196676C CRC64;
MENLLKDLTN IHGPCGFEED VATYIAKRLN DSVDSIEVDG VGNLTVRKKG RKDGPKIVVA
AHMDEIGFIV KKIEENGLLR FEKLGGHDDR ILLSQRVQLN TSKGLRNGII GTISAHMKKF
DEPNKIRSHQ QLYIDIGANS KQDAAELGVK VGDTVTWHPY YDRLTENRVM GKAFDDRAGC
AVLIQAFEEL EANDFSGEMV GVFTVQEEVG LRGARVASRQ QNADVAIALD TTAVSDTPEE
MMDQTLAIGG GTGIKVLDFS LIANKKVRNH LVEIAEREKI THQLEVFPGI GTDAGELSLA
HQGVPTGVLS IPSRYAHSSV EVVDLNDIEA TKNLLVAFVK EMKATVEYKF NI
//