ID A0A256CTD6_9GAMM Unreviewed; 365 AA.
AC A0A256CTD6;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Hydrolase {ECO:0000313|EMBL:OYQ81357.1};
GN ORFNames=B9T19_01400 {ECO:0000313|EMBL:OYQ81357.1};
OS Ignatzschineria sp. F8392.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cardiobacteriales;
OC Ignatzschineriaceae; Ignatzschineria.
OX NCBI_TaxID=1980117 {ECO:0000313|EMBL:OYQ81357.1, ECO:0000313|Proteomes:UP000215803};
RN [1] {ECO:0000313|EMBL:OYQ81357.1, ECO:0000313|Proteomes:UP000215803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F8392 {ECO:0000313|EMBL:OYQ81357.1,
RC ECO:0000313|Proteomes:UP000215803};
RA Gulvik C.A.;
RT "Wohlfahrtiimonas and Ignatzschineria genomes.";
RL Submitted (APR-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:OYQ81357.1}.
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DR EMBL; NEFF01000001; OYQ81357.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A256CTD6; -.
DR OrthoDB; 9772053at2; -.
DR Proteomes; UP000215803; 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 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, ECO:0000313|EMBL:OYQ81357.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR001123-2}; Protease {ECO:0000256|ARBA:ARBA00022670}.
FT ACT_SITE 213
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-1"
FT BINDING 69
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 181
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 181
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 214
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 236
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 332
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
SQ SEQUENCE 365 AA; 39357 MW; 196ABEEC95E9CB1C CRC64;
MANLKENIKS LLKDLTHINA GVGQEQPVIS YIMSALKGEV DELKVDHNGN VHAIKRGHKE
GLTMMVAAHT DEIGLIVKNI LPNGFLLIEK LGGVPDNMLL GRKVYVGKNN LPGVIGTKPG
HLQTAEEAKR VKTVAECYVD MALPSREAVE AHGVSVGDQV IISGEFTEMV DPDYISMKAI
DDRLGCSILI ELLKNLSKQD FAGTLHGVFT VQEEVGLYGA QKVGDGYTPD YAIVLDTIPA
GDTPDVNTER DLPVRLGAGP ALPLADAVMP IFFSMVHPAV RRAIEKQATT QNIHLQKLTL
LGGGYTTDSA KLSHAGGGIP CATLAIPRRY SHSPIELTNL NDSVDVYNIL QGLIRDNENM
NTAFI
//