ID A0A3S3Z4J7_9SPHI Unreviewed; 371 AA.
AC A0A3S3Z4J7;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 22-FEB-2023, entry version 17.
DE SubName: Full=M42 family peptidase {ECO:0000313|EMBL:RWY57216.1};
GN ORFNames=EPL05_01390 {ECO:0000313|EMBL:RWY57216.1};
OS Mucilaginibacter gilvus.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Mucilaginibacter.
OX NCBI_TaxID=2305909 {ECO:0000313|EMBL:RWY57216.1, ECO:0000313|Proteomes:UP000286701};
RN [1] {ECO:0000313|EMBL:RWY57216.1, ECO:0000313|Proteomes:UP000286701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F01003 {ECO:0000313|EMBL:RWY57216.1,
RC ECO:0000313|Proteomes:UP000286701};
RA Yan Y.-Q., Du Z.-J.;
RT "Mucilaginibacter antarcticum sp. nov., isolated from antarctic soil.";
RL Submitted (JAN-2019) 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:RWY57216.1}.
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DR EMBL; SBIW01000001; RWY57216.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S3Z4J7; -.
DR OrthoDB; 9772053at2; -.
DR Proteomes; UP000286701; 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:UP000286701}.
FT ACT_SITE 226
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-1"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 192
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 192
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 227
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 249
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 336
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
SQ SEQUENCE 371 AA; 41406 MW; 3D51DCA31ED9E5EC CRC64;
MAKKKTEVEQ KPAVVTENSL AFFEKYINNA SPTGFEWKGQ QMWLDYLKPY IDDHFVDNYG
TAVGVINPTA EYKVVIEAHA DEISWFVNYI TSDGLIYVIR NGGSDHQIAP SKRVNIHTDN
GIVKAVFGWP AIHTRLGGEK EEAPTLKNIF LDCGCTSKEE VEKLGIHVGC VITYEDEFMV
LNNRYYVGRA LDNRAGGFMI AEVARLLKEN NVTLPFGLYI VNAVQEEIGL RGAEMIAHRI
KPHVAIVTDV THDTGTPMIN KITQGDLSCG KGPVISYAPA VQNNLNKLLI ESAQKANIPF
QRQASSRSTG TDTDAFAYSN DGVPSALISL PLRYMHTTVE MIHKEDVDNV IRLIYESLLN
IKSGQDFRYF K
//
