ID A0A239HGS5_9PSED Unreviewed; 429 AA.
AC A0A239HGS5;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Probable M18 family aminopeptidase 2 {ECO:0000256|HAMAP-Rule:MF_00467};
DE EC=3.4.11.- {ECO:0000256|HAMAP-Rule:MF_00467};
GN Name=apeB {ECO:0000256|HAMAP-Rule:MF_00467};
GN ORFNames=SAMN05444352_115106 {ECO:0000313|EMBL:SNS80512.1};
OS Pseudomonas japonica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=256466 {ECO:0000313|EMBL:SNS80512.1, ECO:0000313|Proteomes:UP000198407};
RN [1] {ECO:0000313|Proteomes:UP000198407}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22348 {ECO:0000313|Proteomes:UP000198407};
RA Varghese N., Submissions S.;
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947,
CC ECO:0000256|HAMAP-Rule:MF_00467, ECO:0000256|RuleBase:RU004387};
CC -!- SIMILARITY: Belongs to the peptidase M18 family.
CC {ECO:0000256|ARBA:ARBA00008290, ECO:0000256|HAMAP-Rule:MF_00467,
CC ECO:0000256|RuleBase:RU004386}.
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DR EMBL; FZOL01000015; SNS80512.1; -; Genomic_DNA.
DR RefSeq; WP_042127920.1; NZ_FZOL01000015.1.
DR AlphaFoldDB; A0A239HGS5; -.
DR STRING; 1215104.GCA_000730585_01460; -.
DR OrthoDB; 5288740at2; -.
DR Proteomes; UP000198407; Unassembled WGS sequence.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-UniRule.
DR CDD; cd05658; M18_DAP; 1.
DR Gene3D; 2.30.250.10; Aminopeptidase i, Domain 2; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR HAMAP; MF_00467; Aminopeptidase_M18_2; 1.
DR InterPro; IPR022984; M18_aminopeptidase_2.
DR InterPro; IPR001948; Peptidase_M18.
DR InterPro; IPR023358; Peptidase_M18_dom2.
DR PANTHER; PTHR28570; ASPARTYL AMINOPEPTIDASE; 1.
DR PANTHER; PTHR28570:SF3; ASPARTYL AMINOPEPTIDASE; 1.
DR Pfam; PF02127; Peptidase_M18; 1.
DR PRINTS; PR00932; AMINO1PTASE.
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, ECO:0000256|HAMAP-
KW Rule:MF_00467};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00467};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00467};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049, ECO:0000256|HAMAP-
KW Rule:MF_00467};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_00467};
KW Reference proteome {ECO:0000313|Proteomes:UP000198407};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00467}.
FT BINDING 82
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00467"
FT BINDING 156
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00467"
FT BINDING 401
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00467"
SQ SEQUENCE 429 AA; 46948 MW; 66DAEE90704B1443 CRC64;
MRDALNHGLI EFLKASPTPF HATASLAKRL EAAGYQRLDE RDSWATVPGG RYYLTRNDSS
IIAIKLGRHS PLLDGIRLVG AHTDSPCLRV KPQPELQRHG FWQLGVEVYG GALLAPWFDR
DLSLAGRVTF RRDGKVESAL VDFKLPIAVI PNLAIHLNRS ANEGWAINPQ TELPPILAQV
AGDERVDFRA LLTEQLAREH GLNADVVLDY ELSFYDTQDA ALIGLHGEFI AGARLDNLLS
CFAGLQALLN ADSDETCVLV CNDHEEVGSC SACGADGPML EQTLRRLLPD GDEFVRTIQR
SLLVSADNAH GVHPNYADKH DGNHGPKLNA GPVIKVNNNQ RYATNSETAG FFRHLCMAEE
VPVQSFVVRS DMGCGSTIGP ITASHLGVRT VDIGLPTFAM HSIRELCGSQ DLAHLVKVLT
AFYRTRELP
//
