ID A0A1Q5KWR2_9ACTN Unreviewed; 432 AA.
AC A0A1Q5KWR2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=AMK32_01405 {ECO:0000313|EMBL:OKJ86010.1};
OS Streptomyces sp. CB01883.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1703943 {ECO:0000313|EMBL:OKJ86010.1, ECO:0000313|Proteomes:UP000186398};
RN [1] {ECO:0000313|EMBL:OKJ86010.1, ECO:0000313|Proteomes:UP000186398}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB01883 {ECO:0000313|EMBL:OKJ86010.1,
RC ECO:0000313|Proteomes:UP000186398};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(2016).
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}.
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:OKJ86010.1}.
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DR EMBL; LIWA01000001; OKJ86010.1; -; Genomic_DNA.
DR RefSeq; WP_073887536.1; NZ_LIWA01000001.1.
DR AlphaFoldDB; A0A1Q5KWR2; -.
DR OrthoDB; 5288740at2; -.
DR Proteomes; UP000186398; 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:UP000186398};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00467}.
FT BINDING 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00467"
FT BINDING 157
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00467"
FT BINDING 408
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00467"
SQ SEQUENCE 432 AA; 46038 MW; E02820E1C08F4691 CRC64;
MSAPARFDRG HTDDLMSFLA ASPSPYHAVA NTAERLEKAG FRQVAETDAW DGTSGGKYLL
RGGAIVAWFV PEDAAPHTPF HIIGAHTDSP NLRIKPRPDS GAHGWRQVAV EIYGGPLLNS
WLDRDLGLAG RLTLRDGSTV LADVDRPLLR VPQLAIHLDR TVGTDGLKLD KQRHLQPVWG
LGDDVLDGDL IAFLEQEAGL ETGSVTGWDL MTYPVEPPAY LGRDRELVAG PRMDNLLSVH
AGVAALVAAA TSGAELTRIP VLAAFDHEEN GSQSDTGADG PLLGTALERS VFARGGSYED
RARAFAGTVC LSSDTGHAVH PNYAERHDPT HHPRVNGGPI LKVNVNNRYA TDGSGRAVFA
AACERADVPF QSFVSNNSMP CGTTIGPITA ARHGIRTVDI GVAILSMHSV RELCGADDPF
HLANALTAFL EG
//