ID L1KKN2_9ACTN Unreviewed; 432 AA.
AC L1KKN2;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-SEP-2017, entry version 27.
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=STRIP9103_04893 {ECO:0000313|EMBL:EKX61346.1};
OS Streptomyces ipomoeae 91-03.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=698759 {ECO:0000313|EMBL:EKX61346.1, ECO:0000313|Proteomes:UP000010411};
RN [1] {ECO:0000313|EMBL:EKX61346.1, ECO:0000313|Proteomes:UP000010411}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91-03 {ECO:0000313|EMBL:EKX61346.1,
RC ECO:0000313|Proteomes:UP000010411};
RA Huguet-Tapia J.C., Durkin A.S., Pettis G.S., Badger J.H.;
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_00467, ECO:0000256|RuleBase:RU004387};
CC -!- SIMILARITY: Belongs to the peptidase M18 family.
CC {ECO:0000256|HAMAP-Rule:MF_00467, ECO:0000256|RuleBase:RU004386}.
CC -!- CAUTION: The sequence shown here is derived from an
CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC preliminary data. {ECO:0000313|EMBL:EKX61346.1}.
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DR EMBL; AEJC01000601; EKX61346.1; -; Genomic_DNA.
DR RefSeq; WP_009336522.1; NZ_AEJC01000601.1.
DR MEROPS; M18.002; -.
DR EnsemblBacteria; EKX61346; EKX61346; STRIP9103_04893.
DR PATRIC; fig|698759.3.peg.7909; -.
DR OrthoDB; POG091H01I4; -.
DR Proteomes; UP000010411; 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 HAMAP; MF_00467; Aminopeptidase_M18_2; 1.
DR InterPro; IPR022984; M18_aminopeptidase_2.
DR InterPro; IPR001948; Peptidase_M18.
DR Pfam; PF02127; Peptidase_M18; 1.
DR PRINTS; PR00932; AMINO1PTASE.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|HAMAP-Rule:MF_00467,
KW ECO:0000256|RuleBase:RU004386, ECO:0000313|EMBL:EKX61346.1};
KW Complete proteome {ECO:0000313|Proteomes:UP000010411};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00467,
KW ECO:0000256|RuleBase:RU004386};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00467,
KW ECO:0000256|RuleBase:RU004386};
KW Metalloprotease {ECO:0000256|HAMAP-Rule:MF_00467,
KW ECO:0000256|RuleBase:RU004386, ECO:0000313|EMBL:EKX61346.1};
KW Protease {ECO:0000256|HAMAP-Rule:MF_00467,
KW ECO:0000256|RuleBase:RU004386, ECO:0000313|EMBL:EKX61346.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010411};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_00467, ECO:0000256|RuleBase:RU004386}.
FT METAL 86 86 Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
FT METAL 157 157 Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
FT METAL 408 408 Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
SQ SEQUENCE 432 AA; 46229 MW; ED073D9023BEDAE5 CRC64;
MRTPPRFDRG HTDDLMSFLT ASPSPYHAVA NAAERLEKAG FRQVSETDAW DGSLGGKYVL
RGGAIIAWYV PEGADPHTPF RIVGAHTDSP NLRVKPRPDT GGHGFRQVAV EIYGGPLLNS
WLDRDLGIAG RLSLRDGTSR LVNIDRPLLR VPQLAIHLDR AVTSEGLKLD KQRHLQPIWG
LGDDIRDGDL ISFLEQESGL PAGEVTGWDL MTHSVEPPAY LGRDKELLAG PRMDNLLSVH
AGTAALAAVA TSGDDLPYIP VLAAFDHEEN GSQSDTGADG PLLGGVLERS VFARGGSYED
RARAFAGTVC LSSDTGHAVH PNYAERHDPT HHPRADAGPI LKVNVNNRYA TDGSGRAIFA
AACERAGVPF QTFVSNNSMP CGTTIGPITA ARHGIRTVDI GVAILSMHSA RELCGAKDPY
LLTNALAAFL EG
//
