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Database: UniProt
Entry: A0A0B5EQN4_STRA4
LinkDB: A0A0B5EQN4_STRA4
Original site: A0A0B5EQN4_STRA4 
ID   A0A0B5EQN4_STRA4        Unreviewed;       430 AA.
AC   A0A0B5EQN4;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-SEP-2017, entry version 12.
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=SLNWT_3528 {ECO:0000313|EMBL:AJE83904.1};
OS   Streptomyces albus (strain ATCC 21838 / DSM 41398 / FERM P-419 / JCM
OS   4703 / NBRC 107858).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1081613 {ECO:0000313|EMBL:AJE83904.1, ECO:0000313|Proteomes:UP000031523};
RN   [1] {ECO:0000313|EMBL:AJE83904.1, ECO:0000313|Proteomes:UP000031523}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 21838 / DSM 41398 / FERM P-419 / JCM 4703 / NBRC 107858
RC   {ECO:0000313|Proteomes:UP000031523};
RA   Lu C.;
RT   "Enhanced salinomycin production by adjusting the supply of polyketide
RT   extender units in Streptomyce albus DSM 41398.";
RL   Submitted (JAN-2015) 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}.
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DR   EMBL; CP010519; AJE83904.1; -; Genomic_DNA.
DR   EnsemblBacteria; AJE83904; AJE83904; SLNWT_3528.
DR   KEGG; sals:SLNWT_3528; -.
DR   KO; K01267; -.
DR   Proteomes; UP000031523; Chromosome.
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:AJE83904.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000031523};
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};
KW   Protease {ECO:0000256|HAMAP-Rule:MF_00467,
KW   ECO:0000256|RuleBase:RU004386};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031523};
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       406    406       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
SQ   SEQUENCE   430 AA;  45743 MW;  AA404FE89482D292 CRC64;
     MSTPPRFDRG HTDDLMSFLA TSPTPYHAVA NAAERLEKAG FRQVAETDAW EGGTGGRYVL
     RGGALIAWFV PEGAEPHTPF RIVGAHTDSP NLRIKPLPDT SAHGWRQVAV EVYGGPLLNS
     WLDRDLGLAG RLSLRDGASR LVNVDRALLR VPQLAIHLDR AVGTDGLQLD KQRHVQPVWG
     LGEAHEGDLI RFLEQEYGLA EGEVTGWDLM THSIEPPAYL GRDRELVAGP RMDNLLSVHA
     GTAALAAASS SGSLRHIPVL AAFDHEESGS QSDTGADGPL LGSVLERSIF ARGGGFEDRA
     RAFAGTVCLS SDTGHAVHPN YAERHDPTHH PRAGGGPILK VNVNNRYATD GSGRAVFAAA
     CEKAGVPFQS FVSNNSMPCG TTIGPITAAR HGIRTVDIGV AILSMHSARE LCAAEDPSLL
     TSALVAFLDG
//
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