ID A4F8I7_SACEN Unreviewed; 503 AA.
AC A4F8I7;
DT 17-APR-2007, integrated into UniProtKB/TrEMBL.
DT 17-APR-2007, sequence version 1.
DT 24-JAN-2024, entry version 94.
DE SubName: Full=Leucine aminopeptidase {ECO:0000313|EMBL:CAM00362.1};
DE EC=3.4.11.1 {ECO:0000313|EMBL:CAM00362.1};
DE SubName: Full=Leucyl aminopeptidase {ECO:0000313|EMBL:PFG94156.1};
GN Name=pepA {ECO:0000313|EMBL:CAM00362.1};
GN OrderedLocusNames=SACE_1030 {ECO:0000313|EMBL:CAM00362.1};
GN ORFNames=A8924_1423 {ECO:0000313|EMBL:PFG94156.1};
OS Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748 /
OS NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharopolyspora.
OX NCBI_TaxID=405948 {ECO:0000313|EMBL:CAM00362.1, ECO:0000313|Proteomes:UP000006728};
RN [1] {ECO:0000313|EMBL:CAM00362.1, ECO:0000313|Proteomes:UP000006728}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 /
RC NRRL 2338 {ECO:0000313|Proteomes:UP000006728}, and NRRL 2338
RC {ECO:0000313|EMBL:CAM00362.1};
RX PubMed=17369815; DOI=10.1038/nbt1297;
RA Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N., Dickens S.,
RA Haydock S.F., Leadlay P.F.;
RT "Complete genome sequence of the erythromycin-producing bacterium
RT Saccharopolyspora erythraea NRRL23338.";
RL Nat. Biotechnol. 25:447-453(2007).
RN [2] {ECO:0000313|EMBL:PFG94156.1, ECO:0000313|Proteomes:UP000225825}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40517 {ECO:0000313|EMBL:PFG94156.1,
RC ECO:0000313|Proteomes:UP000225825};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase M17 family.
CC {ECO:0000256|ARBA:ARBA00009528}.
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DR EMBL; AM420293; CAM00362.1; -; Genomic_DNA.
DR EMBL; PDBV01000001; PFG94156.1; -; Genomic_DNA.
DR RefSeq; WP_009949793.1; NZ_PDBV01000001.1.
DR AlphaFoldDB; A4F8I7; -.
DR STRING; 405948.SACE_1030; -.
DR KEGG; sen:SACE_1030; -.
DR eggNOG; COG0260; Bacteria.
DR HOGENOM; CLU_013734_2_2_11; -.
DR OMA; HFDIYGW; -.
DR OrthoDB; 9809354at2; -.
DR Proteomes; UP000006728; Chromosome.
DR Proteomes; UP000225825; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00433; Peptidase_M17; 1.
DR Gene3D; 3.40.220.10; Leucine Aminopeptidase, subunit E, domain 1; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR011356; Leucine_aapep/pepB.
DR InterPro; IPR043472; Macro_dom-like.
DR InterPro; IPR000819; Peptidase_M17_C.
DR PANTHER; PTHR11963:SF23; CYTOSOL AMINOPEPTIDASE; 1.
DR PANTHER; PTHR11963; LEUCINE AMINOPEPTIDASE-RELATED; 1.
DR Pfam; PF00883; Peptidase_M17; 1.
DR PRINTS; PR00481; LAMNOPPTDASE.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00631; CYTOSOL_AP; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000313|EMBL:CAM00362.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CAM00362.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000006728}.
FT DOMAIN 349..356
FT /note="Cytosol aminopeptidase"
FT /evidence="ECO:0000259|PROSITE:PS00631"
SQ SEQUENCE 503 AA; 52577 MW; 126F71CC872AE8B5 CRC64;
MIPTSLVEVD VVRRPRDGVP TAVPLPDGES GPELAPVAEA FEVDIALLEA IGVKSAAGDV
RTVPLPEGRF GWVVGIGSGE AAQWRTAGAA LARATREKLG ETGEAEGDTV DFGEPSEAEY
LQIRLPAGIG QDAVSALALG LALGDYRFRV TGQPAPPRLR KALLVTDDEE LREPVARARE
WAAATALARD LANSPSNVKD PDWFTGLAAR LAGEVDGLTA TVRDEKWLAD HGFGGILAVG
GGSASPPRLL ELAWRPADAT GPHLVLVGKG ITFDTGGISL KPAEGMHLMR TDMSGGAAVI
GAMLAVARLG LRVRVTALVP SAENHLSGSS YRPGDVVRHY GGKTTEVGNT DAEGRMVMAD
ALVYGVRHHE ADLLVDVATL TGAMKVALGL RTGGVFATDP DLSRRLRDAG DRVGEAWWPM
PLIEDHTEAV RGELADVNQT PPGPGGVTAA LFLREFTEGL PWAHLDIAGP ARADKNYAEV
VAGGTGFAAR SLVEFVASLA EQG
//