ID   A1BB03_PARDP            Unreviewed;       492 AA.
AC   A1BB03;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 93.
DE   SubName: Full=Leucyl aminopeptidase {ECO:0000313|EMBL:ABL72697.1};
DE            EC=3.4.11.1 {ECO:0000313|EMBL:ABL72697.1};
GN   OrderedLocusNames=Pden_4634 {ECO:0000313|EMBL:ABL72697.1};
OS   Paracoccus denitrificans (strain Pd 1222).
OG   Plasmid pPD1222 {ECO:0000313|Proteomes:UP000000361}.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Paracoccus.
OX   NCBI_TaxID=318586 {ECO:0000313|EMBL:ABL72697.1, ECO:0000313|Proteomes:UP000000361};
RN   [1] {ECO:0000313|Proteomes:UP000000361}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pd 1222 {ECO:0000313|Proteomes:UP000000361};
RC   PLASMID=pPD1222 {ECO:0000313|Proteomes:UP000000361};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S.,
RA   Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M.,
RA   Richardson P.;
RT   "Complete sequence of plasmid 1 of Paracoccus denitrificans PD1222.";
RL   Submitted (DEC-2006) 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; CP000491; ABL72697.1; -; Genomic_DNA.
DR   RefSeq; WP_011750856.1; NC_008688.1.
DR   AlphaFoldDB; A1BB03; -.
DR   EnsemblBacteria; ABL72697; ABL72697; Pden_4634.
DR   GeneID; 75503996; -.
DR   KEGG; pde:Pden_4634; -.
DR   eggNOG; COG0260; Bacteria.
DR   HOGENOM; CLU_013734_6_0_5; -.
DR   OrthoDB; 9809354at2; -.
DR   Proteomes; UP000000361; Plasmid pPD1222.
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; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR011356; Leucine_aapep/pepB.
DR   InterPro; IPR000819; Peptidase_M17_C.
DR   PANTHER; PTHR11963; LEUCINE AMINOPEPTIDASE-RELATED; 1.
DR   PANTHER; PTHR11963:SF23; ZGC:152830; 1.
DR   Pfam; PF00883; Peptidase_M17; 1.
DR   PRINTS; PR00481; LAMNOPPTDASE.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW   ECO:0000313|EMBL:ABL72697.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ABL72697.1};
KW   Plasmid {ECO:0000313|EMBL:ABL72697.1};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000361}.
FT   DOMAIN          168..482
FT                   /note="Cytosol aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00883"
SQ   SEQUENCE   492 AA;  51856 MW;  08B018633ED40C08 CRC64;
     MTAWTQIDIL QSDEPAAEFV LAFASKDGAI PEQDEARLSL AIRHAGFAAQ PGQWLDVSPA
     KGTDPRIILI GAPEIGTATP HDWASLGGSI VEAMAALRLE AARLSDGAAL ADDARLSGVL
     LGVLLHGFRP DTGRKQPDPT PWPQRLLIPQ GRNGACDQAM RTARAVNRAR AWVEAPANRL
     TPQVWAAELP AIFEPLGATL RIFDSGALQE MGASALLAVG RASEFPPLLA VVEWRGAPAR
     KGWDAVLVGK GMTFDSGGLN LKTAAPVIAR MGFDMGGGAA VLGAVELAAS RKAGCNVAAI
     VPMAENAIDG KSFRPGDVIE SLGGLTIEIR NTDGEGRLVL ADGIAYGLQT YRPAHVIDIA
     TLTGMIAVAL LEEFAGLYSN DDALAAELDE AGRATGEFLW RMPCQSNQDH VVETPVADVA
     NMSTFPGLLG TGLSAPVSGP KLLQKFVGDT PWAHIDIAGT VWATRRSAYG GNNATGYGVR
     LLDQWLRRFE RG
//