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Database: UniProt
Entry: A0A196QWP0_9RHOB
LinkDB: A0A196QWP0_9RHOB
Original site: A0A196QWP0_9RHOB 
ID   A0A196QWP0_9RHOB        Unreviewed;       460 AA.
AC   A0A196QWP0;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Leucyl aminopeptidase {ECO:0000313|EMBL:OAN96150.1};
GN   ORFNames=A8B74_13655 {ECO:0000313|EMBL:OAN96150.1};
OS   Sulfitobacter geojensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Sulfitobacter.
OX   NCBI_TaxID=1342299 {ECO:0000313|EMBL:OAN96150.1, ECO:0000313|Proteomes:UP000078317};
RN   [1] {ECO:0000313|Proteomes:UP000078317}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EhN01 {ECO:0000313|Proteomes:UP000078317};
RA   Rosana A., Orata F., Boucher Y., Case R.;
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase M17 family.
CC       {ECO:0000256|ARBA:ARBA00009528}.
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:OAN96150.1}.
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DR   EMBL; LXYM01000007; OAN96150.1; -; Genomic_DNA.
DR   RefSeq; WP_064222895.1; NZ_LXYM01000007.1.
DR   AlphaFoldDB; A0A196QWP0; -.
DR   STRING; 1342299.Z947_957; -.
DR   eggNOG; COG0260; Bacteria.
DR   Proteomes; UP000078317; 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   InterPro; IPR048816; Peptidase_M17_N_1.
DR   PANTHER; PTHR11963:SF53; AMINOPEPTIDASE; 1.
DR   PANTHER; PTHR11963; LEUCINE AMINOPEPTIDASE-RELATED; 1.
DR   Pfam; PF00883; Peptidase_M17; 1.
DR   Pfam; PF21337; Peptidase_M17_N_1; 1.
DR   PRINTS; PR00481; LAMNOPPTDASE.
DR   SUPFAM; SSF52949; Macro domain-like; 1.
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:OAN96150.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078317}.
FT   DOMAIN          308..315
FT                   /note="Cytosol aminopeptidase"
FT                   /evidence="ECO:0000259|PROSITE:PS00631"
SQ   SEQUENCE   460 AA;  48386 MW;  B22C43D7DF33E6C4 CRC64;
     MPLSFAPSSD TTIPLHVLSE EQLDAWLGTQ PEATQNALAS QGFTGALGQT ASIAGQDGLP
     LMAVAGYGTA AARRRGRFHL AGAAAKLPKG DYRITSDLDA GTLAVEALGW LLASYRFDRY
     RKQPPLLARL VAPEGINAPR IEAQANGEAL TRDLINTPAN DMGPPDLEQA ARDLAGRQGA
     AITVITGDDL LAQNFPLIHT VGRAADRAPR LIDMRWGDTG PKLTLVGKGV CFDTGGLNLK
     PGASMGLMKK DMGGAGAVLG LAQMIMTMDV PVQLRVLIPA VENAVAGNAF RPGDILTSRK
     GLTVEINNTD AEGRLVLADA LALADEEQPD QVISMATLTG AARVAVGPDL APYFSDDSTF
     VSALETAALK ECDPVWRMPF HAPYEAMIEP GIADLDNAPK GGFAGCITAA LFLRRFVSDS
     PYAHFDIYGW QPADAPARPK GGTGQATRAL FDALPALLEL
//
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