ID   A0A2I9EDA5_9FLAO        Unreviewed;       443 AA.
AC   A0A2I9EDA5;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Bacterial leucyl aminopeptidase {ECO:0000313|EMBL:GBF19761.1};
GN   ORFNames=C21_01931 {ECO:0000313|EMBL:GBF19761.1};
OS   Arenibacter sp. NBRC 103722.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Arenibacter.
OX   NCBI_TaxID=1113929 {ECO:0000313|EMBL:GBF19761.1, ECO:0000313|Proteomes:UP000095208};
RN   [1] {ECO:0000313|EMBL:GBF19761.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C-21 {ECO:0000313|EMBL:GBF19761.1};
RA   Ito K., Nakajima N., Yamamura S., Tomita M., Suzuki H., Amachi S.;
RT   "Draft Genome Sequence of Arenibacter sp. Strain C-21, an Iodine-
RT   Accumulating Bacterium Isolated from Surface Marine Sediment.";
RL   Genome Announc. 4:e01155-16(2016).
RN   [2] {ECO:0000313|EMBL:GBF19761.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C-21 {ECO:0000313|EMBL:GBF19761.1};
RA   Gaut B.S., Morton B.R., Clegg M.T., Duvall M.R.;
RL   Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC   -!- SIMILARITY: Belongs to the peptidase M28 family. M28B subfamily.
CC       {ECO:0000256|ARBA:ARBA00005634}.
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:GBF19761.1}.
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DR   EMBL; BDGL02000007; GBF19761.1; -; Genomic_DNA.
DR   RefSeq; WP_069858527.1; NZ_BDGL02000007.1.
DR   AlphaFoldDB; A0A2I9EDA5; -.
DR   Proteomes; UP000095208; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008235; F:metalloexopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd00063; FN3; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR045175; M28_fam.
DR   InterPro; IPR007484; Peptidase_M28.
DR   PANTHER; PTHR12147; METALLOPEPTIDASE M28 FAMILY MEMBER; 1.
DR   PANTHER; PTHR12147:SF55; PEPTIDE HYDROLASE; 1.
DR   Pfam; PF04389; Peptidase_M28; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000313|EMBL:GBF19761.1};
KW   Hydrolase {ECO:0000313|EMBL:GBF19761.1};
KW   Protease {ECO:0000313|EMBL:GBF19761.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000095208}.
FT   DOMAIN          109..305
FT                   /note="Peptidase M28"
FT                   /evidence="ECO:0000259|Pfam:PF04389"
SQ   SEQUENCE   443 AA;  49808 MW;  DD653EB2197628FB CRC64;
     MHKFAIAYIF LFSVCLIGQT DQRIYDIMNK VSAERIKKDV TTLVSFGTRH TLSDTISNTR
     GIGAARRWIK SEFDRISEKC NDCLEVSYQR DLVKKEESNR IPKDVWVVNV VAIQRGTTYP
     DRYIIMSGDI DSRVSDANNY TSDSPGANDN ASGMAGIIEA ARVLSNYKFE NSIIYLGLSG
     EEQGLFGGQG LVKSAKEKGW DIIGIFNNDM IGNIKGGDGI ISNTDFRIFS EPVPPTETER
     ERNMRRFYGG EVDGISRQLA RYVYKNVKTY MPEMNPMMIY RLDRFGRGGH HRPFNDAGYA
     GIRIMEAHEN YTQQHQDIRV ENGIAYGDVL EHVNFDYAKK LTSVNAINLA SLAWAHPAPK
     EVKIGGIVEP SAKFQWSKVP GATGYKIYWR DTTSPTWDHS RFVGDVSEFT LEGVVLDNFF
     FGVSAVGKDG FESVVVFPNA ILR
//