ID   A0A0F2NST5_9FLAO        Unreviewed;       468 AA.
AC   A0A0F2NST5;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Peptidase M17 {ECO:0000313|EMBL:KJS05043.1};
GN   ORFNames=VR77_09820 {ECO:0000313|EMBL:KJS05043.1};
OS   Flavobacteriales bacterium BRH_c54.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales.
OX   NCBI_TaxID=1629721 {ECO:0000313|EMBL:KJS05043.1, ECO:0000313|Proteomes:UP000033681};
RN   [1] {ECO:0000313|EMBL:KJS05043.1, ECO:0000313|Proteomes:UP000033681}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRH_c54 {ECO:0000313|EMBL:KJS05043.1};
RA   Bagnoud A., Chourey K., Hettich R.L., de Bruijn I., Andersson A.F.,
RA   Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT   "Microbial metabolic network in the subsurface.";
RL   Submitted (MAR-2015) 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:KJS05043.1}.
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DR   EMBL; LADZ01000053; KJS05043.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F2NST5; -.
DR   STRING; 1629721.VR77_09820; -.
DR   PATRIC; fig|1629721.3.peg.1879; -.
DR   Proteomes; UP000033681; 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; LEUCINE AMINOPEPTIDASE-RELATED; 1.
DR   PANTHER; PTHR11963:SF23; ZGC:152830; 1.
DR   Pfam; PF00883; Peptidase_M17; 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   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protease {ECO:0000256|ARBA:ARBA00022670}.
FT   DOMAIN          318..325
FT                   /note="Cytosol aminopeptidase"
FT                   /evidence="ECO:0000259|PROSITE:PS00631"
SQ   SEQUENCE   468 AA;  51381 MW;  A3805B97B9A51E87 CRC64;
     MEIKKASKLD PKENLIFLIT NEKELPITSF TKEELSFIKK ELKNEQKQVE INRLNTYVFV
     VLCDKENDYK AAEKIRIAAS NLLTTLNSKK VVSATVIGET IKIVPFIEGI GLANYQFLKY
     FSDKKVNTFN KLNYYTENKS DNIKEIEVLV EAANFAKDLV NEPLSFLTAT QLSKEIKNLG
     KNYGFKVEVL TKAKIEALKM GGLLAVNKGS IDPPTFSILE WKPAKAKNKK PIVLVGKGVV
     YDTGGLSLKP TPNSMDMMKC DMGGAAAVIG AMVAIAKNKL PYHVIVLVPA TDNRPGGNAY
     VPGDVIKMYN GKTVEVLNTD AEGRMILADA LSYADKYQPE LVIDVATLTG AAANAIGHYG
     VVAMGNTPEK TMNKLKESGN NTFERIVEFP FWDEYNEQLK SSIADLTNLG NGAGGAITAG
     KFLENFTNAP YIHLDIAGPA FIKKQINYLS QGGTGVGVRL LYDFVKNY
//