ID   A0A1K1RFP3_9BACT        Unreviewed;       430 AA.
AC   A0A1K1RFP3;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Xaa-Pro aminopeptidase {ECO:0000313|EMBL:SFW70502.1};
GN   ORFNames=SAMN05661012_03718 {ECO:0000313|EMBL:SFW70502.1};
OS   Chitinophaga sancti.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Chitinophaga.
OX   NCBI_TaxID=1004 {ECO:0000313|EMBL:SFW70502.1, ECO:0000313|Proteomes:UP000183788};
RN   [1] {ECO:0000313|EMBL:SFW70502.1, ECO:0000313|Proteomes:UP000183788}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 784 {ECO:0000313|EMBL:SFW70502.1,
RC   ECO:0000313|Proteomes:UP000183788};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- SIMILARITY: Belongs to the peptidase M24B family.
CC       {ECO:0000256|ARBA:ARBA00008766, ECO:0000256|RuleBase:RU000590}.
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DR   EMBL; FPIZ01000011; SFW70502.1; -; Genomic_DNA.
DR   RefSeq; WP_072362717.1; NZ_FPIZ01000011.1.
DR   AlphaFoldDB; A0A1K1RFP3; -.
DR   STRING; 1004.SAMN05661012_03718; -.
DR   OrthoDB; 9806388at2; -.
DR   Proteomes; UP000183788; Unassembled WGS sequence.
DR   GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR   Gene3D; 3.90.230.10; Creatinase/methionine aminopeptidase superfamily; 1.
DR   Gene3D; 3.40.350.10; Creatinase/prolidase N-terminal domain; 1.
DR   InterPro; IPR007865; Aminopep_P_N.
DR   InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR   InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR   InterPro; IPR000994; Pept_M24.
DR   InterPro; IPR001131; Peptidase_M24B_aminopep-P_CS.
DR   PANTHER; PTHR43226; XAA-PRO AMINOPEPTIDASE 3; 1.
DR   PANTHER; PTHR43226:SF4; XAA-PRO AMINOPEPTIDASE 3; 1.
DR   Pfam; PF05195; AMP_N; 1.
DR   Pfam; PF00557; Peptidase_M24; 1.
DR   SMART; SM01011; AMP_N; 1.
DR   SUPFAM; SSF55920; Creatinase/aminopeptidase; 1.
DR   SUPFAM; SSF53092; Creatinase/prolidase N-terminal domain; 1.
DR   PROSITE; PS00491; PROLINE_PEPTIDASE; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000313|EMBL:SFW70502.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU000590};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670}.
FT   DOMAIN          6..142
FT                   /note="Aminopeptidase P N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01011"
SQ   SEQUENCE   430 AA;  49448 MW;  593353E71C40851B CRC64;
     MKNLPLDSQI FIKNRQRFIA EMQPNSIAII NSNDELPSNG DALYRFEQNH DLYWLTGVEQ
     EDTMLILYPD NPDPKYREVL VLVRPNELKE KWDGHRLRKD EALAVSGIST VIWLDVLDGL
     LQPWIHEATN IYLNSNENNR KSSRIAVRDY RYAEEMRARY PLHNYLRAAI IFKKLRAVKT
     PEEIKVMQTA MDITEKAFRR LLQFIRPGVG EHQIQAEIVH EFLSNRSDGE GYTSIIASGD
     RARTLHYIAN NQECKDGELV LMDFGAVYGG YNADMTRTVP VNGKFTPRQR EVYDACLHLH
     NYAKSILKPG LTIAKYHEMM GEEAGKVFVK INLLKEEDIK NQDPESPAYR KYLYHGISHH
     LGVGVHDLGP SFWQPIPDGA VLTIEPGIYI EEEKMGVRIE NNVWITSKGN IDLMKNIPIT
     ADEIEALMKK
//