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Database: UniProt
Entry: A8AZC0_STRGC
LinkDB: A8AZC0_STRGC
Original site: A8AZC0_STRGC 
ID   A8AZC0_STRGC            Unreviewed;       353 AA.
AC   A8AZC0;
DT   23-OCT-2007, integrated into UniProtKB/TrEMBL.
DT   23-OCT-2007, sequence version 1.
DT   24-JAN-2024, entry version 94.
DE   SubName: Full=X-Pro aminopeptidase {ECO:0000313|EMBL:ABV11069.1};
DE            EC=3.4.11.9 {ECO:0000313|EMBL:ABV11069.1};
GN   OrderedLocusNames=SGO_1864 {ECO:0000313|EMBL:ABV11069.1};
OS   Streptococcus gordonii (strain Challis / ATCC 35105 / BCRC 15272 / CH1 /
OS   DL1 / V288).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=467705 {ECO:0000313|EMBL:ABV11069.1, ECO:0000313|Proteomes:UP000001131};
RN   [1] {ECO:0000313|EMBL:ABV11069.1, ECO:0000313|Proteomes:UP000001131}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Challis / ATCC 35105 / BCRC 15272 / CH1 / DL1 / V288
RC   {ECO:0000313|Proteomes:UP000001131};
RX   PubMed=17720781; DOI=10.1128/JB.01023-07;
RA   Vickerman M.M., Iobst S., Jesionowski A.M., Gill S.R.;
RT   "Genome-wide transcriptional changes in Streptococcus gordonii in response
RT   to competence signaling peptide.";
RL   J. Bacteriol. 189:7799-7807(2007).
CC   -!- SIMILARITY: Belongs to the peptidase M24B family.
CC       {ECO:0000256|RuleBase:RU000590}.
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DR   EMBL; CP000725; ABV11069.1; -; Genomic_DNA.
DR   RefSeq; WP_012130888.1; NC_009785.1.
DR   AlphaFoldDB; A8AZC0; -.
DR   STRING; 467705.SGO_1864; -.
DR   KEGG; sgo:SGO_1864; -.
DR   eggNOG; COG0006; Bacteria.
DR   HOGENOM; CLU_017266_4_0_9; -.
DR   OMA; YCSDRTR; -.
DR   Proteomes; UP000001131; Chromosome.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd01092; APP-like; 1.
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; IPR029149; Creatin/AminoP/Spt16_NTD.
DR   InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR   InterPro; IPR000587; Creatinase_N.
DR   InterPro; IPR000994; Pept_M24.
DR   InterPro; IPR001131; Peptidase_M24B_aminopep-P_CS.
DR   PANTHER; PTHR46112; AMINOPEPTIDASE; 1.
DR   PANTHER; PTHR46112:SF3; AMINOPEPTIDASE YPDF; 1.
DR   Pfam; PF01321; Creatinase_N; 1.
DR   Pfam; PF00557; Peptidase_M24; 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:ABV11069.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ABV11069.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU000590}; Protease {ECO:0000313|EMBL:ABV11069.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001131}.
FT   DOMAIN          4..127
FT                   /note="Creatinase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01321"
FT   DOMAIN          135..337
FT                   /note="Peptidase M24"
FT                   /evidence="ECO:0000259|Pfam:PF00557"
SQ   SEQUENCE   353 AA;  39379 MW;  585EC5EBA3F2A1F2 CRC64;
     MLSRVEKFEV ALAQTECDAV LVTNLKNIYY LTGFSGTEAT VFISKTRRIF LTDARYTLIA
     KGVVQGFDIV ETRDALGEIA KIIADDKLEK IGFDDEISYA YFKMLESLFS GYELVPMTGF
     IENLRMIKDE QEIATIRKAC QISDQAFLDV LDFIKPGETT ELAVMNFLDA RMRQLGASGA
     SFDFIIASGY RSAMPHGVAS DKVIQNGETL TMDFGCYYNH YVSDMTRTVH VGQVTDEERE
     IYDIVLRSNQ ALIEAAKAGL SRIDFDRIPR QIINDAGYGP YFSHGIGHGI GLDIHEIPYF
     GKSEEPIEAG MVLTDEPGIY LDGKYGVRIE DDLLITETGC EVLTLAPKEL IVI
//
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