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Database: UniProt
Entry: F2I496_AERUA
LinkDB: F2I496_AERUA
Original site: F2I496_AERUA 
ID   F2I496_AERUA            Unreviewed;       359 AA.
AC   F2I496; A0A9Q4H689;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 55.
DE   SubName: Full=Aminopeptidase P family protein {ECO:0000313|EMBL:MCY3055567.1};
DE   SubName: Full=Creatinase {ECO:0000313|EMBL:AEA00915.1};
GN   OrderedLocusNames=HMPREF9243_0834 {ECO:0000313|EMBL:AEA00915.1};
GN   ORFNames=ODY48_07460 {ECO:0000313|EMBL:MCY3055567.1};
OS   Aerococcus urinae (strain CCUG 59500 / ACS-120-V-Col10a).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Aerococcus;
OC   Aerococcus incertae sedis.
OX   NCBI_TaxID=2976812 {ECO:0000313|EMBL:AEA00915.1, ECO:0000313|Proteomes:UP000008129};
RN   [1] {ECO:0000313|Proteomes:UP000008129}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACS-120-V-Col10a {ECO:0000313|Proteomes:UP000008129};
RA   Durkin A.S., Madupu R., Radune D., Hostetler J., Torralba M., Gillis M.,
RA   Methe B., Sutton G., Nelson K.E.;
RT   "Complete genome sequence of Aerococcus urinae strain ACS-120-V-Col10a.";
RL   Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AEA00915.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ACS-120-V-Col10a {ECO:0000313|EMBL:AEA00915.1};
RA   Durkin A.S., Madupu R., Radune D., Hostetler J., Torralba M., Gillis M.,
RA   Methe B., Sutton G., Nelson K.E.;
RL   Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:MCY3055567.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CDC-1656-U92 {ECO:0000313|EMBL:MCY3055567.1};
RA   Christensen J., Senneby E.;
RT   "Aerococcus urinae taxonomy study.";
RL   Submitted (SEP-2022) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase M24B family.
CC       {ECO:0000256|RuleBase:RU000590}.
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DR   EMBL; CP002512; AEA00915.1; -; Genomic_DNA.
DR   EMBL; JAOTMI010000024; MCY3055567.1; -; Genomic_DNA.
DR   RefSeq; WP_013669159.1; NC_015278.1.
DR   AlphaFoldDB; F2I496; -.
DR   STRING; 866775.HMPREF9243_0834; -.
DR   MEROPS; M24.008; -.
DR   KEGG; aur:HMPREF9243_0834; -.
DR   PATRIC; fig|866775.3.peg.789; -.
DR   eggNOG; COG0006; Bacteria.
DR   HOGENOM; CLU_017266_4_0_9; -.
DR   OMA; YCSDRTR; -.
DR   Proteomes; UP000008129; Chromosome.
DR   Proteomes; UP001075187; Unassembled WGS sequence.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase 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:MCY3055567.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU000590}; Protease {ECO:0000313|EMBL:MCY3055567.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008129}.
FT   DOMAIN          4..133
FT                   /note="Creatinase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01321"
FT   DOMAIN          141..343
FT                   /note="Peptidase M24"
FT                   /evidence="ECO:0000259|Pfam:PF00557"
SQ   SEQUENCE   359 AA;  39842 MW;  466FA9E211F9431D CRC64;
     MEERIKKLQA SLQEESLGAY LVTDSYNLRY MTGFTGTSGL ALVTTKNAYF ITDFRYTEQA
     KLQCQGYEVI EAGGSASHSS PLRLIQELLQ ENGVNQLGYE EQHVTVAQFD DFENVLEVQL
     VPASGMIEVL RQIKDADEIN KIKKACEITD KAFEYILGYI KPGISEIDIA NTLDFKMREF
     GASGISFDTI VASGKRSAMP HGVATDKLIA NHELITIDFG CYYQGYCSDM TRTVAVGQVD
     STLEKIYQIV YDANRMAQEA LKPGMTGQEL DAIARDYIES QGYGKNFGHS LGHSIGLEVH
     EAPMAGPNSK NILKADQFIT DEPGIYLENL GGVRIEDDLL IHEDGNEYIT KSPRELIVL
//
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