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Database: UniProt
Entry: A0A085GBX9_9ENTR
LinkDB: A0A085GBX9_9ENTR
Original site: A0A085GBX9_9ENTR 
ID   A0A085GBX9_9ENTR        Unreviewed;       592 AA.
AC   A0A085GBX9;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Xaa-Pro aminopeptidase {ECO:0000313|EMBL:KFC81224.1};
DE            EC=3.-.-.- {ECO:0000313|EMBL:KFC81224.1};
DE            EC=3.4.11.9 {ECO:0000313|EMBL:KFC81224.1};
GN   ORFNames=GBAG_2507 {ECO:0000313|EMBL:KFC81224.1};
OS   Buttiauxella agrestis ATCC 33320.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Buttiauxella.
OX   NCBI_TaxID=1006004 {ECO:0000313|EMBL:KFC81224.1, ECO:0000313|Proteomes:UP000028653};
RN   [1] {ECO:0000313|EMBL:KFC81224.1, ECO:0000313|Proteomes:UP000028653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33320 {ECO:0000313|EMBL:KFC81224.1,
RC   ECO:0000313|Proteomes:UP000028653};
RA   Plunkett G.III., Neeno-Eckwall E.C., Glasner J.D., Perna N.T.;
RT   "ATOL: Assembling a taxonomically balanced genome-scale reconstruction of
RT   the evolutionary history of the Enterobacteriaceae.";
RL   Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase M24B family.
CC       {ECO:0000256|ARBA:ARBA00008766}.
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:KFC81224.1}.
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DR   EMBL; JMPI01000032; KFC81224.1; -; Genomic_DNA.
DR   RefSeq; WP_034496413.1; NZ_JMPI01000032.1.
DR   AlphaFoldDB; A0A085GBX9; -.
DR   STRING; 1006004.GBAG_2507; -.
DR   eggNOG; COG0006; Bacteria.
DR   OrthoDB; 9806388at2; -.
DR   Proteomes; UP000028653; Unassembled WGS sequence.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR   CDD; cd01085; APP; 1.
DR   Gene3D; 3.90.230.10; Creatinase/methionine aminopeptidase superfamily; 1.
DR   Gene3D; 3.40.350.10; Creatinase/prolidase N-terminal domain; 2.
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; IPR033740; Pept_M24B.
DR   InterPro; IPR032416; Peptidase_M24_C.
DR   PANTHER; PTHR43763; XAA-PRO AMINOPEPTIDASE 1; 1.
DR   PANTHER; PTHR43763:SF6; XAA-PRO AMINOPEPTIDASE 1; 1.
DR   Pfam; PF01321; Creatinase_N; 1.
DR   Pfam; PF16189; Creatinase_N_2; 1.
DR   Pfam; PF00557; Peptidase_M24; 1.
DR   Pfam; PF16188; Peptidase_M24_C; 1.
DR   SUPFAM; SSF55920; Creatinase/aminopeptidase; 1.
DR   SUPFAM; SSF53092; Creatinase/prolidase N-terminal domain; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000313|EMBL:KFC81224.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KFC81224.1};
KW   Protease {ECO:0000313|EMBL:KFC81224.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028653}.
FT   DOMAIN          8..127
FT                   /note="Creatinase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01321"
FT   DOMAIN          312..521
FT                   /note="Peptidase M24"
FT                   /evidence="ECO:0000259|Pfam:PF00557"
FT   DOMAIN          528..587
FT                   /note="Peptidase M24 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16188"
SQ   SEQUENCE   592 AA;  65695 MW;  28DBD9F1A2AD5DEB CRC64;
     MQPTSSLHAL RKLLKERDLD GMIIPRADAH QSEDCSPNDN KLEFISNFDG SAGLALILAD
     RALLFVDGRY QVQARQQVNL EEFEIHHLHD EPLHLWLRDN LPAGKRIAFE PLLMVNSQYE
     SLRTSGCDLV AVNDDPLNTI WADRPAAPRG VVTQMPDEIS GEPSAAKRAR MAALLKEKGV
     DYLAITLLDN IAWLLNVRGS DVAMNPVAQS FALLKNDGEI EWFVDDAKLH QLDSTLLNSV
     SLQHHDSFLA RCQQLAAGKR FSLDGDTAPV AVRIAVEAGG GEIVWQPDPI TLVKANKNSA
     ELEGYRACHI EDGVAWVNFL AWLSHEVPLR EAAGNPVTEL EAQEKQLAFR QQCDNFREQS
     FSTISAAAHN AAMCHYHSAP ETNMAITTKA FYLNDSGGQY FNGTTDATRT LNFGQVDAQR
     RLHYTAVLRG FLALISLQFP QGTQGHQLDA FARRPLWEMG LDYDHGTGHG VGHCLFIHEA
     PHRLAKKVNP WPLLPGVIQT IEPGYYLEGS HGMRVENQVE IVASQPGFCK FASLTLIPID
     LSAVEISLLS EQDIAWLDDY HQQVREILSP LVSGDARPWL IEATAPVRTQ RA
//
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