ID B8DSR6_BIFA0 Unreviewed; 523 AA.
AC B8DSR6;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE SubName: Full=Xaa-Pro aminopeptidase {ECO:0000313|EMBL:ACL29045.1};
DE EC=3.4.11.9 {ECO:0000313|EMBL:ACL29045.1};
GN Name=pepP {ECO:0000313|EMBL:ACL29045.1};
GN OrderedLocusNames=BLA_0752 {ECO:0000313|EMBL:ACL29045.1};
OS Bifidobacterium animalis subsp. lactis (strain AD011).
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=442563 {ECO:0000313|EMBL:ACL29045.1, ECO:0000313|Proteomes:UP000002456};
RN [1] {ECO:0000313|EMBL:ACL29045.1, ECO:0000313|Proteomes:UP000002456}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AD011 {ECO:0000313|EMBL:ACL29045.1,
RC ECO:0000313|Proteomes:UP000002456};
RX PubMed=19011029; DOI=10.1128/JB.01515-08;
RA Kim J.F., Jeong H., Yu D.S., Choi S.-H., Hur C.-G., Park M.-S., Yoon S.H.,
RA Kim D.-W., Ji G.E., Park H.-S., Oh T.K.;
RT "Genome sequence of the probiotic bacterium Bifidobacterium animalis subsp.
RT lactis AD011.";
RL J. Bacteriol. 191:678-679(2009).
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}.
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DR EMBL; CP001213; ACL29045.1; -; Genomic_DNA.
DR RefSeq; WP_004218681.1; NC_011835.1.
DR AlphaFoldDB; B8DSR6; -.
DR STRING; 442563.BLA_0752; -.
DR MEROPS; M24.033; -.
DR GeneID; 66533513; -.
DR KEGG; bla:BLA_0752; -.
DR PATRIC; fig|442563.4.peg.784; -.
DR HOGENOM; CLU_017266_1_0_11; -.
DR Proteomes; UP000002456; Chromosome.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR CDD; cd01087; Prolidase; 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; IPR007865; Aminopep_P_N.
DR InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR000994; Pept_M24.
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.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000313|EMBL:ACL29045.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ACL29045.1};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000313|EMBL:ACL29045.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002456}.
FT DOMAIN 61..208
FT /note="Aminopeptidase P N-terminal"
FT /evidence="ECO:0000259|SMART:SM01011"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 523 AA; 58542 MW; 7A3842B7FB2D8485 CRC64;
MSEVITEQDK EYEAREQAAA PGDDQPMNDR VNNRSLRPRS DAFVDFMSSG WDNNEPEIER
LESASYIPAR LQVLSEAFPG ERLVIPAGQP KVRNNDCDYA FRPDSAFSYY TGLGQDYEAG
AVLVLDPNED GTHTPMLFVA PRADHYTQDF FKDPHYGEYW VGPRAGLKEL EAMTGIETHD
IAQLDDMLGK DVGTENGAVQ LRVIRETDPQ ITAIVNELRE GHGFPDEADN TVRDDKLHEF
ASEARMEKDD FEVREIRRAV DATKHGFDNI LKKLPSALGK PRSERILEGA FNAVSREEGN
EVGYDTIIAS GAHAPILHWI RNTGTVNDGE LLLIDAGVEV DSLYTADITR TFPTNGKFTD
FQKKLYQAVL DSQQAGFEAA KPGATYSDIH HACMRVIAER LHDWGILPVD VEESLSPEGQ
QHRRWLACGV AHHLGLDVHD CAQARYESYQ GAKITPGMVF TIEPGLYFRE DDLMIPPEYR
GIGIRIEDDV LMTEDGPEWI SAGIPKQIDD VEAWMAQMAD TNN
//
