ID Q81AB5_BACCR Unreviewed; 381 AA.
AC Q81AB5;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 114.
DE SubName: Full=N-acyl-L-amino acid amidohydrolase {ECO:0000313|EMBL:AAP10593.1};
DE EC=3.5.1.14 {ECO:0000313|EMBL:AAP10593.1};
GN OrderedLocusNames=BC_3664 {ECO:0000313|EMBL:AAP10593.1};
OS Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=226900 {ECO:0000313|EMBL:AAP10593.1, ECO:0000313|Proteomes:UP000001417};
RN [1] {ECO:0000313|EMBL:AAP10593.1, ECO:0000313|Proteomes:UP000001417}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB
RC 9373 / NCTC 2599 / NRRL B-3711 {ECO:0000313|Proteomes:UP000001417};
RX PubMed=12721630; DOI=10.1038/nature01582;
RA Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.;
RT "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT anthracis.";
RL Nature 423:87-91(2003).
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DR EMBL; AE016877; AAP10593.1; -; Genomic_DNA.
DR RefSeq; NP_833392.1; NC_004722.1.
DR RefSeq; WP_000253674.1; NZ_CP034551.1.
DR AlphaFoldDB; Q81AB5; -.
DR MEROPS; M20.015; -.
DR KEGG; bce:BC3664; -.
DR PATRIC; fig|226900.8.peg.3767; -.
DR HOGENOM; CLU_023257_1_1_9; -.
DR OrthoDB; 9776731at2; -.
DR Proteomes; UP000001417; Chromosome.
DR GO; GO:0004046; F:aminoacylase activity; IEA:UniProtKB-EC.
DR GO; GO:0016787; F:hydrolase activity; IBA:GO_Central.
DR CDD; cd05669; M20_Acy1_YxeP-like; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR017439; Amidohydrolase.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR InterPro; IPR033846; YxeP-like.
DR NCBIfam; TIGR01891; amidohydrolases; 1.
DR PANTHER; PTHR11014:SF63; METALLOPEPTIDASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G09600)-RELATED; 1.
DR PANTHER; PTHR11014; PEPTIDASE M20 FAMILY MEMBER; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PIRSF; PIRSF005962; Pept_M20D_amidohydro; 1.
DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:AAP10593.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001417}.
FT DOMAIN 179..274
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 381 AA; 41663 MW; 9F3B50913F8EBE5A CRC64;
MVSISNQLKE KLISIRRHLH EYPELSYEEF ETTKAIKNWL EEKNITIIDS NLETGIIAEV
SGNKNGPIVA VRADIDALPI QEETHLSYAS KVRGKMHACG HDFHTAAILG TAFLLKERES
SLNGTVRFIF QPAEESSNGA CKVIDAGHLR NVQAIFGMHN KPDLPVGTIG IKDGPLMAGV
DRFEIEIHGV GTHAAVPDAG VDPIVASSQI VMALQTIVSR NISSSHNAVV SVTNIHAGNT
WNVIPEKATL EGTIRTFQAE TREKIPALME RIIKGVSDAL GVKTKFRFYS GPPAVHNDKA
LSDLSTQVAT KMNLNIISPS LSMAGEDFSF YQQEIPGSFV FMGTSGTHEW HHPAFTINEE
ALPISAEYFA LLAERALKQF S
//
