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Database: UniProt
Entry: A8F9Q6_BACP2
LinkDB: A8F9Q6_BACP2
Original site: A8F9Q6_BACP2 
ID   A8F9Q6_BACP2            Unreviewed;       375 AA.
AC   A8F9Q6;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   27-MAR-2024, entry version 85.
DE   SubName: Full=Amidohydrolase {ECO:0000313|EMBL:ABV60973.1};
GN   OrderedLocusNames=BPUM_0275 {ECO:0000313|EMBL:ABV60973.1};
OS   Bacillus pumilus (strain SAFR-032).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=315750 {ECO:0000313|EMBL:ABV60973.1, ECO:0000313|Proteomes:UP000001355};
RN   [1] {ECO:0000313|EMBL:ABV60973.1, ECO:0000313|Proteomes:UP000001355}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SAFR-032 {ECO:0000313|EMBL:ABV60973.1,
RC   ECO:0000313|Proteomes:UP000001355};
RX   PubMed=17895969; DOI=10.1371/journal.pone.0000928;
RA   Gioia J., Yerrapragada S., Qin X., Jiang H., Igboeli O.C., Muzny D.,
RA   Dugan-Rocha S., Ding Y., Hawes A., Liu W., Perez L., Kovar C., Dinh H.,
RA   Lee S., Nazareth L., Blyth P., Holder M., Buhay C., Tirumalai M.R., Liu Y.,
RA   Dasgupta I., Bokhetache L., Fujita M., Karouia F., Eswara Moorthy P.,
RA   Siefert J., Uzman A., Buzumbo P., Verma A., Zwiya H., McWilliams B.D.,
RA   Olowu A., Clinkenbeard K.D., Newcombe D., Golebiewski L., Petrosino J.F.,
RA   Nicholson W.L., Fox G.E., Venkateswaran K., Highlander S.K.,
RA   Weinstock G.M.;
RT   "Paradoxical DNA repair and peroxide resistance gene conservation in
RT   Bacillus pumilus SAFR-032.";
RL   PLoS ONE 2:E928-E928(2007).
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DR   EMBL; CP000813; ABV60973.1; -; Genomic_DNA.
DR   RefSeq; WP_012008845.1; NZ_VEIS01000004.1.
DR   AlphaFoldDB; A8F9Q6; -.
DR   STRING; 315750.BPUM_0275; -.
DR   MEROPS; M20.A26; -.
DR   KEGG; bpu:BPUM_0275; -.
DR   eggNOG; COG1473; Bacteria.
DR   HOGENOM; CLU_023257_0_1_9; -.
DR   OrthoDB; 9776731at2; -.
DR   Proteomes; UP000001355; Chromosome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR   CDD; cd08018; M20_Acy1_amhX-like; 1.
DR   Gene3D; 3.30.70.360; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR037484; AmhX-like.
DR   InterPro; IPR017439; Amidohydrolase.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   NCBIfam; TIGR01891; amidohydrolases; 1.
DR   PANTHER; PTHR11014:SF122; AMIDOHYDROLASE AMHX; 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;
FT   DOMAIN          176..263
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   375 AA;  40925 MW;  FCC5546E8A5B93CF CRC64;
     MTTLTNDMQQ TVKDIFEHLH AHPEISWEET NTTAYLEDLL KKIGCQTRTF DDCTGVIGEI
     GEGSPVVAVR ADIDALWQEV DGEFQANHSC GHDAHMTMAL GTFMALKEKE LPNGTIRFIF
     QPAEEKGGGA LKMIEEGVLA DVDYLYGVHV RPIQETLNGR CAPAILHGSS NHYIGTIIGE
     EAHGARPHLG INVIEVASTL VQRLAHIHVD PRVAHSVKMT NLHAGGGSSN IIPGKASFTL
     DVRAQTNEVM DELEKEIERA VHSVADAFGA SISLSTDHRL PAATLNEEAV QMMSQAIEKV
     LGKEQLDPPL VTTGGEDFHF YAAKLPHIKS TMLGLGCDLE PGLHHPYMTF DRSAIFTGIE
     ILTEAVYQTL QQHSS
//
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