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Database: UniProt
Entry: D5U7A4_BRAM5
LinkDB: D5U7A4_BRAM5
Original site: D5U7A4_BRAM5 
ID   D5U7A4_BRAM5            Unreviewed;       405 AA.
AC   D5U7A4;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   SubName: Full=Amidohydrolase {ECO:0000313|EMBL:ADG70692.1};
DE            EC=3.5.1.14 {ECO:0000313|EMBL:ADG70692.1};
GN   OrderedLocusNames=Bmur_0591 {ECO:0000313|EMBL:ADG70692.1};
OS   Brachyspira murdochii (strain ATCC 51284 / DSM 12563 / 56-150) (Serpulina
OS   murdochii).
OC   Bacteria; Spirochaetota; Spirochaetia; Brachyspirales; Brachyspiraceae;
OC   Brachyspira.
OX   NCBI_TaxID=526224 {ECO:0000313|EMBL:ADG70692.1, ECO:0000313|Proteomes:UP000001915};
RN   [1] {ECO:0000313|EMBL:ADG70692.1, ECO:0000313|Proteomes:UP000001915}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51284 / DSM 12563 / 56-150
RC   {ECO:0000313|Proteomes:UP000001915};
RX   PubMed=21304710; DOI=10.4056/sigs.831993;
RA   Pati A., Sikorski J., Gronow S., Munk C., Lapidus A., Copeland A.,
RA   Glavina Del Tio T., Nolan M., Lucas S., Chen F., Tice H., Cheng J.F.,
RA   Han C., Detter J.C., Bruce D., Tapia R., Goodwin L., Pitluck S.,
RA   Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Spring S.,
RA   Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Brachyspira murdochii type strain (56-150).";
RL   Stand. Genomic Sci. 2:260-269(2010).
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DR   EMBL; CP001959; ADG70692.1; -; Genomic_DNA.
DR   RefSeq; WP_013113118.1; NC_014150.1.
DR   AlphaFoldDB; D5U7A4; -.
DR   STRING; 526224.Bmur_0591; -.
DR   KEGG; brm:Bmur_0591; -.
DR   eggNOG; COG1473; Bacteria.
DR   HOGENOM; CLU_023257_0_1_12; -.
DR   OrthoDB; 9776731at2; -.
DR   Proteomes; UP000001915; Chromosome.
DR   GO; GO:0004046; F:aminoacylase activity; IEA:UniProtKB-EC.
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   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:ADG70692.1}.
FT   DOMAIN          189..284
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   405 AA;  44772 MW;  FDC3B486613C8A40 CRC64;
     MEELELIKSK IKEIKEELIN IRRDLHSHPE LSEKEFQTMN TISNHLKKYN IEHKTEVADT
     GITADIKGKD KSFTAAFRAD IDALPIDDLK NCSYSSKNKG VCHACGHDIH TAINLGIASV
     FQNNSKGITP PCNIRLIFQP AEETVGGALR MIKENALENV NVIYGLHVST HSDTGFVQIN
     DNIVNASCLD FKIKVYGRSA HAANPAGGID TIVIAAKIID SIQTIISRNV QAEDSAVITI
     GTINGGTAEN IICGYTEMTG TIRALRESTM TKIITKIKKI IKGIAYSFDA NAEFIETVYF
     ASLVNWKEAS DIVRENAVSL LGEKNVLELK PSMGAEDFSF FIQNKAGAFF NIGARNKKKG
     IIHEAHNGLF DADEECIEIG LTLQIMNLYK SYSKKDIFWL GKERD
//
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