ID C5BXR2_BEUC1 Unreviewed; 427 AA.
AC C5BXR2;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=Amidohydrolase {ECO:0000313|EMBL:ACQ78806.1};
DE EC=3.5.1.32 {ECO:0000313|EMBL:ACQ78806.1};
GN OrderedLocusNames=Bcav_0543 {ECO:0000313|EMBL:ACQ78806.1};
OS Beutenbergia cavernae (strain ATCC BAA-8 / DSM 12333 / NBRC 16432).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Beutenbergiaceae;
OC Beutenbergia.
OX NCBI_TaxID=471853 {ECO:0000313|EMBL:ACQ78806.1, ECO:0000313|Proteomes:UP000007962};
RN [1] {ECO:0000313|EMBL:ACQ78806.1, ECO:0000313|Proteomes:UP000007962}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-8 / DSM 12333 / NBRC 16432
RC {ECO:0000313|Proteomes:UP000007962};
RX PubMed=21304633; DOI=10.4056/sigs.1162;
RA Land M., Pukall R., Abt B., Goker M., Rohde M., Glavina Del Rio T.,
RA Tice H., Copeland A., Cheng J.F., Lucas S., Chen F., Nolan M., Bruce D.,
RA Goodwin L., Pitluck S., Ivanova N., Mavromatis K., Ovchinnikova G.,
RA Pati A., Chen A., Palaniappan K., Hauser L., Chang Y.J., Jefferies C.C.,
RA Saunders E., Brettin T., Detter J.C., Han C., Chain P., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA Lapidus A.;
RT "Complete genome sequence of Beutenbergia cavernae type strain (HKI
RT 0122).";
RL Stand. Genomic Sci. 1:21-28(2009).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001618; ACQ78806.1; -; Genomic_DNA.
DR AlphaFoldDB; C5BXR2; -.
DR STRING; 471853.Bcav_0543; -.
DR KEGG; bcv:Bcav_0543; -.
DR eggNOG; COG1473; Bacteria.
DR HOGENOM; CLU_023257_6_0_11; -.
DR Proteomes; UP000007962; Chromosome.
DR GO; GO:0047980; F:hippurate hydrolase 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:ACQ78806.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007962}.
FT DOMAIN 202..298
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 427 AA; 44482 MW; D8C8DB84D67C64F5 CRC64;
MTDAPTRIDA LTDGLDGRLA DLRSLYEDLH AHPELSMQEH RTAGVVAERL RAQGYEVTEG
VGGTGVVGVL ANGAGPRVLL RADMDGLPLR EDTGLPFAST VTAIGADGVE VPVMHGCGHD
VHVTALLGAT AQLAENRGAW SGTVLAVFQP AEETGEGAQA MIEDDLFARF GTPDVCLGQH
VSSLPAGHAM LRPGPMMATA DAVHIRLFGR GGHGSTPELT VDPVVMGASL VMRLQTIASR
EISSQDPVVV TVGSLVAGMK ENIIPDDAVL KISVRTFDPT IRDQVMAAIE RMARAEAAAS
GAPREPEFTY LHSLPLNAND VDGEARTRAA LALGLGTGHV HEMPRPVSGS EDFGRFGAAA
GCPSVFWFVG GYDPALFADI LAGRASIMSL PEGVAYNHSP HFAPSAPGTL DGAVRAMLAA
ASEWLGS
//
