ID D5UFB3_CELFN Unreviewed; 442 AA.
AC D5UFB3;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Peptidase M20 {ECO:0000313|EMBL:ADG74910.1};
GN OrderedLocusNames=Cfla_2015 {ECO:0000313|EMBL:ADG74910.1};
OS Cellulomonas flavigena (strain ATCC 482 / DSM 20109 / BCRC 11376 / JCM
OS 18109 / NBRC 3775 / NCIMB 8073 / NRS 134).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=446466 {ECO:0000313|EMBL:ADG74910.1, ECO:0000313|Proteomes:UP000000849};
RN [1] {ECO:0000313|EMBL:ADG74910.1, ECO:0000313|Proteomes:UP000000849}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 482 / DSM 20109 / BCRC 11376 / JCM 18109 / NBRC 3775 /
RC NCIMB 8073 / NRS 134 {ECO:0000313|Proteomes:UP000000849};
RX PubMed=21304688; DOI=10.4056/sigs.1012662;
RA Abt B., Foster B., Lapidus A., Clum A., Sun H., Pukall R., Lucas S.,
RA Glavina Del Rio T., Nolan M., Tice H., Cheng J.F., Pitluck S., Liolios K.,
RA Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Goodwin L., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Rohde M.,
RA Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Cellulomonas flavigena type strain (134).";
RL Stand. Genomic Sci. 3:15-25(2010).
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; CP001964; ADG74910.1; -; Genomic_DNA.
DR RefSeq; WP_013117244.1; NC_014151.1.
DR AlphaFoldDB; D5UFB3; -.
DR STRING; 446466.Cfla_2015; -.
DR KEGG; cfl:Cfla_2015; -.
DR eggNOG; COG0624; Bacteria.
DR HOGENOM; CLU_021802_11_2_11; -.
DR Proteomes; UP000000849; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 1.10.150.900; -; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR PANTHER; PTHR43808; ACETYLORNITHINE DEACETYLASE; 1.
DR PANTHER; PTHR43808:SF32; CONSERVED PROTEIN; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PIRSF; PIRSF036696; ACY-1; 2.
DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000000849}.
FT DOMAIN 199..331
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 442 AA; 46733 MW; EFD9089A39F2BC8A CRC64;
MTADATGVPT AEDEVVDLCR DLIRIDTTNP GDGTGPGERA AAEYVVGLLQ EVGLEPELFE
SAPGRANVVV RLEGSDPSRP ALVVHGHLDV VPAHAPDWSV DPFGAEIRDG LVWGRGAVDM
KDMDAMVLAV VRQMVREGRR PARDVVLAMF ADEEAGGRLG AHWAVEHRPE LFAGATEAIS
EVGGFSVDVA GQRVYLLQTA EKGLAWLRLV AEGRAGHGSQ VNADNAVTHL AAAVARLGQH
RWPLQLTPTV RALLDGVADL TGLRFDPEDD GSVDALVDAL GPASRFVGAT LRHSTNPTRL
AAGYKENVIP GSATASVDGR FLPGRQDEFD ATVAELVGPH VRVEDLVRDT GLEAPTSGDL
VDAMVAAVVA EDPGAHVLPY MLSGGTDNKS LSLLGITGYG FAPLRLPADL DFAGMFHGVD
ERVPVDALRF GTRVLDRLLT TC
//
