ID D1BHV5_SANKS Unreviewed; 445 AA.
AC D1BHV5;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Acetylornithine deacetylase/succinyldiaminopimelate desuccinylase-like deacylase {ECO:0000313|EMBL:ACZ22025.1};
GN OrderedLocusNames=Sked_21030 {ECO:0000313|EMBL:ACZ22025.1};
OS Sanguibacter keddieii (strain ATCC 51767 / DSM 10542 / NCFB 3025 / ST-74).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Sanguibacteraceae;
OC Sanguibacter.
OX NCBI_TaxID=446469 {ECO:0000313|EMBL:ACZ22025.1, ECO:0000313|Proteomes:UP000000322};
RN [1] {ECO:0000313|EMBL:ACZ22025.1, ECO:0000313|Proteomes:UP000000322}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51767 / DSM 10542 / NCFB 3025 / ST-74
RC {ECO:0000313|Proteomes:UP000000322};
RX PubMed=21304646;
RA Ivanova N., Sikorski J., Sims D., Brettin T., Detter J.C., Han C.,
RA Lapidus A., Copeland A., Glavina Del Rio T., Nolan M., Chen F., Lucas S.,
RA Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S., Pati A.,
RA Mavromatis K., Chen A., Palaniappan K., D'haeseleer P., Chain P.,
RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Goker M., Pukall R.,
RA Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Sanguibacter keddieii type strain (ST-74).";
RL Stand. Genomic Sci. 1:110-118(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; CP001819; ACZ22025.1; -; Genomic_DNA.
DR RefSeq; WP_012867094.1; NC_013521.1.
DR AlphaFoldDB; D1BHV5; -.
DR STRING; 446469.Sked_21030; -.
DR KEGG; ske:Sked_21030; -.
DR eggNOG; COG0624; Bacteria.
DR HOGENOM; CLU_021802_11_2_11; -.
DR OrthoDB; 7055905at2; -.
DR Proteomes; UP000000322; 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}.
FT DOMAIN 202..343
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 445 AA; 47512 MW; A859340BEFABD46F CRC64;
MTSQNTAPTP VPSAQDEVVQ ICQDLLRIDT SNFGDGSGPG ERAAAEYVMT SLHEVGLEPE
LFESERGRAS VVVRLPGLDP TRPALVLHGH LDVVPAQADD WRVDPFGGEE IDGLLWGRGA
VDMKDMDAMM LAVVRQMVRE GRKPARDVVL AFFADEEAGG ALGARWAVDH RPELFEGATE
AISEVGGFST TINGQRAYLL QTAEKGIGWL RLIADGRAGH GSQVQTDNAV VHLAAAVARI
GQHRWPYVMT PTVEALLRGV CDLTGLPFDP EDPATVDALI DAMGSAARFV GATVQNTSNP
SQLAAGYKAN VIPGRAEATV DARFLPGHEE SAMATLRELA GEHVRIEPIH QDIALEVPFS
GNLVDAMTSS LLAEDPEAVV LPYALSGGTD NKSLARLGIT GYGFAPLLLP ESLDFPGMFH
GVDERVPTDS LKFGTRVLDR LLATC
//
