ID D6Y138_BACIE Unreviewed; 242 AA.
AC D6Y138;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=Alpha/beta hydrolase fold protein {ECO:0000313|EMBL:ADH98642.1};
GN OrderedLocusNames=Bsel_1125 {ECO:0000313|EMBL:ADH98642.1};
OS Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC Salisediminibacterium.
OX NCBI_TaxID=439292 {ECO:0000313|EMBL:ADH98642.1, ECO:0000313|Proteomes:UP000000271};
RN [1] {ECO:0000313|EMBL:ADH98642.1, ECO:0000313|Proteomes:UP000000271}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700615 / DSM 15326 / MLS10
RC {ECO:0000313|Proteomes:UP000000271};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., Stolz J.;
RT "Complete sequence of Bacillus selenitireducens MLS10.";
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP001791; ADH98642.1; -; Genomic_DNA.
DR RefSeq; WP_013172066.1; NC_014219.1.
DR AlphaFoldDB; D6Y138; -.
DR STRING; 439292.Bsel_1125; -.
DR ESTHER; bacie-d6y138; CarbLipBact_2.
DR KEGG; bse:Bsel_1125; -.
DR eggNOG; COG1647; Bacteria.
DR HOGENOM; CLU_076594_0_2_9; -.
DR OrthoDB; 9786110at2; -.
DR Proteomes; UP000000271; Chromosome.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR012354; Esterase_lipase.
DR InterPro; IPR022742; Hydrolase_4.
DR PANTHER; PTHR43798:SF32; MHPC-RELATED PROTEIN; 1.
DR PANTHER; PTHR43798; MONOACYLGLYCEROL LIPASE; 1.
DR Pfam; PF12146; Hydrolase_4; 1.
DR PIRSF; PIRSF017388; Esterase_lipase; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:ADH98642.1}.
FT DOMAIN 4..210
FT /note="Serine aminopeptidase S33"
FT /evidence="ECO:0000259|Pfam:PF12146"
FT ACT_SITE 78
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR017388-1"
FT ACT_SITE 177
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR017388-1"
FT ACT_SITE 207
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR017388-1"
FT BINDING 10
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR017388-2"
FT BINDING 79
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR017388-2"
SQ SEQUENCE 242 AA; 27660 MW; F282A3180A65B8AA CRC64;
MIGCLIIHGF AGTKEEIAEV ETHLRSKNWL VYTPELPGHT GKKEDLASVT YMHWLAMAKV
ALEELFDRCE KVYVVGFSMG GVIAAYLAGR YPVDKLVLIS PAAYYLNPKQ MFEDVKGWFM
EGVRGELDED EYFQMYRNKI RNVPVKATLE FAKLVQKIRP MMEAVDAPTL IVQGQKDGLV
PPKSAEYIFE TISSEDKELY HFPNAKHYIW YSDAKVEMLE RIDQFLETKT GDGQSETTRS
VI
//
