ID B2FL48_STRMK Unreviewed; 372 AA.
AC B2FL48;
DT 10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT 10-JUN-2008, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=Exported alpha/beta hydrolase fold protein {ECO:0000313|EMBL:CAQ45281.1};
GN OrderedLocusNames=Smlt1759 {ECO:0000313|EMBL:CAQ45281.1};
OS Stenotrophomonas maltophilia (strain K279a).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX NCBI_TaxID=522373 {ECO:0000313|EMBL:CAQ45281.1, ECO:0000313|Proteomes:UP000008840};
RN [1] {ECO:0000313|EMBL:CAQ45281.1, ECO:0000313|Proteomes:UP000008840}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K279a {ECO:0000313|EMBL:CAQ45281.1,
RC ECO:0000313|Proteomes:UP000008840};
RX PubMed=18419807; DOI=10.1186/gb-2008-9-4-r74;
RA Crossman L.C., Gould V.C., Dow J.M., Vernikos G.S., Okazaki A.,
RA Sebaihia M., Saunders D., Arrowsmith C., Carver T., Peters N., Adlem E.,
RA Kerhornou A., Lord A., Murphy L., Seeger K., Squares R., Rutter S.,
RA Quail M.A., Rajandream M.A., Harris D., Churcher C., Bentley S.D.,
RA Parkhill J., Thomson N.R., Avison M.B.;
RT "The complete genome, comparative and functional analysis of
RT Stenotrophomonas maltophilia reveals an organism heavily shielded by drug
RT resistance determinants.";
RL Genome Biol. 9:R74.1-R74.13(2008).
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DR EMBL; AM743169; CAQ45281.1; -; Genomic_DNA.
DR RefSeq; WP_005409039.1; NC_010943.1.
DR AlphaFoldDB; B2FL48; -.
DR EnsemblBacteria; CAQ45281; CAQ45281; Smlt1759.
DR GeneID; 61465595; -.
DR KEGG; sml:Smlt1759; -.
DR eggNOG; COG1073; Bacteria.
DR HOGENOM; CLU_721432_0_0_6; -.
DR Proteomes; UP000008840; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR PANTHER; PTHR43194; HYDROLASE ALPHA/BETA FOLD FAMILY; 1.
DR PANTHER; PTHR43194:SF5; PIMELOYL-[ACYL-CARRIER PROTEIN] METHYL ESTER ESTERASE; 1.
DR Pfam; PF12697; Abhydrolase_6; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:CAQ45281.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008840};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..372
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002777875"
FT DOMAIN 119..332
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF12697"
SQ SEQUENCE 372 AA; 40282 MW; 62DF16DD91B568C3 CRC64;
MKRLLLLLLA CAGLWLAACS SSINASSTSL ADRLIAPGGV STLLDRPRIA AAIAELPNRH
GFAPGRDGVP IFWRVFDPGD YGARYHYLPQ RHENGLPLDT GLSLAVPQPF RAQAPRGTVV
LLHGWMMNGD SMLPWSLQLA ESGYRVVTLD LRNHGQSGTG PSGYGTYESD DVVDVIGELR
ARGEVTGPLY LFGVSYGAAT AVFTADKLGD QVEGVVAMES FANAGVAIRT MIPHLMGLQP
EGLKAQAMAS YARWRYGGQD INQVIAAASR RIDVDLDRVD VARALADTRA CVLLLHGQGD
QHIPVSQGRE LAQANPRAHY IEMRGEDHIT LPLRLDLLAG VVDDWMARDE HHPKSACPAP
QLPAQAEWLA HR
//
