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Database: UniProt
Entry: F7VCJ3_9PROT
LinkDB: F7VCJ3_9PROT
Original site: F7VCJ3_9PROT 
ID   F7VCJ3_9PROT            Unreviewed;       379 AA.
AC   F7VCJ3;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=Esterase/lipase {ECO:0000313|EMBL:GAA08088.1};
GN   ORFNames=ATPR_1092 {ECO:0000313|EMBL:GAA08088.1};
OS   Acetobacter tropicalis NBRC 101654.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Acetobacter.
OX   NCBI_TaxID=749388 {ECO:0000313|EMBL:GAA08088.1, ECO:0000313|Proteomes:UP000004319};
RN   [1] {ECO:0000313|EMBL:GAA08088.1, ECO:0000313|Proteomes:UP000004319}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101654 {ECO:0000313|EMBL:GAA08088.1,
RC   ECO:0000313|Proteomes:UP000004319};
RX   PubMed=21554859; DOI=10.1016/j.bbrc.2011.04.126;
RA   Matsutani M., Hirakawa H., Nishikura M., Soemphol W., Ali I.A.I.,
RA   Yakushi T., Matsushita K.;
RT   "Increased number of Arginine-based salt bridges contributes to the
RT   thermotolerance of thermotolerant acetic acid bacteria, Acetobacter
RT   tropicalis SKU1100.";
RL   Biochem. Biophys. Res. Commun. 409:120-124(2011).
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAA08088.1}.
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DR   EMBL; BABS01000022; GAA08088.1; -; Genomic_DNA.
DR   RefSeq; WP_006558108.1; NZ_BABS01000022.1.
DR   AlphaFoldDB; F7VCJ3; -.
DR   Proteomes; UP000004319; Unassembled WGS sequence.
DR   CDD; cd06849; lipoyl_domain; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   PANTHER; PTHR43798; MONOACYLGLYCEROL LIPASE; 1.
DR   PANTHER; PTHR43798:SF5; MONOACYLGLYCEROL LIPASE ABHD6; 1.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   PRINTS; PR00111; ABHYDROLASE.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF51230; Single hybrid motif; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
PE   4: Predicted;
FT   DOMAIN          5..80
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   379 AA;  40070 MW;  C35AF824B999F163 CRC64;
     MTNTIVPLTM PKFGLAMTEG KLASWLVEPG QSVKQGDELA DIETSKITSG YESPTAGVLR
     KQVAPAGETL PVGALIGVLA DPAVSDADIE AFVTRFQAEQ STGEEAEGAN SADTEPHQVQ
     AGEYSLNVRD VGTGDDLPLL LIHGFGGDIS NWLLTQDALA SGRRVIAFDL PGHGASTKAV
     KDGSLVGLAR AVGDLLEALS IPKVHVMGHS LGGGIALTLL REHPDKVASL SLLAPAGLEK
     AVNMAFITGF IEADRNRAMQ QELEKLVHDK SLIGRKMVDS VMRARRLDGA RDALRTIAAA
     CFPNGEQGDD LRPVLDAAKV PVQLFWGEAD EVLPVAGADN VPSSVKKHIL PGVGHLPQLE
     KASEVNKETE EFLKERVPA
//
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