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Database: UniProt
Entry: F8C286_THEGP
LinkDB: F8C286_THEGP
Original site: F8C286_THEGP 
ID   F8C286_THEGP            Unreviewed;       508 AA.
AC   F8C286;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   SubName: Full=Acyl-(Acyl-carrier-protein)--phospholipid O-acyltransferase {ECO:0000313|EMBL:AEH23344.1};
DE            EC=2.3.1.40 {ECO:0000313|EMBL:AEH23344.1};
GN   OrderedLocusNames=TOPB45_1263 {ECO:0000313|EMBL:AEH23344.1};
OS   Thermodesulfobacterium geofontis (strain OPF15).
OC   Bacteria; Thermodesulfobacteriota; Thermodesulfobacteria;
OC   Thermodesulfobacteriales; Thermodesulfobacteriaceae;
OC   Thermodesulfobacterium.
OX   NCBI_TaxID=795359 {ECO:0000313|EMBL:AEH23344.1, ECO:0000313|Proteomes:UP000006583};
RN   [1] {ECO:0000313|EMBL:AEH23344.1, ECO:0000313|Proteomes:UP000006583}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OPF15 {ECO:0000313|EMBL:AEH23344.1,
RC   ECO:0000313|Proteomes:UP000006583};
RX   PubMed=23580711; DOI=10.1128/genomea.00162-13;
RA   Elkins J.G., Hamilton-Brehm S.D., Lucas S., Han J., Lapidus A., Cheng J.F.,
RA   Goodwin L.A., Pitluck S., Peters L., Mikhailova N., Davenport K.W.,
RA   Detter J.C., Han C.S., Tapia R., Land M.L., Hauser L., Kyrpides N.C.,
RA   Ivanova N.N., Pagani I., Bruce D., Woyke T., Cottingham R.W.;
RT   "Complete genome sequence of the hyperthermophilic sulfate-reducing
RT   bacterium Thermodesulfobacterium geofontis OPF15T.";
RL   Genome Announc. 1:E0016213-E0016213(2013).
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DR   EMBL; CP002829; AEH23344.1; -; Genomic_DNA.
DR   AlphaFoldDB; F8C286; -.
DR   STRING; 795359.TOPB45_1263; -.
DR   KEGG; top:TOPB45_1263; -.
DR   PATRIC; fig|795359.3.peg.1284; -.
DR   eggNOG; COG0318; Bacteria.
DR   HOGENOM; CLU_000022_59_8_0; -.
DR   OrthoDB; 9799237at2; -.
DR   Proteomes; UP000006583; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008779; F:acyl-[acyl-carrier-protein]-phospholipid O-acyltransferase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR   InterPro; IPR025110; AMP-bd_C.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR   InterPro; IPR042099; ANL_N_sf.
DR   PANTHER; PTHR43201; ACYL-COA SYNTHETASE; 1.
DR   PANTHER; PTHR43201:SF5; MEDIUM-CHAIN ACYL-COA LIGASE ACSF2, MITOCHONDRIAL; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
PE   4: Predicted;
KW   Acyltransferase {ECO:0000313|EMBL:AEH23344.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006583};
KW   Transferase {ECO:0000313|EMBL:AEH23344.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        52..73
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          10..368
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          428..490
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
SQ   SEQUENCE   508 AA;  57817 MW;  67DE53A4E1DE8BA8 CRC64;
     MQLHEKFIYT AKTYSNKIAI VDKLIEKRFT YQQTLIASLI FSRKIKRFRE RLIGIMLPNS
     AVAIFTVIGT LMAEKIPVML NYSTGAEYNL KYAREKCNFR TVITSQKLLE RVNCPILENM
     EFVENWIEEI DLKEKVIASF ISKLPLKFLM SYCGVDGDPE KTAVILFTSG TEKDPKAVEL
     SHKNILSNIE GFSQMAKLTE KDVIMSILPY FHVFGLTVNL WTPLYHGMTL ITYPTPLDYQ
     KICQIVKGEK PTLMAATPSF WWGYLKKSEP GTFDSLRLMI SGADKCPQPL RDTFWEKHKK
     LLLEGYGTTE TSPVISVNMP DAYKPGSVGK PLPNLEVMIE NYETGEKCGP NEIGRILVRG
     PNVMKGYFND LEETSMRIRH GWYDTGDMGY LDEDGYLWHV GRLKRFVKIG GEMISLVKVE
     DELEKVLPKN VECCVVEIPD EVKGAKIVAV VSQKIDEKAI LKQLAKVLPN LAIPKHFVVM
     EDLPKMGSGK IDFRKVQELI MEKLGLKV
//
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