ID A6Q9G0_SULNB Unreviewed; 1153 AA.
AC A6Q9G0;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE SubName: Full=2-acyl-glycerophospho-ethanolamine acyltransferase acyl-acyl-carrier protein synthetase {ECO:0000313|EMBL:BAF72119.1};
DE EC=2.3.1.40 {ECO:0000313|EMBL:BAF72119.1};
DE EC=6.2.1.20 {ECO:0000313|EMBL:BAF72119.1};
GN OrderedLocusNames=SUN_1164 {ECO:0000313|EMBL:BAF72119.1};
OS Sulfurovum sp. (strain NBC37-1).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Sulfurovaceae; Sulfurovum.
OX NCBI_TaxID=387093 {ECO:0000313|EMBL:BAF72119.1, ECO:0000313|Proteomes:UP000006378};
RN [1] {ECO:0000313|EMBL:BAF72119.1, ECO:0000313|Proteomes:UP000006378}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBC37-1 {ECO:0000313|EMBL:BAF72119.1,
RC ECO:0000313|Proteomes:UP000006378};
RX PubMed=17615243; DOI=10.1073/pnas.0700687104;
RA Nakagawa S., Takaki Y., Shimamura S., Reysenbach A.-L., Takai K.,
RA Horikoshi K.;
RT "Deep-sea vent epsilon-proteobacterial genomes provide insights into
RT emergence of pathogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12146-12150(2007).
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DR EMBL; AP009179; BAF72119.1; -; Genomic_DNA.
DR RefSeq; WP_011980852.1; NC_009663.1.
DR AlphaFoldDB; A6Q9G0; -.
DR STRING; 387093.SUN_1164; -.
DR KEGG; sun:SUN_1164; -.
DR eggNOG; COG0204; Bacteria.
DR eggNOG; COG0318; Bacteria.
DR eggNOG; COG2814; Bacteria.
DR HOGENOM; CLU_008489_1_0_7; -.
DR OrthoDB; 9799237at2; -.
DR Proteomes; UP000006378; 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 GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008922; F:long-chain fatty acid [acyl-carrier-protein] ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR CDD; cd07989; LPLAT_AGPAT-like; 1.
DR CDD; cd06173; MFS_MefA_like; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR PANTHER; PTHR24096:SF149; 4-COUMARATE--COA LIGASE 1-RELATED; 1.
DR PANTHER; PTHR24096; LONG-CHAIN-FATTY-ACID--COA LIGASE; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF07690; MFS_1; 1.
DR SMART; SM00563; PlsC; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
DR SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000313|EMBL:BAF72119.1};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000313|EMBL:BAF72119.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Transferase {ECO:0000313|EMBL:BAF72119.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 44..66
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 78..95
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 101..120
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 176..197
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 239..262
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 274..295
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 302..322
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 328..351
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 371..390
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 449..561
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 1153 AA; 126165 MW; B6B3BC6021B4A63E CRC64;
MKHLFKISGF TPYIFIILLN AMTDLGHKII LQNTIFKAYD GSELIVLTAI VNALILLPFI
FLFSPAGFIS DKYPKVKVVE YASAAAIGIT TLILLSYYMG WFWAAFGLTF ILAAQSAIYS
PAKYGLIKEM TGNENLAPAN ALVQSVTIVS ILAGAVIYSV FFESLLQDRS VIPSEILTYI
APVGYMLIGA SILEYILARR LVKKVKPVAI DESMAFEPQA YKDLHYLKEN LSIIRQNSAV
WLSILGLSII WGVSQVVLAI FGEYLKATLG VTDTVTAQGL LALSGLGMIA GSMVVGRVSR
NYIETGIIPL GALGVTVMLF MMPTLSSLWT LGSALFLFGF SAGLFVVPLN AIIQFAAPSP
ILGKVLAGNN FMQNVSMFGF LILTALFGYF NLDAVGLFYI IATVSLLGMG YTFIKLPQSL
VRYVVRMIIG FKYRLHVDGL RNIPADKGVL LLGNHVSFLD WAILQMAYPK QIRFVMERSY
YDKWYLKPFL DFFGVIPISS RGSKGALALV TAALNRGETV ALFPEGHLSR NGHLGTFQRG
FEVAAKDAED AVIIPFYLRG LWEDNFSYAS NKMKRNTNKD ISVTFGEELN VHSGASEVKK
AVFDLSVKSW KTYTQTLPSL QKAWIRAAKE QGGKLCIADS TGVEVNGDRF VTGTLMIASA
LKPILKESQN IGLLLPTSVA GSMANMAILT LGKTIVNLNY SSGEASLLHA LKIANITKVV
ASKQFVTKLK AKGFDLGEVL SKVEVIYLED IKAKMGKVKG VFTLGLVKLL PACLLSLFYI
KDADLEETAA ILFSSGSEGT PKGIELSHKN MMGNIKQAIT LINPKDDDVM LGTLPIFHSF
GLTVTTLLPL IEGLPVVCHP DPTDGFGIGK MAAKYEATML FATATFFRLY TRNKKLHPLM
FKDLRMVIAG AEKLPQEIRD EFKKKFGHDI YEGYGATETT PVASINIPDV LMQDSWKPQI
GHKIGTVGLP VPGSSFKIVD PESFEELPTG EEGMILIGGT QIMKGYIGDP EKTASVIKEI
DGIRWYVTGD KGRIDEDGFL TIVDRYSRFA KVAGEMVSLG LVEFEIATVL GENDQIAVAA
LPDAKKGEKL VLLLEGEMEI ETLKEKIKSL EMNPLFVPGE YYKVEELPKL GTGKADFKGA
KSLAQKMSEN RKG
//
