ID Q98BS2_RHILO Unreviewed; 1137 AA.
AC Q98BS2;
DT 01-OCT-2001, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2001, sequence version 1.
DT 27-MAR-2024, entry version 108.
DE SubName: Full=2-acylglycerophosphoethanolamine acyltransferase {ECO:0000313|EMBL:BAB51900.1};
GN OrderedLocusNames=mlr5451 {ECO:0000313|EMBL:BAB51900.1};
OS Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS (Mesorhizobium loti (strain MAFF 303099)).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Mesorhizobium.
OX NCBI_TaxID=266835 {ECO:0000313|EMBL:BAB51900.1, ECO:0000313|Proteomes:UP000000552};
RN [1] {ECO:0000313|EMBL:BAB51900.1, ECO:0000313|Proteomes:UP000000552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 29417 / CECT 9101 / MAFF 303099
RC {ECO:0000313|Proteomes:UP000000552};
RX PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT Mesorhizobium loti.";
RL DNA Res. 7:331-338(2000).
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DR EMBL; BA000012; BAB51900.1; -; Genomic_DNA.
DR AlphaFoldDB; Q98BS2; -.
DR KEGG; mlo:mlr5451; -.
DR eggNOG; COG0204; Bacteria.
DR eggNOG; COG0318; Bacteria.
DR eggNOG; COG2814; Bacteria.
DR HOGENOM; CLU_008489_1_0_5; -.
DR Proteomes; UP000000552; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; PTHR43201; ACYL-COA SYNTHETASE; 1.
DR PANTHER; PTHR43201:SF5; MEDIUM-CHAIN ACYL-COA LIGASE ACSF2, MITOCHONDRIAL; 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:BAB51900.1};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Transferase {ECO:0000313|EMBL:BAB51900.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 52..75
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 113..132
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 144..165
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 171..190
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 230..252
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 264..283
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 290..313
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 333..358
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 370..392
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 454..564
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 1137 AA; 121557 MW; 0BEBA18BC058F8C4 CRC64;
MEIAMNTHLM LSRRFAPLFW TQFLSAFNDN FLKNTLVFLI LFTLAADQAA SLVTLAGAVF
MAPFLLLSAL GGEIADRFDK ALIARRLKFA EIAAAAVSVA GIALSSIPVL MTALLMFGII
SALFGPIKYG ILPDHLERKE LPKANAWIES ATFAAILGGT IAGGVVSADG IGVTVFGPIM
MALAVGCWFV SRYIPPTGSA APGLVIDKNI FRSTWRQVSE LRTDTRIWRA GLMTSWFWLI
GAIVLSILPT LIKDSLGGNE IAVTVYLAVF AVSIAIGSAI AAWMSQGRIV LLPAPVGTAL
LALFGLHLAW TIWSMQPSPK AQTLALFFAG PNTIRVAIDL AAMAIASAFL VVPTFAAVQA
WSPEARRARV VAAVSIVNAG FMTVGGIVVA VIQTKVSTGG ILFGLAVANA VAAWLMLKFL
PTNAFRDFVS ILFRAFLRLE VEGMENLKAA GKAPILALNH VSFLDGPLAL TLTDEEPVFA
IDYAIAQAWW MKPFMKLARA LPLNPAKPMS TRTLIKIVQG GDPLVIFPEG RITVTGGLMK
VYDGAAMVAD KTGSMVVPIR IDGLEKSPFS RLTSQHVRRR LFPKVKVTIL EPVKLQVPPE
LKGRKRRAAA GSALYQVMSD LVFRTQDIDK TVLEKIILTA NERGMKRLAV QDPVTGSLSY
GKLLTAAAVL GEKFQNLYAG QQTLGIMLPN ANGSCATLLG VMSAGKVPAM INFTAGAANI
LSACKAAEVR TVLTSRAFVE QAKLGAVVEE IGRSVDIVWL DDLRATMGLK DKLLGLLRKS
TPRAPRKPDD PAVILFTSGS EGTPKGVVLT HRNILANAAQ AASRIDFHSG DKVFNVLPIF
HSFGMTAGTV LPLISGVPVY FYPSPLHYRI VPELIYASNA TIIFGTDTFL SGYARTAHPY
DFRSIRYCFA GAEPVKAATR MTYMEKFGVR ILEGYGVTEA APVIAINTPM YNKSGSVGKI
MPGMEYRLDP VPGVDEGGRL YVRGPNVMAG YLRAEKPGAL EPLEDGWHDT GDVVSVDEGG
FITIRGRAKR FAKIGGEMIS LAAVEALAGE VWKGSLSAVA SVPDARKGEK LILITEAPGA
TRAELLAFAK ANGAMDLMVP AEVRVVPKVP VLGSGKLDFA GVTKLVRDAP VAKVEAA
//
