ID   A8F2A6_RICM5            Unreviewed;      1148 AA.
AC   A8F2A6;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   27-MAR-2024, entry version 74.
DE   SubName: Full=2-acylglycerophosphoethanolamine acyltransferase {ECO:0000313|EMBL:ABV85042.1};
GN   Name=aas {ECO:0000313|EMBL:ABV85042.1};
GN   OrderedLocusNames=RMA_0988 {ECO:0000313|EMBL:ABV85042.1};
OS   Rickettsia massiliae (strain Mtu5).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=416276 {ECO:0000313|EMBL:ABV85042.1, ECO:0000313|Proteomes:UP000001311};
RN   [1] {ECO:0000313|EMBL:ABV85042.1, ECO:0000313|Proteomes:UP000001311}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mtu5 {ECO:0000313|Proteomes:UP000001311};
RX   PubMed=17916642; DOI=10.1101/gr.6742107;
RA   Blanc G., Ogata H., Robert C., Audic S., Claverie J.-M., Raoult D.;
RT   "Lateral gene transfer between obligate intracellular bacteria: evidence
RT   from the Rickettsia massiliae genome.";
RL   Genome Res. 17:1657-1664(2007).
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004429}.
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DR   EMBL; CP000683; ABV85042.1; -; Genomic_DNA.
DR   AlphaFoldDB; A8F2A6; -.
DR   KEGG; rms:RMA_0988; -.
DR   HOGENOM; CLU_008489_1_0_5; -.
DR   Proteomes; UP000001311; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016746; F:acyltransferase activity; 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; 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; 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:ABV85042.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transferase {ECO:0000313|EMBL:ABV85042.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        61..81
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        93..112
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        118..139
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        151..176
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        182..200
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        234..257
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        269..288
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        300..318
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        346..368
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        380..405
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        411..431
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          471..581
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
SQ   SEQUENCE   1148 AA;  129571 MW;  882C8FA02D61D49D CRC64;
     MAFKIFYIMD TNKLYLFKDR RFLPNFIVQL CGCLNDNILK NALVILITYG ISGALSKYNN
     LLVLIANATF VLPFIIFASI AGQIADKYER ANLIKIIKIC EIGIIAFAIY GFHHNNLLIL
     FCSICLMGIH STFFGPIKYS VLPDHLNKDE LLGANGFVEA GTFIGIFIGT IIGSYYTISN
     NFIIYSLITI AFLGFITSLF SPKSKNANRD IKINFNIIDE SINMIKYAKA KKQIYLAILG
     ISWFWFIGAA IISQIPLLAK ITFKADENVA NLFLAVFSLG VGVGSFLCSK IFEDEITVKY
     LFISALGISI FGIDLFFASR ISSVNYEPTQ LKSILVFLSK RHNWRIVIDL LFLAAIGGLY
     IVPLFAILQH YANPAHRSRI IAVNNLINSI FMVGSTIILS LLFYLNFTIP WIILFISLAN
     IIVTIHIYRL IPEVKIIPFK LLRRIFQICF DLMYKVEVKG FENFQKAGKK VVVVANHISY
     LDPPLIATYL REEMTFAISP DIQKIWWIKP FLRMARTLPV DPSNPMAIKT LVKEIQKDQK
     VAIFPEGRIS VTGSLMKIYE GPGMIADKAG ATILPVRIDG TQFTHLSKLK NILKRKIFPK
     ITITVLPPVK FANMDATNNQ ARRSYISRTL YDIMADMMFE SSDYKNTVFS SLIEAAKIHG
     FKKKIVDDFE NNAVTYRDLI LKSFILGDLI KKNNIFGRNL GLMLPNTTNM LMTFYAMQSS
     GYVPAIINWS NGISTIINSC KLAQIKVVYT SKQFIEKANL HELITNLLDF GIKIIYLEDF
     KNQIGTALKL KAKIGSYCAQ TYYNYFCRNR DDEKAAVIIF TSGTEGEPKA VLLSHRNLQT
     NRYQITAKVP FSPEDIVFNA LPLFHCFGLS GAIITTLNGI KLFLYPSPLN YRSIPEVIYD
     IGATILISTD TFLNGYANYA HPYDFYSLRY IFAGSEKLKE STRQFWLNKY GIRIFEGYGI
     TEASPIIACN TPMHNKAGTV GRLLPKIDYK LEKVEGINEV GRLFIKGPNI MLGYLDLEGH
     LTYKEWYDTG DIVKIDSEGY ITILGRLKRF AKIAEEMISL TKIEELASEI DPDSLHAAIS
     IPDKTHGEKI ILLTTGSDIN RENFADAVSK AQISLLHLPK VIITDSGIPL LTSGKIDYLE
     IMKNVDRF
//