ID D7K800_9BACE Unreviewed; 1285 AA.
AC D7K800;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Putative acyltransferase {ECO:0000313|EMBL:EFI36886.1};
GN ORFNames=HMPREF9010_02512 {ECO:0000313|EMBL:EFI36886.1};
OS Bacteroides sp. 3_1_23.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=457390 {ECO:0000313|EMBL:EFI36886.1, ECO:0000313|Proteomes:UP000003808};
RN [1] {ECO:0000313|EMBL:EFI36886.1, ECO:0000313|Proteomes:UP000003808}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3_1_23 {ECO:0000313|EMBL:EFI36886.1,
RC ECO:0000313|Proteomes:UP000003808};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Earl A., Feldgarden M., Gevers D., Young S.K., Zeng Q.,
RA Koehrsen M., Alvarado L., Berlin A., Bochicchio J., Borenstein D.,
RA Chapman S.B., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D.,
RA Larson L., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J.,
RA Yandava C., Strauss J., Daigneault M., McDonald J., Ambrose C.E.,
RA Allen-Vercoe E., Haas B., Nusbaum C., Birren B.;
RT "The Genome Sequence of Bacteroides sp. strain 3_1_23.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; GG774955; EFI36886.1; -; Genomic_DNA.
DR RefSeq; WP_008650508.1; NZ_GG774955.1.
DR HOGENOM; CLU_003055_0_0_10; -.
DR Proteomes; UP000003808; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR CDD; cd07989; LPLAT_AGPAT-like; 1.
DR Gene3D; 1.20.1640.10; Multidrug efflux transporter AcrB transmembrane domain; 2.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR041698; Methyltransf_25.
DR InterPro; IPR004869; MMPL_dom.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR33406; MEMBRANE PROTEIN MJ1562-RELATED; 1.
DR PANTHER; PTHR33406:SF2; MEMBRANE PROTEIN SCO6666-RELATED; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR Pfam; PF13649; Methyltransf_25; 1.
DR Pfam; PF03176; MMPL; 1.
DR SMART; SM00563; PlsC; 1.
DR SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
DR SUPFAM; SSF82866; Multidrug efflux transporter AcrB transmembrane domain; 2.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000313|EMBL:EFI36886.1};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transferase {ECO:0000313|EMBL:EFI36886.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 17..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 273..291
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 297..318
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 325..346
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 361..381
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 390..409
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 441..457
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 664..683
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 689..709
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 716..737
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 757..775
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 787..810
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 830..851
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 898..1007
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 1285 AA; 147074 MW; B94595D6F3B03810 CRC64;
MTQFFIGLYD YFERHKILFY LSLISCVLLM GFFALQVRFE ENITQFFPDT KDSQNTIKVF
DNLKIKDKII IMLSSADTCH RVEPDSLIEA AGQLQQNLTE KAGGKLIKGI FAQVDQSLIQ
GATDFVYEHL PLFLTDTDYQ RFDSLLTDKG IQATMQKNYT NLLSPAGIAL RNYILRDPLG
LGSETLKHLQ DFQLEANYEI YDEHIFSKDG STLLMFITPV FSTGSTGKND ELIKILEEEL
KHVQEKSPTI RAEYFGGPSV GVYNARQIKK DTILTSSLAL LIIIVFISLV FKRKRSIPLI
ITPVLFGGLF ALFLIFFIKG SISAIAVGAG SAVMGIALSY SIHMLAHQNH VSTVQQLIKE
IAYPLTVGSF TTIGAFLGLI FTSSDLLRDF GLFASLALVG TTLFCLIYLP HFLKGQADVK
QGRILRIIEK INAYSYEKNK WLVGGILLIT VICLFTSQKV GFNNDMMSLN YEPRHLQQSE
EKLLQLFDND EKTVLFVSVG KDMNQATEIY ATTNQKLSAL KEQGLIKEYA SASQFLISPQ
EQQKRLKKWK DYWTDEKQQQ VREQLETVAT EYRFRPGSFE PFYQWMNQPF GEYHYTAQED
DLSGKLLNEW QTSADSITML ISQIRISEPN KEAVYQNFNK DPNVVIFDRS YFANKWVSAI
NDDFYLILYI SSFLIFFALW FSYGRIELTL MSFLPMLISW VIILGLMGIL GIEFNIINII
LSTFIFGIGD DFSIFIMDGL QNKYRTGQKV LNSHKTAIFF SAFTTVVGMG ALVFAKHPAL
QSISLISILG MIAVVLVAYT IQPLIFRFFI AGPASKGLPP YTLIGLIRTV LLFLLFFIGC
IVLRILIILL YPVPVRKSSK QRLVCRLIQI TCKGILLLAT AVKKEHINKA NERFRHPAII
IANHQSFIDI LVLLSLSSKI LMVTNHWVWH SPFFGAIIRY VDFYYIGEGY EQYMERMRKK
VKEGYSIAIF PEGTRTYNGK MKRFHKGAFY LAEALKLDIL PILLYGNNKI IAKAQPFNIR
KGIIYTEILP RIPLDDLSFG STYQERTKRI SAYMKEVYAR ICREQNTTDN PAFYEALIQN
YIYKGPVVEW YIRIKVKMEK NYRLFNRLIP VQGQITDIGC GFGPLCYMLS LLSEDREILG
IDYDEDKIAL AQHGWLRNEH LQFKHGNALE YPLPESDVFI LNDMLHYMSY EHQQTLLLKC
AGRLRSQGMI IIRDGNSANA SKHRLTRFTE LLSTRIFNFN RTTGELYFTT ETQLREIAVA
CGMAVEIIPN DKYTSNTIYI FRKPN
//
