ID A2SDQ0_METPP Unreviewed; 389 AA.
AC A2SDQ0;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE SubName: Full=Acyltransferase-like protein {ECO:0000313|EMBL:ABM93689.1};
GN OrderedLocusNames=Mpe_A0727 {ECO:0000313|EMBL:ABM93689.1};
OS Methylibium petroleiphilum (strain ATCC BAA-1232 / LMG 22953 / PM1).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Methylibium.
OX NCBI_TaxID=420662 {ECO:0000313|EMBL:ABM93689.1, ECO:0000313|Proteomes:UP000000366};
RN [1] {ECO:0000313|EMBL:ABM93689.1, ECO:0000313|Proteomes:UP000000366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1232 / LMG 22953 / PM1
RC {ECO:0000313|Proteomes:UP000000366};
RX PubMed=17158667; DOI=10.1128/JB.01259-06;
RA Kane S.R., Chakicherla A.Y., Chain P.S.G., Schmidt R., Shin M.W.,
RA Legler T.C., Scow K.M., Larimer F.W., Lucas S.M., Richardson P.M.,
RA Hristova K.R.;
RT "Whole-genome analysis of the methyl tert-butyl ether-degrading beta-
RT proteobacterium Methylibium petroleiphilum PM1.";
RL J. Bacteriol. 189:1931-1945(2007).
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DR EMBL; CP000555; ABM93689.1; -; Genomic_DNA.
DR RefSeq; WP_011828327.1; NC_008825.1.
DR AlphaFoldDB; A2SDQ0; -.
DR STRING; 420662.Mpe_A0727; -.
DR KEGG; mpt:Mpe_A0727; -.
DR eggNOG; COG1835; Bacteria.
DR HOGENOM; CLU_005679_2_0_4; -.
DR Proteomes; UP000000366; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR InterPro; IPR002656; Acyl_transf_3_dom.
DR PANTHER; PTHR23028; ACETYLTRANSFERASE; 1.
DR PANTHER; PTHR23028:SF53; O-ACYLTRANSFERASE HOMOLOG; 1.
DR Pfam; PF01757; Acyl_transf_3; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000313|EMBL:ABM93689.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000000366};
KW Transferase {ECO:0000313|EMBL:ABM93689.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 28..47
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 100..118
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 151..177
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 184..201
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 235..254
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 260..282
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 303..324
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 330..356
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 23..352
FT /note="Acyltransferase 3"
FT /evidence="ECO:0000259|Pfam:PF01757"
SQ SEQUENCE 389 AA; 42380 MW; D374A44E7581DFA9 CRC64;
MNWLVHRFEL ARGGQADNVR PMEGLRGFAV LLVFLTHYTG MVEPWIAGST ETVRIASGLR
HAGHAGVDLF FVLSGYLIYG SLMKRPQPFI GFMRRRVARI YPAFIVVFVA YVLLSFAFPS
ESRIPADPAE AALYLVQNLL LLPGLLPIDP LITVAWSLSY EMLFYLVTPA FIAVLGLRQR
SRRWRVVFLL VLAGALALYG ALQGGPIRLM MFVAGMLLHE ALAHRLKAAS ASPPGALAGV
LALLAGLGAV LLPGEGHAAQ AAQVCILFVA WPLLCLVCFR APSAWLPRAF SWTPLRWLGN
MSYSYYLLHG LVLNAGFLLL AQVLPPAGQG AWVFWGLLPV LFGLTLLPTA VLFLLVERPY
SLAPSSKAAR IGGVPQVRTG ASPTERRSD
//
