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Database: UniProt
Entry: A0A061LVY3_9MICO
LinkDB: A0A061LVY3_9MICO
Original site: A0A061LVY3_9MICO 
ID   A0A061LVY3_9MICO        Unreviewed;       645 AA.
AC   A0A061LVY3;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=Lipopolysaccharide modification acyltransferase {ECO:0000313|EMBL:EYT52083.1};
GN   ORFNames=H490_0113925 {ECO:0000313|EMBL:EYT52083.1};
OS   Leucobacter sp. UCD-THU.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Leucobacter.
OX   NCBI_TaxID=1292023 {ECO:0000313|EMBL:EYT52083.1, ECO:0000313|Proteomes:UP000026917};
RN   [1] {ECO:0000313|EMBL:EYT52083.1, ECO:0000313|Proteomes:UP000026917}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCD-THU {ECO:0000313|EMBL:EYT52083.1,
RC   ECO:0000313|Proteomes:UP000026917};
RX   PubMed=23792744; DOI=10.1128/genomeA.00325-13;
RA   Holland-Moritz H.E., Bevans D.R., Lang J.M., Darling A.E., Eisen J.A.,
RA   Coil D.A.;
RT   "Draft Genome Sequence of Leucobacter sp. Strain UCD-THU (Phylum
RT   Actinobacteria).";
RL   Genome Announc. 1:S69-S82(2013).
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EYT52083.1}.
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DR   EMBL; APJM01000027; EYT52083.1; -; Genomic_DNA.
DR   RefSeq; WP_017885298.1; NZ_KB714605.1.
DR   AlphaFoldDB; A0A061LVY3; -.
DR   STRING; 1292023.H490_0113925; -.
DR   HOGENOM; CLU_005679_11_2_11; -.
DR   OrthoDB; 3404679at2; -.
DR   Proteomes; UP000026917; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR   CDD; cd01840; SGNH_hydrolase_yrhL_like; 1.
DR   Gene3D; 3.40.50.1110; SGNH hydrolase; 1.
DR   InterPro; IPR002656; Acyl_transf_3_dom.
DR   InterPro; IPR036514; SGNH_hydro_sf.
DR   PANTHER; PTHR23028; ACETYLTRANSFERASE; 1.
DR   PANTHER; PTHR23028:SF53; O-ACYLTRANSFERASE HOMOLOG; 1.
DR   Pfam; PF01757; Acyl_transf_3; 1.
DR   SUPFAM; SSF52266; SGNH hydrolase; 1.
PE   4: Predicted;
KW   Acyltransferase {ECO:0000313|EMBL:EYT52083.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000026917};
KW   Transferase {ECO:0000313|EMBL:EYT52083.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        41..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        83..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        178..197
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        209..228
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        240..258
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        270..289
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        310..328
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        334..354
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        382..403
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          17..351
FT                   /note="Acyltransferase 3"
FT                   /evidence="ECO:0000259|Pfam:PF01757"
FT   REGION          421..480
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        426..447
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   645 AA;  67684 MW;  F422DF1000D9D1DA CRC64;
     MPQPQTRPAP RTARFGGLDG LRAIAVGLVL CYHLFPPLLP GGFLGVDVFF VMSGFLITSL
     LLREYELGGR IRLGAFWRRR ARRLLPALGL VLLVSTALAL PVGGDLLVGI GQQIAGAAFF
     VSNWVFIANG ADYFARDTPE LFRNMWSLAI EEQFYIVLPL VVLLLVRLRS RPSRAIPLAA
     LGLASAALMF ELSRAGVDPT RIYFGSDSHT FGLLLGAAMA AVLHRPEASE VLNPGPLRQL
     AAAAAALAGL AVLGWLAATL SEGSPASFQW GFQLATAAAL LVVWAVTRPG AWVGRALDAP
     PLRWVGERSY GIYLWHWPLL LICAGALGPD LEWLVAPLAL AATVLAAALS YRFVEQPVRR
     FGLRRSLRML VRVGDHTPRR RFVAIGLAAV VAVAAPAAVV AIVTAPQQSS AAEAIARGQE
     ALERSRAAQQ ADEGRSGRGE RSEGASETGK TENPAPGKGS GGGAKEQSAE PAPLSPDGRD
     LVAVGDSVML ASLPELEAAY PGISIDAAVS RGMGTGAEIV TGLSSQGSLR GVLVVGLGTN
     GPVQAEDLDT IRASAGTRPV VLVNAHADRD WIPSVNQLLT DYAAAHRGVV VADWTGSVTG
     VPDALAGDDI HPNPSGGEIY AGSVQRALEE LQSPGEGIGF GLPRR
//
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