ID F9N3R4_9FIRM Unreviewed; 367 AA.
AC F9N3R4;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Acyltransferase {ECO:0000313|EMBL:EGS39882.1};
GN ORFNames=HMPREF9200_1522 {ECO:0000313|EMBL:EGS39882.1};
OS Veillonella sp. oral taxon 780 str. F0422.
OC Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC Veillonella.
OX NCBI_TaxID=944564 {ECO:0000313|EMBL:EGS39882.1, ECO:0000313|Proteomes:UP000010295};
RN [1] {ECO:0000313|EMBL:EGS39882.1, ECO:0000313|Proteomes:UP000010295}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0422 {ECO:0000313|EMBL:EGS39882.1,
RC ECO:0000313|Proteomes:UP000010295};
RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Nelson K.E.;
RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the acyltransferase 3 family.
CC {ECO:0000256|ARBA:ARBA00007400}.
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:EGS39882.1}.
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DR EMBL; AFUJ01000005; EGS39882.1; -; Genomic_DNA.
DR RefSeq; WP_009352830.1; NZ_AFUJ01000005.1.
DR AlphaFoldDB; F9N3R4; -.
DR eggNOG; COG1835; Bacteria.
DR OrthoDB; 1661854at2; -.
DR Proteomes; UP000010295; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; PTHR40074; O-ACETYLTRANSFERASE WECH; 1.
DR PANTHER; PTHR40074:SF3; POLY-BETA-1,6-N-ACETYL-D-GLUCOSAMINE EXPORT PROTEIN-RELATED; 1.
DR Pfam; PF01757; Acyl_transf_3; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000313|EMBL:EGS39882.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000010295};
KW Transferase {ECO:0000313|EMBL:EGS39882.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 37..63
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 156..175
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 195..213
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 225..250
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 270..289
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 301..319
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 325..349
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 7..348
FT /note="Acyltransferase 3"
FT /evidence="ECO:0000259|Pfam:PF01757"
SQ SEQUENCE 367 AA; 41972 MW; BCAC184BA95F8DF8 CRC64;
MRKPAIPAIT YMRGLCMLGV IGIHVGSYAL ANPTINIHLL GLLEIVSRFT VPAFFFLSAF
GLFYHTSVED DFSYSDFLRR RTQVVLYPYI VWTILYTAYN AVLAHNAWGL MPHVLGLTLL
FGNGMYHLYF LVILLWFYTL MPLWRWALRS ILKAPIVLMT ILFFVQMAVN YWSSYMAGSV
QFSQEWLQYI FSMRLNYFVG FYIWIFLLGG LLAERFDAML EWIDAHGFGI TVGFILSLVA
MLGSYYYVMA EWGYTRLEAI YTVHQLSPQG LVYTGMGCIF FVWAFTVSSM SDIVETFWTE
LGNASYGIYL VHPFMLILLD KVLQIGGLGY TTTIVVLMYV SAVILSFGVT KGLETLPKQV
RAYVLGK
//
