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Database: UniProt
Entry: A0A1M6KV27_9FLAO
LinkDB: A0A1M6KV27_9FLAO
Original site: A0A1M6KV27_9FLAO 
ID   A0A1M6KV27_9FLAO        Unreviewed;      1232 AA.
AC   A0A1M6KV27;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Phospholipid/glycerol acyltransferase domain-containing protein {ECO:0000259|SMART:SM00563};
GN   ORFNames=SAMN04487908_12143 {ECO:0000313|EMBL:SHJ62704.1};
OS   Aequorivita viscosa.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Aequorivita.
OX   NCBI_TaxID=797419 {ECO:0000313|EMBL:SHJ62704.1, ECO:0000313|Proteomes:UP000184172};
RN   [1] {ECO:0000313|Proteomes:UP000184172}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 26349 {ECO:0000313|Proteomes:UP000184172};
RA   Varghese N., Submissions S.;
RL   Submitted (NOV-2016) 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; FQYV01000021; SHJ62704.1; -; Genomic_DNA.
DR   RefSeq; WP_073219966.1; NZ_FQYV01000021.1.
DR   AlphaFoldDB; A0A1M6KV27; -.
DR   STRING; 797419.SAMN05216556_11548; -.
DR   OrthoDB; 9803035at2; -.
DR   Proteomes; UP000184172; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR   CDD; cd07989; LPLAT_AGPAT-like; 1.
DR   Gene3D; 1.20.1640.10; Multidrug efflux transporter AcrB transmembrane domain; 2.
DR   InterPro; IPR004869; MMPL_dom.
DR   InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR   PANTHER; PTHR33406; MEMBRANE PROTEIN MJ1562-RELATED; 1.
DR   PANTHER; PTHR33406:SF2; MEMBRANE PROTEIN SCO6666-RELATED; 1.
DR   Pfam; PF01553; Acyltransferase; 1.
DR   Pfam; PF03176; MMPL; 2.
DR   SMART; SM00563; PlsC; 1.
DR   SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
DR   SUPFAM; SSF82866; Multidrug efflux transporter AcrB transmembrane domain; 2.
PE   4: Predicted;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184172};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        269..288
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        295..315
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        321..342
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        362..381
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        387..410
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        435..452
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        658..677
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        684..704
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        710..729
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        750..769
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        775..800
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        821..842
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        854..874
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          890..999
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
SQ   SEQUENCE   1232 AA;  139472 MW;  8A0ECBC8405A8D8C CRC64;
     MGKWFYKTHQ FLQKNKIGTA LVFLLLLSGL VFLVTKTRFE EDISKLIPIN GESQNLQKVL
     KTVNFTDKII VTIRRNDSVD VTELTQYATE FIDSLETHSS QYIKNIRGKV DDDDLLRTMD
     FVYENLPLFL DKADYKTIAN KLEKDSVSAL TEANYKTLIS PSGIVSKDVI LKDPLGLSFI
     ALKKLRQLGV ADEFVLKDGF LVSKDENNLL LFITPKFASS ETSENSKFAE DLYSLQNTLN
     QKYSGQVKSE YFGAALIAVA NAQQIKSDIQ FTVGIAFTVL ILVFMLFYRK VYVPIILFVP
     TLFGGLLAVS LLYLLRDNIS AISLGIGSVL LGVTLDYSLH ILTHIRNNET VESLYKDVAE
     PILMSSLTTA LAFLCLLFLD SQALQDLGVF AAISVLGASV FALLFIPLVY KNPLSPKQQI
     NVLDRVADYP FHKNKWLLIG LGAALIVSFF TFNKVEFNKD ISKLNYESEE IKAAMQHLDE
     LTDISSKSVY LATYGKSVES TLQLNDSIYK TLELLEEEGK ISSFSSIGAL VQSQRDQRDK
     IAEWQQFWSK SRKDSTENNL IRSGEQLGFK PSTFNRFYAF LNTDFQTLKP EDYQQIPSVI
     LEDYIKTEAD FTTITTLVKL NDENDLGIKN IFNETPNTLV IDRQEMNETF LGNLKNDFNS
     LIGYCLLAVL LILFLFFRSL SLTIVTATPI FLTWFLTLGI MGLFNIQFNI FNIIISTFIF
     GLGIDYSIFM TKGLLKELRT GEKVMVTNKT SIMLSVLTTI LGVGVLVFAK HPALYSISIV
     SIIGIFSAMF TAFTVQPLLF KLFIGSSKKR PITPRMFVHS VLSFSYFGLG GICLSIYSVT
     LMPILPFSKK MKMGWFHIVI AKFFKSVLYT NPFVKKKVIN RAGEHFSKPA VIIANHTSFL
     DIVAVGMLHP KICFLVNDWV YNSPIFGKAV QKADFYPVSS GIENSLEPLQ KKIEQGYSLM
     AFPEGTRSHT NKIKRFHKGA FYLANQFNLD ILPVLIHGNS EVNPKGSFII KDGSISVIIL
     PRIKAEDKSF GTNHTQQAKK IGAYFRDEFL NLRNEIEDET YFHHIVLEEY RYKGDSIYKT
     VKRDLIENAE VYFQVIRQLE KRGSIAHISE DFGQLDFLLT LDSPDRKIYS LIEESESRTI
     LQNSYITHKY EKLFFKASVS EILNSDIEML ILSSEKHLAE IMNQLSDLSV QTIVLLKQAS
     LAETENIITL GFQRIYQNLN ISIFKKSGNN AE
//
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