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Database: UniProt
Entry: M6VVI1_9LEPT
LinkDB: M6VVI1_9LEPT
Original site: M6VVI1_9LEPT 
ID   M6VVI1_9LEPT            Unreviewed;       497 AA.
AC   M6VVI1;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=Membrane-bound O-acyltransferase family MBOAT {ECO:0000313|EMBL:EMO59156.1};
GN   ORFNames=LEP1GSC161_0573 {ECO:0000313|EMBL:EMO59156.1};
OS   Leptospira santarosai str. CBC1416.
OC   Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC   Leptospira.
OX   NCBI_TaxID=1193059 {ECO:0000313|EMBL:EMO59156.1, ECO:0000313|Proteomes:UP000012149};
RN   [1] {ECO:0000313|EMBL:EMO59156.1, ECO:0000313|Proteomes:UP000012149}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBC1416 {ECO:0000313|EMBL:EMO59156.1,
RC   ECO:0000313|Proteomes:UP000012149};
RA   Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D.,
RA   Sanka R., DePew J., Purushe J., Matthias M.A., Vinetz J.M., Sutton G.G.,
RA   Nierman W.C., Fouts D.E.;
RL   Submitted (JAN-2013) 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 membrane-bound acyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00010323, ECO:0000256|PIRNR:PIRNR016636}.
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:EMO59156.1}.
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DR   EMBL; AKWE02000043; EMO59156.1; -; Genomic_DNA.
DR   AlphaFoldDB; M6VVI1; -.
DR   Proteomes; UP000012149; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0042121; P:alginic acid biosynthetic process; IEA:InterPro.
DR   InterPro; IPR024194; Ac/AlaTfrase_AlgI/DltB.
DR   InterPro; IPR028362; AlgI.
DR   InterPro; IPR004299; MBOAT_fam.
DR   PANTHER; PTHR13285; ACYLTRANSFERASE; 1.
DR   PANTHER; PTHR13285:SF23; TEICHOIC ACID D-ALANYLTRANSFERASE; 1.
DR   Pfam; PF03062; MBOAT; 1.
DR   PIRSF; PIRSF500217; AlgI; 1.
DR   PIRSF; PIRSF016636; AlgI_DltB; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW   ECO:0000256|PIRNR:PIRNR016636};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW   ECO:0000256|PIRNR:PIRNR016636};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR016636};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR016636};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        14..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        69..85
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        97..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        137..154
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        174..193
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        248..266
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        336..356
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        388..410
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        431..453
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        473..495
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   497 AA;  57715 MW;  FA44859A16A28D9D CRC64;
     MKKDRGDRSG ANDLLFPTLE FFVFFIFVFL VYWYLIPYLF GNDTKALSLT HFFLLVVSYY
     FYMSWDWRFG GLILLSTVID FVLAAKIGSS QDGRTRFALI TISLILNLVF ILGFFKYYNF
     FADSINLFLG HFGVKNALPI LRVILPVGIS FYTFQSLSYT IDVYRRQILP EKSFLRFALF
     VSFFPQLVAG PIVTAKTFLP QLDTAKNLTE IRFRKAIRYF ILGYIKKVVL SDNAAPIVEK
     IFGHPENFGT VALWLGATLF LIQIYCDFSG YTDMAYASAL LLGYELPENF RMPFIARSVT
     EHWRRWHMTL STWLRDYVYI SLGGNRAGVL RHRFNLWFTM FVAGFWHGAA WTFIIWGSCQ
     GTILLLEALY GSLKEKHFRD FRILPDKILA PIQIILTCFV SVAVGTWFRA ESFTKGWVML
     KKMFVYSEGG LRPYMLKTGI PVVLCVIAGQ WLGYFIFEKN KEWNPPVWLE FSFYPIVAVI
     LALLTPDLEL PFIYFQF
//
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