ID   ALGI_PSEFL              Reviewed;         495 AA.
AC   P59789;
DT   25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2003, sequence version 1.
DT   25-MAY-2022, entry version 61.
DE   RecName: Full=Probable alginate O-acetylase AlgI;
DE            EC=2.3.1.-;
DE   AltName: Full=Alginate biosynthesis protein AlgI;
GN   Name=algI;
OS   Pseudomonas fluorescens.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=294;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 17397 / DSM 50091 / CIP 73.25 / NCIMB 10525 / 12;
RX   PubMed=12775688; DOI=10.1128/jb.185.12.3515-3523.2003;
RA   Gimmestad M., Sletta H., Ertesvaag H., Bakkevig K., Jain S., Suh S.-J.,
RA   Skjaak-Braek G., Ellingsen T.E., Ohman D.E., Valla S.;
RT   "The Pseudomonas fluorescens AlgG protein, but not its mannuronan C-5-
RT   epimerase activity, is needed for alginate polymer formation.";
RL   J. Bacteriol. 185:3515-3523(2003).
CC   -!- FUNCTION: Together with AlgJ and AlgF, forms an inner membrane complex
CC       which probably interacts with the alginate polymerization-transport
CC       complex and adds acetyl groups at the O-2 and O-3 positions of
CC       mannuronate residues. Acetylation of alginate is important for the
CC       architecture of biofilms and increases the ability of alginate to act
CC       as a defense barrier (By similarity). {ECO:0000250}.
CC   -!- PATHWAY: Glycan biosynthesis; alginate biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AF527790; AAP46697.1; -; Genomic_DNA.
DR   AlphaFoldDB; P59789; -.
DR   SMR; P59789; -.
DR   STRING; 690597.JH730920_gene1195; -.
DR   eggNOG; COG1696; Bacteria.
DR   UniPathway; UPA00286; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0042121; P:alginic acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR024194; Ac/AlaTfrase_AlgI/DltB.
DR   InterPro; IPR028362; AlgI.
DR   InterPro; IPR004299; MBOAT_fam.
DR   Pfam; PF03062; MBOAT; 1.
DR   PIRSF; PIRSF500217; AlgI; 1.
DR   PIRSF; PIRSF016636; AlgI_DltB; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Alginate biosynthesis; Cell inner membrane; Cell membrane;
KW   Membrane; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..495
FT                   /note="Probable alginate O-acetylase AlgI"
FT                   /id="PRO_0000213125"
FT   TRANSMEM        7..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        39..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        101..123
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        136..158
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        296..318
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        344..366
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        387..409
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        471..493
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        307
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   495 AA;  56186 MW;  AB14A159E9757DED CRC64;
     MVFSSNVFLF LFLPIFLGLY YLSGQRYRNL LLLLASYVFY AWWRVDFLAL FAAVTLWNYW
     IGLKVGAAGV RTKPAQRWLL LGVVVDSINV MMKSAGLEPF ILTHVLLPIG ISFYIFESIS
     YIIDVYRGDT PATRNLIDFA AFVAIFPHLI AGPVLRFRDL ADQFNNRTHT LDKFSEGCTR
     FMQGFIKKVF IADTLAVVAD HCFALQNPTT GDAWLGALAY TAQLYFDFSG YSDMAIGLGL
     MMGFRFMENF KQPYISQSIT EFWRRWHISL STWLRDYLYI TLGGNRKGTL TTYRNLFLTM
     LLGGLWHGAN ITYIVWGAWH GMWLAIEKAI GLNTSPRSFN PVRWAFTFLL VVMGWVIFRA
     ENLHVAGRMY GAMFSFGEWS LSELNRANLT GLQVATLVVA YATLAFFGLR DFYTNRPAEK
     TKPADPSLIK AVPGDNPGSI HEPGFTVGQD AAVQPAYWTA DWPRYAMRAA VLLLFVASIL
     KLSAQSFSPF LYFQF