ID   ALGI_PSEPK              Reviewed;         485 AA.
AC   Q88ND2;
DT   25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Probable alginate O-acetylase AlgI;
DE            EC=2.3.1.-;
DE   AltName: Full=Alginate biosynthesis protein AlgI;
GN   Name=algI; OrderedLocusNames=PP_1280;
OS   Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS   / KT2440).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=160488;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX   PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA   Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA   Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA   Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA   Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA   Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA   Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA   Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA   Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT   "Complete genome sequence and comparative analysis of the metabolically
RT   versatile Pseudomonas putida KT2440.";
RL   Environ. Microbiol. 4:799-808(2002).
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; AE015451; AAN66904.1; -; Genomic_DNA.
DR   RefSeq; NP_743440.1; NC_002947.4.
DR   RefSeq; WP_010952409.1; NC_002947.4.
DR   AlphaFoldDB; Q88ND2; -.
DR   SMR; Q88ND2; -.
DR   STRING; 160488.PP_1280; -.
DR   EnsemblBacteria; AAN66904; AAN66904; PP_1280.
DR   KEGG; ppu:PP_1280; -.
DR   PATRIC; fig|160488.4.peg.1357; -.
DR   eggNOG; COG1696; Bacteria.
DR   HOGENOM; CLU_025255_1_3_6; -.
DR   OMA; IIWGAWH; -.
DR   PhylomeDB; Q88ND2; -.
DR   BioCyc; PPUT160488:G1G01-1367-MON; -.
DR   UniPathway; UPA00286; -.
DR   Proteomes; UP000000556; Chromosome.
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; Reference proteome; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..485
FT                   /note="Probable alginate O-acetylase AlgI"
FT                   /id="PRO_0000213126"
FT   TRANSMEM        7..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        39..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        78..100
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        115..137
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        150..172
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        312..334
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        360..382
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        402..424
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        461..483
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        322
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   485 AA;  55452 MW;  D3E30CC528EB92A1 CRC64;
     MVFSSNVFLF LFLPIFLGLY YLSGQRYRNL LLLVASYIFY AWWRVDFLAL FAGVTLWNYW
     IGLKVGAAGV RTKPAQRWLL LGVGVDLAIL GYFKYANFGV DSLNAIMTSF GLEPFILTHV
     LLPIGISFYI FESISYIIDV YRGDTPATRN LIDFAAFVAI FPHLIAGPVL RFKDLVDQFN
     NRTHTLDKFS EGCTRFMQGF IKKVFIADTL AVVADHCFAL QNPTTGDAWL GALAYTAQLY
     FDFSGYSDMA IGLGLMMGFR FMENFKQPYI SQSITEFWRR WHISLSTWLR DYLYITLGGN
     RKGTFNTYRN LFLTMLLGGL WHGANFTYII WGAWHGMWLA IERALGLDTN PQRFNPVKWA
     FTFLLVVVGW VIFRAENLHV AARMYGAMFS FGDWQLSELN RAQLTGLQVA TLVIAYLTLA
     FFGLRDFYRN ARPTPKATPV QVNADGSIGL DWTRVMTRAL ILLLFVASIL KLSAQSYSPF
     LYFQF