ID   ALGI_PSESM              Reviewed;         518 AA.
AC   Q887Q6;
DT   25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 101.
DE   RecName: Full=Probable alginate O-acetylase AlgI;
DE            EC=2.3.1.-;
DE   AltName: Full=Alginate biosynthesis protein AlgI;
GN   Name=algI; OrderedLocusNames=PSPTO_1235;
OS   Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=223283;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-871 / DC3000;
RX   PubMed=12928499; DOI=10.1073/pnas.1731982100;
RA   Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T.,
RA   Gwinn M.L., Dodson R.J., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA   Daugherty S.C., Brinkac L.M., Beanan M.J., Haft D.H., Nelson W.C.,
RA   Davidsen T.M., Zafar N., Zhou L., Liu J., Yuan Q., Khouri H.M.,
RA   Fedorova N.B., Tran B., Russell D., Berry K.J., Utterback T.R.,
RA   Van Aken S.E., Feldblyum T.V., D'Ascenzo M., Deng W.-L., Ramos A.R.,
RA   Alfano J.R., Cartinhour S., Chatterjee A.K., Delaney T.P., Lazarowitz S.G.,
RA   Martin G.B., Schneider D.J., Tang X., Bender C.L., White O., Fraser C.M.,
RA   Collmer A.;
RT   "The complete genome sequence of the Arabidopsis and tomato pathogen
RT   Pseudomonas syringae pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(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; AE016853; AAO54760.1; -; Genomic_DNA.
DR   RefSeq; NP_791065.1; NC_004578.1.
DR   RefSeq; WP_005764153.1; NC_004578.1.
DR   AlphaFoldDB; Q887Q6; -.
DR   SMR; Q887Q6; -.
DR   STRING; 223283.PSPTO_1235; -.
DR   EnsemblBacteria; AAO54760; AAO54760; PSPTO_1235.
DR   GeneID; 1182871; -.
DR   KEGG; pst:PSPTO_1235; -.
DR   PATRIC; fig|223283.9.peg.1256; -.
DR   eggNOG; COG1696; Bacteria.
DR   HOGENOM; CLU_025255_1_3_6; -.
DR   OMA; IIWGAWH; -.
DR   OrthoDB; 1297594at2; -.
DR   PhylomeDB; Q887Q6; -.
DR   UniPathway; UPA00286; -.
DR   Proteomes; UP000002515; 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..518
FT                   /note="Probable alginate O-acetylase AlgI"
FT                   /id="PRO_0000213127"
FT   TRANSMEM        2..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        319..341
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        354..373
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        402..424
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        493..515
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          435..456
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        322
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   518 AA;  58606 MW;  4621789C6FACD9B5 CRC64;
     MVFSSNVFLF MFLPIFLGLY YLSGQRYRNL LLLIASYIFY AWWRVDFLAL FIGVTVWNYW
     IGLKVGAAGV RTKPAQRWLL LGVIVDLCIL GYFKYANFGV DSINAAMTSM GLEPFILTHV
     LLPIGISFYV FESISYIIDV YRGDTPATRN LIDFAAFVAI FPHLIAGPVL RFRDLADQFN
     NRTHTLDKFS EGATRFMQGF IKKVFIADTL AIVADHCFAL QNPTTGDAWL GALAYTAQLY
     FDFSGYSDMA IGLGLMMGFR FMENFKQPYI SQSITEFWRR WHISLSTWLR DYLYITLGGN
     RGGKVATYRN LFLTMLLGGL WHGANVTYII WGAWHGMWLA IEKAVGINTK PYSFNVIRWA
     LTFLLVVIGW VIFRSENLHV AGRMYGAMFS FGDWQLSELN RASLTGLQVA TLVVAYATLA
     FFGLRDFYQN REKDSGKSAR ADGPATEQPG TIKAVPGDAP GSLHLPGYTV GSEAQVQPAY
     WVADWPRYAM RALILLLFVA SILKLSAQSF SPFLYFQF