ID   ALGJ_PSEFL              Reviewed;         394 AA.
AC   P59792;
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 AlgJ;
DE            EC=2.3.1.-;
DE   AltName: Full=Alginate biosynthesis protein AlgJ;
DE   Flags: Precursor;
GN   Name=algJ;
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 AlgI 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}; Peripheral
CC       membrane protein {ECO:0000250}; Periplasmic side {ECO:0000250}.
CC       Periplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the AlgJ family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF527790; AAP46698.1; -; Genomic_DNA.
DR   AlphaFoldDB; P59792; -.
DR   SMR; P59792; -.
DR   STRING; 690597.JH730920_gene1196; -.
DR   PRIDE; P59792; -.
DR   eggNOG; ENOG502Z851; Bacteria.
DR   UniPathway; UPA00286; -.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
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   CDD; cd14442; AlgJ_like; 1.
DR   InterPro; IPR034657; AlgJ.
DR   InterPro; IPR031811; ALGX/ALGJ_SGNH-like.
DR   Pfam; PF16822; ALGX; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Alginate biosynthesis; Cell inner membrane; Cell membrane;
KW   Membrane; Periplasm; Signal; Transferase.
FT   SIGNAL          1..37
FT                   /evidence="ECO:0000255"
FT   CHAIN           38..394
FT                   /note="Probable alginate O-acetylase AlgJ"
FT                   /id="PRO_0000001121"
FT   ACT_SITE        191
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        193
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        287
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   394 AA;  43952 MW;  235ABA6150BF3F67 CRC64;
     MTRSLRVLYI GLFLVLLLAL GAWSLRSFFG FSTNADATVL NGRWTKAVET HYDEEFPIKR
     LGTNLWAALD YKLFNEGRPG VVLGRDHWLY SDEEFNPAVN EDQNLEGNYA LVEGVRQKLK
     AQGIQLVMAI VPAKVRLYPE HLGEVKPASI HANLYQDFHA RVAADKIIAP DLLGPLQQAK
     LGGKQVFLRT DTHWTPDGAE IAAKQLAKTI ADKTPLNGEP QRFVTEAEKT EPHKGDLRLF
     LPLDPLFENL MPPKEPLEKR VTHLAETKGD DALFSDSETP VALVGTSYSA NPNWNFVGAL
     KQALGSDVIS YAEDGHGPIL PMLSYLKSDD FKNNPPQVLI WEFPERYLPV NNEIGDADPS
     WVAQLKQAGS RQQNMALNTP VNHQKSETPD RAQN