ID   ALGX_PSEFL              Reviewed;         485 AA.
AC   P59788;
DT   25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2003, sequence version 1.
DT   25-MAY-2022, entry version 51.
DE   RecName: Full=Alginate biosynthesis protein AlgX;
DE   AltName: Full=Probable alginate O-acetyltransferase AlgX;
DE            EC=2.3.1.-;
DE   Flags: Precursor;
GN   Name=algX;
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: Plays two roles in the biosynthesis of the exopolysaccharide
CC       alginate: protects alginate from degradation as the polymer traverses
CC       the periplasm, and also plays a role in its O-acetylation. Probably has
CC       acetyltransferase activity in vivo (By similarity). {ECO:0000250}.
CC   -!- PATHWAY: Glycan biosynthesis; alginate biosynthesis.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
CC   -!- DOMAIN: Consists of two domains, with an N-terminal domain with
CC       structural homology to members of the SGNH (GDSL) hydrolase superfamily
CC       and a C-terminal carbohydrate-binding module (CBM) that may bind
CC       alginate. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the AlgX family. {ECO:0000305}.
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DR   EMBL; AF527790; AAP46695.1; -; Genomic_DNA.
DR   AlphaFoldDB; P59788; -.
DR   SMR; P59788; -.
DR   STRING; 690597.JH730920_gene1193; -.
DR   PRIDE; P59788; -.
DR   eggNOG; ENOG502Z8PP; Bacteria.
DR   UniPathway; UPA00286; -.
DR   GO; GO:0042597; C:periplasmic space; 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; cd14487; AlgX_C; 1.
DR   CDD; cd14441; AlgX_N; 1.
DR   Gene3D; 2.60.120.1380; -; 1.
DR   InterPro; IPR031811; ALGX/ALGJ_SGNH-like.
DR   InterPro; IPR031798; AlgX_C.
DR   InterPro; IPR038639; AlgX_C_sf.
DR   InterPro; IPR034655; AlgX_N.
DR   Pfam; PF16822; ALGX; 1.
DR   Pfam; PF16824; CBM_26; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Alginate biosynthesis; Disulfide bond; Periplasm; Signal;
KW   Transferase.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..485
FT                   /note="Alginate biosynthesis protein AlgX"
FT                   /id="PRO_0000020672"
FT   REGION          30..355
FT                   /note="SGNH hydrolase-like domain"
FT   REGION          356..482
FT                   /note="CBM domain"
FT   ACT_SITE        182
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        184
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        277
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   DISULFID        47..237
FT                   /evidence="ECO:0000250"
FT   DISULFID        355..468
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   485 AA;  53856 MW;  9983BDB1050ECC7D CRC64;
     MTLMHPHMIK LLSLSGLTLG LLAASQGVRA DEIKAPTFTA EPCCSLCPAA HDAKNYTTRY
     QQNFTTLVQA QGDWLFRTQE DLRTEFDTTP SGYKRMQQLH DAFKAKGVEL VVVYQPTRGL
     VNRNKLNPEE KAKFDFDKAL GNYKTMLGRF AKMGYVVPDL SPLTNEQLPD ELPAHDFYFR
     GDQHWTPYGA QRTAKIVAAK VKQMPEYAEI PKREFETKRS GRMGKTGTLH NMAGQLCGTS
     YAIQYMDQFT TEPKGEAGDG DLFSDSGNPQ ITLVGTSHSG KNYNFAGFLE EEIGADILNV
     AFPGGGLEGS MIQYLGSDEF QKSPPKILIW EFSPLYRLDQ ETIYRQMMAL LDNGCEGKTA
     QMSASTTLKP GKNELLVNSS NKDLRNANHQ VDIRFADPSV KTLQATLWYM NGRHEDIKIE
     KPETSDTDGR FAFELRTDED WASQNLLAVE VQGPEAGAAA QKVEAKICTR NVFPAGGQQT
     AAAGQ