ID   ALGX_PSESM              Reviewed;         479 AA.
AC   Q887Q4;
DT   25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 88.
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; OrderedLocusNames=PSPTO_1237;
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: 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; AE016853; AAO54762.1; -; Genomic_DNA.
DR   RefSeq; NP_791067.1; NC_004578.1.
DR   RefSeq; WP_011103482.1; NC_004578.1.
DR   AlphaFoldDB; Q887Q4; -.
DR   SMR; Q887Q4; -.
DR   STRING; 223283.PSPTO_1237; -.
DR   EnsemblBacteria; AAO54762; AAO54762; PSPTO_1237.
DR   GeneID; 1182873; -.
DR   KEGG; pst:PSPTO_1237; -.
DR   PATRIC; fig|223283.9.peg.1258; -.
DR   eggNOG; ENOG502Z8PP; Bacteria.
DR   HOGENOM; CLU_651753_0_0_6; -.
DR   OMA; KILIWEF; -.
DR   OrthoDB; 1439364at2; -.
DR   PhylomeDB; Q887Q4; -.
DR   UniPathway; UPA00286; -.
DR   Proteomes; UP000002515; Chromosome.
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;
KW   Reference proteome; Signal; Transferase.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..479
FT                   /note="Alginate biosynthesis protein AlgX"
FT                   /id="PRO_0000020674"
FT   REGION          27..347
FT                   /note="SGNH hydrolase-like domain"
FT   REGION          348..476
FT                   /note="CBM domain"
FT   ACT_SITE        174
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        176
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        269
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   DISULFID        44..229
FT                   /evidence="ECO:0000250"
FT   DISULFID        347..462
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   479 AA;  53348 MW;  93FDC8723BE32358 CRC64;
     MHAHLIKLLS LSSLTAALMA AAGVARADDA QAPTFKAEPC CSLCPAAHDA KNYTTRYQQN
     FTTLVQAQGD WLFRTQEDLR TEFDTTPGGY RRMKELHDAF KSKGVELVVV YQPTRGLVDR
     NKLFPAERDK FDYDKALKNY QAMLGRFSKM GYWVPDLSPL TNEQQAHDFY FRGDQHWTPY
     GAQRTAKIVA ETVKKVPGYS SIPKREFESH ISGRMGKTGT LHNMAGQLCG TSYAVQYMDQ
     FTTEPKGEAG DGDLFGDAGN PEITLVGTSH SGKNYNFAGF LQEYMGADVL NVAFPGGGLE
     GSMLQYLGSE DFQKRPPKIL IWEFSPLYRL DQETIYRQMM ALLDNGCEGK PAVMSASTTL
     KPGNNEVLVN GKNGIKDIRN GSNQIDIRFD DTSVKTLQAR LWYMNGRHED LKIEKPETSD
     TDGRFAFELR EDEDWADQQL LALEIQGPEA GTAPQKVAAK VCKRNVFPSA AKHTAQAGL