ID   ALGX_PSEPK              Reviewed;         479 AA.
AC   Q88ND0;
DT   25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 90.
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=PP_1282;
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: 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; AE015451; AAN66906.1; -; Genomic_DNA.
DR   RefSeq; NP_743442.1; NC_002947.4.
DR   RefSeq; WP_010952411.1; NC_002947.4.
DR   AlphaFoldDB; Q88ND0; -.
DR   SMR; Q88ND0; -.
DR   STRING; 160488.PP_1282; -.
DR   EnsemblBacteria; AAN66906; AAN66906; PP_1282.
DR   KEGG; ppu:PP_1282; -.
DR   PATRIC; fig|160488.4.peg.1359; -.
DR   eggNOG; ENOG502Z8PP; Bacteria.
DR   HOGENOM; CLU_651753_0_0_6; -.
DR   OMA; KILIWEF; -.
DR   PhylomeDB; Q88ND0; -.
DR   BioCyc; PPUT160488:G1G01-1369-MON; -.
DR   UniPathway; UPA00286; -.
DR   Proteomes; UP000000556; 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..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..479
FT                   /note="Alginate biosynthesis protein AlgX"
FT                   /id="PRO_0000020673"
FT   REGION          24..349
FT                   /note="SGNH hydrolase-like domain"
FT   REGION          350..476
FT                   /note="CBM domain"
FT   ACT_SITE        176
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        178
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        271
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   DISULFID        41..231
FT                   /evidence="ECO:0000250"
FT   DISULFID        349..463
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   479 AA;  53356 MW;  3D402728C9C43D07 CRC64;
     MTPHLMKLLG LSAALLAISQ GVRAEDVKAP TFSAEPCCQL CPEAHDASRY TTRYQQNFTT
     LVQAQGDWLF RTREDLRTEF NTTPAGYKRL QQVHDAFKKR GVELVVVYQP TRGLVNRNML
     NPAEKAAFDY QKALGNYQAM LKRFASMGYN VPDLSPLTNE QLAAADQGKD FYFRGDQHWT
     PYGAERAAKI VADTVHKMPA FEGIPRKEFE TRKSGRMGKT GTLHNVAGQL CGTSYAVQYM
     DQFATEPKGA SGGDDLFGDS GNAQITLVGT SHSGKNYNFS GFLEQYIGAD VLNVAFPGGG
     LEGSMIQYLG SEEFQKNPPK ILIWEFSPLY RLDQETIWRQ ILGLLDDGCD DRPALMSAST
     TLKPGKNELM VNGKGGVIKD LINRNLQMDV KFEDPSVKVL QATLWYLNGR HEDIKLEKPE
     TSDTDGRFVF QMREDEDWAS QRLLAFEVQG PESGTQKVEA KLCKRNNFAV PAQTAQAGQ