ALGX_PSEAE
ID ALGX_PSEAE Reviewed; 474 AA.
AC Q51372; Q9HY68;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2003, sequence version 2.
DT 03-AUG-2022, entry version 106.
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=PA3546;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=FRD1;
RX PubMed=8550492; DOI=10.1128/jb.178.3.625-632.1996;
RA Monday S.R., Schiller N.L.;
RT "Alginate synthesis in Pseudomonas aeruginosa: the role of AlgL (alginate
RT lyase) and AlgX.";
RL J. Bacteriol. 178:625-632(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [3]
RP PROTEIN SEQUENCE OF 27-32, FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=FRD1;
RX PubMed=15489449; DOI=10.1128/jb.186.21.7369-7377.2004;
RA Robles-Price A., Wong T.Y., Sletta H., Valla S., Schiller N.L.;
RT "AlgX is a periplasmic protein required for alginate biosynthesis in
RT Pseudomonas aeruginosa.";
RL J. Bacteriol. 186:7369-7377(2004).
RN [4]
RP INTERACTION WITH MUCD, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=FRD1;
RX PubMed=16376476; DOI=10.1016/j.biochi.2005.06.003;
RA Gutsche J., Remminghorst U., Rehm B.H.;
RT "Biochemical analysis of alginate biosynthesis protein AlgX from
RT Pseudomonas aeruginosa: purification of an AlgX-MucD (AlgY) protein
RT complex.";
RL Biochimie 88:245-251(2006).
RN [5]
RP CRYSTALLIZATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=20445266; DOI=10.1107/s1744309110011851;
RA Weadge J.T., Yip P.P., Robinson H., Arnett K., Tipton P.A., Howell P.L.;
RT "Expression, purification, crystallization and preliminary X-ray analysis
RT of Pseudomonas aeruginosa AlgX.";
RL Acta Crystallogr. F 66:588-591(2010).
RN [6]
RP INTERACTION WITH ALGK AND MUCD, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=21713511; DOI=10.1007/s00253-011-3430-0;
RA Hay I.D., Schmidt O., Filitcheva J., Rehm B.H.;
RT "Identification of a periplasmic AlgK-AlgX-MucD multiprotein complex in
RT Pseudomonas aeruginosa involved in biosynthesis and regulation of
RT alginate.";
RL Appl. Microbiol. Biotechnol. 93:215-227(2012).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.14 ANGSTROMS) OF 27-474, FUNCTION, DOMAIN,
RP DISULFIDE BONDS, ACTIVE SITES, REACTION MECHANISM, SUBUNIT, AND MUTAGENESIS
RP OF ASP-174; HIS-176; SER-269; TYR-275 AND TYR-328.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=23779107; DOI=10.1074/jbc.m113.484931;
RA Riley L.M., Weadge J.T., Baker P., Robinson H., Codee J.D., Tipton P.A.,
RA Ohman D.E., Howell P.L.;
RT "Structural and functional characterization of Pseudomonas aeruginosa AlgX:
RT role of AlgX in alginate acetylation.";
RL J. Biol. Chem. 288:22299-22314(2013).
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. Acetylation
CC of alginate causes the cells in the biofilm to adhere better to lung
CC epithelium, form microcolonies, and resist the effects of the host
CC immune system and/or antibiotics. Displays a low acetylesterase
CC activity in vitro using a pseudosubstrate, 3-carboxyumbelliferyl
CC acetate. Probably has acetyltransferase activity in vivo.
CC {ECO:0000269|PubMed:15489449, ECO:0000269|PubMed:23779107}.
CC -!- PATHWAY: Glycan biosynthesis; alginate biosynthesis.
CC -!- SUBUNIT: Monomer. Interacts with AlgK and MucD.
CC {ECO:0000269|PubMed:16376476, ECO:0000269|PubMed:21713511,
CC ECO:0000269|PubMed:23779107}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:15489449,
CC ECO:0000269|PubMed:16376476}.
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:0000269|PubMed:23779107}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene in the mucoid strain FRD1
CC are phenotypically non-mucoid, i.e. non-alginate producing, and secrete
CC dialyzable oligouronic acids of various lengths that are mainly
CC mannuronic acid dimers resulting from alginate lyase (AlgL) degradation
CC of polymannuronic acid. Disruption of algX in the non-mucoid strain
CC PAO1 does not visibly alter the phenotype of the parent.
CC {ECO:0000269|PubMed:15489449, ECO:0000269|PubMed:16376476,
CC ECO:0000269|PubMed:21713511}.
CC -!- SIMILARITY: Belongs to the AlgX family. {ECO:0000305}.
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DR EMBL; U27829; AAA91126.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG06934.1; -; Genomic_DNA.
DR PIR; G83202; G83202.
DR RefSeq; NP_252236.1; NC_002516.2.
DR RefSeq; WP_003112885.1; NZ_QZGE01000001.1.
DR PDB; 4KNC; X-ray; 2.14 A; A/B=27-474.
DR PDBsum; 4KNC; -.
DR AlphaFoldDB; Q51372; -.
DR SMR; Q51372; -.
DR IntAct; Q51372; 1.
DR STRING; 287.DR97_4396; -.
DR PaxDb; Q51372; -.
DR PRIDE; Q51372; -.
DR EnsemblBacteria; AAG06934; AAG06934; PA3546.
DR GeneID; 878551; -.
DR KEGG; pae:PA3546; -.
DR PATRIC; fig|208964.12.peg.3710; -.
DR PseudoCAP; PA3546; -.
DR HOGENOM; CLU_651753_0_0_6; -.
DR OMA; KILIWEF; -.
DR PhylomeDB; Q51372; -.
DR BioCyc; PAER208964:G1FZ6-3614-MON; -.
DR UniPathway; UPA00286; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IDA:PseudoCAP.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0042121; P:alginic acid biosynthetic process; IDA:PseudoCAP.
DR GO; GO:0044010; P:single-species biofilm formation; IDA:PseudoCAP.
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 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Alginate biosynthesis;
KW Direct protein sequencing; Disulfide bond; Periplasm; Reference proteome;
KW Signal; Transferase.
FT SIGNAL 1..26
FT /evidence="ECO:0000269|PubMed:15489449"
FT CHAIN 27..474
FT /note="Alginate biosynthesis protein AlgX"
FT /id="PRO_0000020671"
FT REGION 27..347
FT /note="SGNH hydrolase-like domain"
FT REGION 348..474
FT /note="CBM domain"
FT ACT_SITE 174
FT /evidence="ECO:0000305|PubMed:23779107"
FT ACT_SITE 176
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:23779107"
FT ACT_SITE 269
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:23779107"
FT DISULFID 44..229
FT /evidence="ECO:0000269|PubMed:23779107"
FT DISULFID 347..460
FT /evidence="ECO:0000269|PubMed:23779107"
FT MUTAGEN 174
FT /note="D->A: Produces a non-acetylated alginate. Loss of in
FT vitro acetylesterase activity."
FT /evidence="ECO:0000269|PubMed:23779107"
FT MUTAGEN 176
FT /note="H->A: Produces a non-acetylated alginate. Loss of in
FT vitro acetylesterase activity."
FT /evidence="ECO:0000269|PubMed:23779107"
FT MUTAGEN 269
FT /note="S->A: Produces a non-acetylated alginate. Loss of in
FT vitro acetylesterase activity."
FT /evidence="ECO:0000269|PubMed:23779107"
FT MUTAGEN 275
FT /note="Y->A: 40% reduction in alginate acetylation."
FT /evidence="ECO:0000269|PubMed:23779107"
FT MUTAGEN 328
FT /note="Y->A: 50% reduction in alginate acetylation."
FT /evidence="ECO:0000269|PubMed:23779107"
FT CONFLICT 49
FT /note="Y -> D (in Ref. 1; AAA91126)"
FT /evidence="ECO:0000305"
FT HELIX 45..48
FT /evidence="ECO:0007829|PDB:4KNC"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:4KNC"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:4KNC"
FT STRAND 63..66
FT /evidence="ECO:0007829|PDB:4KNC"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:4KNC"
FT TURN 75..78
FT /evidence="ECO:0007829|PDB:4KNC"
FT HELIX 87..102
FT /evidence="ECO:0007829|PDB:4KNC"
FT STRAND 106..111
FT /evidence="ECO:0007829|PDB:4KNC"
FT HELIX 115..119
FT /evidence="ECO:0007829|PDB:4KNC"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:4KNC"
FT HELIX 125..130
FT /evidence="ECO:0007829|PDB:4KNC"
FT HELIX 133..149
FT /evidence="ECO:0007829|PDB:4KNC"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:4KNC"
FT STRAND 174..177
FT /evidence="ECO:0007829|PDB:4KNC"
FT HELIX 179..195
FT /evidence="ECO:0007829|PDB:4KNC"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:4KNC"
FT STRAND 206..217
FT /evidence="ECO:0007829|PDB:4KNC"
FT HELIX 220..229
FT /evidence="ECO:0007829|PDB:4KNC"
FT STRAND 236..247
FT /evidence="ECO:0007829|PDB:4KNC"
FT HELIX 253..259
FT /evidence="ECO:0007829|PDB:4KNC"
FT STRAND 263..266
FT /evidence="ECO:0007829|PDB:4KNC"
FT HELIX 269..271
FT /evidence="ECO:0007829|PDB:4KNC"
FT HELIX 273..275
FT /evidence="ECO:0007829|PDB:4KNC"
FT HELIX 277..285
FT /evidence="ECO:0007829|PDB:4KNC"
FT STRAND 289..291
FT /evidence="ECO:0007829|PDB:4KNC"
FT TURN 298..300
FT /evidence="ECO:0007829|PDB:4KNC"
FT HELIX 301..308
FT /evidence="ECO:0007829|PDB:4KNC"
FT HELIX 310..314
FT /evidence="ECO:0007829|PDB:4KNC"
FT STRAND 318..324
FT /evidence="ECO:0007829|PDB:4KNC"
FT HELIX 333..342
FT /evidence="ECO:0007829|PDB:4KNC"
FT TURN 343..349
FT /evidence="ECO:0007829|PDB:4KNC"
FT STRAND 352..359
FT /evidence="ECO:0007829|PDB:4KNC"
FT STRAND 362..369
FT /evidence="ECO:0007829|PDB:4KNC"
FT HELIX 378..380
FT /evidence="ECO:0007829|PDB:4KNC"
FT STRAND 381..389
FT /evidence="ECO:0007829|PDB:4KNC"
FT STRAND 394..401
FT /evidence="ECO:0007829|PDB:4KNC"
FT STRAND 406..412
FT /evidence="ECO:0007829|PDB:4KNC"
FT STRAND 422..426
FT /evidence="ECO:0007829|PDB:4KNC"
FT TURN 431..435
FT /evidence="ECO:0007829|PDB:4KNC"
FT STRAND 437..444
FT /evidence="ECO:0007829|PDB:4KNC"
FT STRAND 454..461
FT /evidence="ECO:0007829|PDB:4KNC"
SQ SEQUENCE 474 AA; 52596 MW; D31FBD293547069A CRC64;
MKTRTSRLFR LSALAAGLCL AQAALAADPG AAPSYQALPA GNLCPAAAYD SRYNTKYLGF
FTHLVQAQDD WLFRTTYDLR TDFGTSAEGW RELRALRDEL KRKGIELVVV YQPTRGLVNR
EKLSPAEKAG FDYELAKKNY LATIARFRQA GIWTPDFSPL FDEKEEHAYY FKGDHHWTPH
GARRSAKIVA ETLKQVPGFE EIPKKQFESK RVGLLSKLGT FHKAAAQLCG NSYATQYVDR
FETEPVGASD SGDLFGDGGN PQIALVGTSN SGPAYNFAGF LEEFSGADIL NNAVSGGGFD
SSLLAYMTSE EFHKNPPKIL IWEFATHYDM AQKSFYRQAM PLVDNGCSGR KTVLSRKVKL
RQGRNEVLLN SAALPIRSGS YVADVTYSDP SVHELKNTIW YMNGRREQLK IEQSKAVDTG
GRYVFQLRND SDWADQQFLS LEIEAPEDMP QGLEVQASIC QAAPAKASQS VAGR
