ALGI_PSEAE
ID ALGI_PSEAE Reviewed; 520 AA.
AC Q51392; Q9HY67;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2003, sequence version 2.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Probable alginate O-acetylase AlgI;
DE EC=2.3.1.-;
DE AltName: Full=Alginate biosynthesis protein AlgI;
GN Name=algI; OrderedLocusNames=PA3548;
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], AND SUBCELLULAR LOCATION.
RC STRAIN=FRD1;
RX PubMed=8636017; DOI=10.1128/jb.178.8.2186-2195.1996;
RA Franklin M.J., Ohman D.E.;
RT "Identification of algI and algJ in the Pseudomonas aeruginosa alginate
RT biosynthetic gene cluster which are required for alginate O acetylation.";
RL J. Bacteriol. 178:2186-2195(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 SUBCELLULAR LOCATION.
RC STRAIN=FRD1;
RX PubMed=12003941; DOI=10.1128/jb.184.11.3000-3007.2002;
RA Franklin M.J., Ohman D.E.;
RT "Mutant analysis and cellular localization of the AlgI, AlgJ, and AlgF
RT proteins required for O acetylation of alginate in Pseudomonas
RT aeruginosa.";
RL J. Bacteriol. 184:3000-3007(2002).
RN [4]
RP ROLE IN BIOFILM FORMATION.
RC STRAIN=FRD1;
RX PubMed=11208804; DOI=10.1128/jb.183.3.1047-1057.2001;
RA Nivens D.E., Ohman D.E., Williams J., Franklin M.J.;
RT "Role of alginate and its O acetylation in formation of Pseudomonas
RT aeruginosa microcolonies and biofilms.";
RL J. Bacteriol. 183:1047-1057(2001).
RN [5]
RP ROLE IN RESISTANCE TO PHAGOCYTOSIS.
RC STRAIN=FRD1;
RX PubMed=11179370; DOI=10.1128/iai.69.3.1895-1901.2001;
RA Pier G.B., Coleman F., Grout M., Franklin M., Ohman D.E.;
RT "Role of alginate O acetylation in resistance of mucoid Pseudomonas
RT aeruginosa to opsonic phagocytosis.";
RL Infect. Immun. 69:1895-1901(2001).
CC -!- FUNCTION: Together with AlgJ 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 resistance to opsonic killing in
CC the host. {ECO:0000269|PubMed:11179370, ECO:0000269|PubMed:11208804}.
CC -!- PATHWAY: Glycan biosynthesis; alginate biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:12003941,
CC ECO:0000269|PubMed:8636017}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:12003941, ECO:0000269|PubMed:8636017}.
CC -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
CC {ECO:0000305}.
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DR EMBL; U50202; AAB09781.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG06936.1; -; Genomic_DNA.
DR PIR; A83203; A83203.
DR RefSeq; NP_252238.1; NC_002516.2.
DR RefSeq; WP_003112884.1; NZ_QZGE01000001.1.
DR AlphaFoldDB; Q51392; -.
DR SMR; Q51392; -.
DR STRING; 287.DR97_4394; -.
DR PaxDb; Q51392; -.
DR EnsemblBacteria; AAG06936; AAG06936; PA3548.
DR GeneID; 877959; -.
DR KEGG; pae:PA3548; -.
DR PATRIC; fig|208964.12.peg.3713; -.
DR PseudoCAP; PA3548; -.
DR HOGENOM; CLU_025255_1_3_6; -.
DR InParanoid; Q51392; -.
DR OMA; IIWGAWH; -.
DR PhylomeDB; Q51392; -.
DR BioCyc; MetaCyc:MON-19201; -.
DR BioCyc; PAER208964:G1FZ6-3616-MON; -.
DR UniPathway; UPA00286; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016746; F:acyltransferase activity; IBA:GO_Central.
DR GO; GO:0051979; P:alginic acid acetylation; IMP:PseudoCAP.
DR GO; GO:0042121; P:alginic acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR024194; Ac/AlaTfrase_AlgI/DltB.
DR InterPro; IPR028362; AlgI.
DR InterPro; IPR004299; MBOAT_fam.
DR Pfam; PF03062; MBOAT; 1.
DR PIRSF; PIRSF500217; AlgI; 1.
DR PIRSF; PIRSF016636; AlgI_DltB; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Alginate biosynthesis; Cell inner membrane; Cell membrane;
KW Membrane; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..520
FT /note="Probable alginate O-acetylase AlgI"
FT /id="PRO_0000213124"
FT TRANSMEM 7..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 39..61
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 78..100
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..137
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..172
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..261
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 311..333
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 353..375
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 402..424
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 483..505
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 322
FT /evidence="ECO:0000255"
FT CONFLICT 360..361
FT /note="VI -> AF (in Ref. 1; AAB09781)"
FT /evidence="ECO:0000305"
FT CONFLICT 403
FT /note="N -> S (in Ref. 1; AAB09781)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 520 AA; 58746 MW; 29146A26A2C6738B CRC64;
MVFSSNVFLF LFLPVFLGLY YLSGERYRNL LLLIASYVFY AWWRVDFLLL FAGVTVFNYW
IGLRIGAAGV RTRAAQRWLI LGVVVDLCVL GYFKYANFGV DSLNEIITSF GMQPFVLTHI
LLPIGISFYT FESISYIIDV YRGDTPATHN LIDFAAFVAI FPHLIAGPVL RFKDLVDQFN
HRTHTVDKFA EGCTRFMQGF VKKVFIADTL AALADHCFAL QNPTTGDAWL GALAYTAQLY
FDFSGYSDMA IGLGLMMGFR FMENFNQPYI SQSITEFWRR WHISLSTWLR DYLYISLGGN
RGSTFQTYRN LFLTMLLGGL WHGANFTYII WGAWHGMWLA IERALGVNAA PRVLNPLKWV
ITFLLVVIGW VIFRAENLQV AWRMYEAMFS FGTWQLSELN RANLTGLQVG TLVLAYLVLA
FFGLRQFYNQ PLQTKAPKAA ANSDEVAADG PASAQPRAPR EAAGDPAAIA YSPSGALVYQ
PSWLSQLPVL ATRLALLLLF AASVLKLSAQ SYSPFLYFQF
