ALGJ_PSEAE
ID ALGJ_PSEAE Reviewed; 391 AA.
AC Q51393;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Probable alginate O-acetylase AlgJ;
DE EC=2.3.1.-;
DE AltName: Full=Alginate biosynthesis protein AlgJ;
DE Flags: Precursor;
GN Name=algJ; OrderedLocusNames=PA3549;
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=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).
CC -!- FUNCTION: Together with AlgI 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.
CC -!- PATHWAY: Glycan biosynthesis; alginate biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:12003941}; Peripheral membrane protein
CC {ECO:0000269|PubMed:12003941}; Periplasmic side
CC {ECO:0000269|PubMed:12003941}. Periplasm {ECO:0000269|PubMed:12003941}.
CC -!- SIMILARITY: Belongs to the AlgJ family. {ECO:0000305}.
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DR EMBL; U50202; AAB09782.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG06937.1; -; Genomic_DNA.
DR PIR; B83203; B83203.
DR RefSeq; NP_252239.1; NC_002516.2.
DR RefSeq; WP_003092111.1; NZ_QZGE01000001.1.
DR AlphaFoldDB; Q51393; -.
DR SMR; Q51393; -.
DR STRING; 287.DR97_4393; -.
DR PaxDb; Q51393; -.
DR EnsemblBacteria; AAG06937; AAG06937; PA3549.
DR GeneID; 878716; -.
DR KEGG; pae:PA3549; -.
DR PATRIC; fig|208964.12.peg.3714; -.
DR PseudoCAP; PA3549; -.
DR HOGENOM; CLU_057510_0_0_6; -.
DR OMA; FNEGRPG; -.
DR PhylomeDB; Q51393; -.
DR BioCyc; MetaCyc:MON-19199; -.
DR BioCyc; PAER208964:G1FZ6-3617-MON; -.
DR UniPathway; UPA00286; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0051979; P:alginic acid acetylation; IDA:PseudoCAP.
DR GO; GO:0042121; P:alginic acid biosynthetic process; IDA:PseudoCAP.
DR CDD; cd14442; AlgJ_like; 1.
DR InterPro; IPR034657; AlgJ.
DR InterPro; IPR031811; ALGX/ALGJ_SGNH-like.
DR Pfam; PF16822; ALGX; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Alginate biosynthesis; Cell inner membrane; Cell membrane;
KW Membrane; Periplasm; Reference proteome; Signal; Transferase.
FT SIGNAL 1..39
FT /evidence="ECO:0000255"
FT CHAIN 40..391
FT /note="Probable alginate O-acetylase AlgJ"
FT /id="PRO_0000001120"
FT REGION 259..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 193
FT /evidence="ECO:0000250"
FT ACT_SITE 195
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 297
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
SQ SEQUENCE 391 AA; 43107 MW; AE048823947D5503 CRC64;
MTQSISRPLQ YAYIAAFGGL LLGLAGWSLK SVPGFSAAAD TPLLNGKLAH AFEAHYDKEF
PIKRLGTNLW AALDYTLFHE GRPGVVIGKD GWLFTDEEFK PAPSGQQLED NWALVRGVQR
ELNRRGVKLV LAVIPAKARL YPEHIGREQP AALHDSLYQD FLARARAAGI DSPDLLGSLR
QAKDNGAVFL RTDTHWSPLG AETVAQRLGA EIRETHLLDV PAQNFVTRVG EERTHKGDLL
SFLPLDPLFD ELLPRPEQLQ QRTTEAAPAL PGGQQSGAGD DLFGDSQQPR LALVGTSYSA
NPRWNFEGAL KQALSADLIN YAKEGKGPLE PMLELLQDEG FRKDPPQLLV WEFPERYLPM
ASDLSQFDAD WVAQLKASGG RDERLAASRN D