ALGJ_PSEPK
ID ALGJ_PSEPK Reviewed; 385 AA.
AC Q88ND3;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2003, sequence version 2.
DT 25-MAY-2022, entry version 101.
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=PP_1279;
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: 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 the ability of alginate to act
CC as a defense barrier (By similarity). {ECO:0000250}.
CC -!- PATHWAY: Glycan biosynthesis; alginate biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}; Periplasmic side {ECO:0000250}.
CC Periplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the AlgJ family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN66903.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE015451; AAN66903.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_743439.1; NC_002947.4.
DR RefSeq; WP_049587323.1; NC_002947.4.
DR PDB; 4O8V; X-ray; 1.82 A; A/B=75-370.
DR PDBsum; 4O8V; -.
DR AlphaFoldDB; Q88ND3; -.
DR SMR; Q88ND3; -.
DR STRING; 160488.PP_1279; -.
DR EnsemblBacteria; AAN66903; AAN66903; PP_1279.
DR KEGG; ppu:PP_1279; -.
DR PATRIC; fig|160488.4.peg.1356; -.
DR eggNOG; ENOG502Z851; Bacteria.
DR HOGENOM; CLU_057510_0_0_6; -.
DR OMA; FNEGRPG; -.
DR PhylomeDB; Q88ND3; -.
DR UniPathway; UPA00286; -.
DR Proteomes; UP000000556; 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:0042121; P:alginic acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd14442; AlgJ_like; 1.
DR InterPro; IPR034657; AlgJ.
DR InterPro; IPR031811; ALGX/ALGJ_SGNH-like.
DR Pfam; PF16822; ALGX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Alginate biosynthesis; Cell inner membrane;
KW Cell membrane; Membrane; Periplasm; Reference proteome; Signal;
KW Transferase.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..385
FT /note="Probable alginate O-acetylase AlgJ"
FT /id="PRO_0000001122"
FT ACT_SITE 190
FT /evidence="ECO:0000250"
FT ACT_SITE 192
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 288
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:4O8V"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:4O8V"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:4O8V"
FT HELIX 101..121
FT /evidence="ECO:0007829|PDB:4O8V"
FT STRAND 125..131
FT /evidence="ECO:0007829|PDB:4O8V"
FT HELIX 134..137
FT /evidence="ECO:0007829|PDB:4O8V"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:4O8V"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:4O8V"
FT HELIX 154..164
FT /evidence="ECO:0007829|PDB:4O8V"
FT HELIX 173..179
FT /evidence="ECO:0007829|PDB:4O8V"
FT TURN 180..182
FT /evidence="ECO:0007829|PDB:4O8V"
FT STRAND 188..193
FT /evidence="ECO:0007829|PDB:4O8V"
FT HELIX 195..211
FT /evidence="ECO:0007829|PDB:4O8V"
FT STRAND 222..232
FT /evidence="ECO:0007829|PDB:4O8V"
FT HELIX 235..239
FT /evidence="ECO:0007829|PDB:4O8V"
FT HELIX 244..249
FT /evidence="ECO:0007829|PDB:4O8V"
FT STRAND 254..263
FT /evidence="ECO:0007829|PDB:4O8V"
FT STRAND 281..285
FT /evidence="ECO:0007829|PDB:4O8V"
FT HELIX 288..291
FT /evidence="ECO:0007829|PDB:4O8V"
FT HELIX 293..295
FT /evidence="ECO:0007829|PDB:4O8V"
FT HELIX 297..305
FT /evidence="ECO:0007829|PDB:4O8V"
FT STRAND 315..317
FT /evidence="ECO:0007829|PDB:4O8V"
FT HELIX 320..327
FT /evidence="ECO:0007829|PDB:4O8V"
FT HELIX 330..334
FT /evidence="ECO:0007829|PDB:4O8V"
FT STRAND 338..345
FT /evidence="ECO:0007829|PDB:4O8V"
FT HELIX 346..348
FT /evidence="ECO:0007829|PDB:4O8V"
FT HELIX 360..367
FT /evidence="ECO:0007829|PDB:4O8V"
SQ SEQUENCE 385 AA; 42675 MW; 34180471D46476FD CRC64;
MTRTLRITYS LSFLGLLVGM GAWSTGGLQS FQRTEQMTLL NGKLAKAAET HYDAEFPIKR
LGTNVWAAMD FKLFNEGRPG VVLGRDQWLF SDEEFKPTAG AEQLMQENLA LIRGVRDTLQ
QHGSQLVLAI VPAKARVYTE YLGKERPASL HDDLYNQFHA QARQANVFAP DLMAPMEQAK
ARGQVFLRTD THWTPMGAEV AAQALAEAVS RQSLLNGDPQ AFITEAGNTA PYKGDLTNFL
PLDPLFSNLL PAPDNLQKRT TRPVDAEGDA GDALFADKQI PVALVGTSYS ANPHWNFLGA
LQQALRSDVA NYAEDGHGPL LPMLKYLQSD AFKNAAPQVV VWEFPERYLP MKNDLSSFDP
QWIAQLKNSR KSEENLALSS TRTDH
