ALGK_PSEAE
ID ALGK_PSEAE Reviewed; 475 AA.
AC P96956; O52506;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Alginate biosynthesis protein AlgK;
DE Flags: Precursor;
GN Name=algK; OrderedLocusNames=PA3543;
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=8830;
RX PubMed=9043140; DOI=10.1099/00221287-143-2-641;
RA Aarons S.J., Sutherland I.W., Chakrabarty A.M., Gallagher M.P.;
RT "A novel gene, algK, from the alginate biosynthesis cluster of Pseudomonas
RT aeruginosa.";
RL Microbiology 143:641-652(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=FRD1;
RX PubMed=9457868; DOI=10.1128/jb.180.3.634-641.1998;
RA Jain S., Ohman D.E.;
RT "Deletion of algK in mucoid Pseudomonas aeruginosa blocks alginate polymer
RT formation and results in uronic acid secretion.";
RL J. Bacteriol. 180:634-641(1998).
RN [3]
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 [4]
RP INTERACTION WITH ALGX, AND SUBCELLULAR LOCATION.
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).
CC -!- FUNCTION: May be involved in the polymerization of mannuronate to
CC alginate. {ECO:0000269|PubMed:9457868}.
CC -!- PATHWAY: Glycan biosynthesis; alginate biosynthesis.
CC -!- SUBUNIT: Interacts with AlgX. {ECO:0000269|PubMed:21713511}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000305|PubMed:21713511,
CC ECO:0000305|PubMed:9457868}; Lipid-anchor {ECO:0000305|PubMed:21713511,
CC ECO:0000305|PubMed:9457868}; Periplasmic side
CC {ECO:0000305|PubMed:21713511, ECO:0000305|PubMed:9457868}.
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 high levels of dialyzable and low-molecular-weight uronic acids.
CC {ECO:0000269|PubMed:9457868}.
CC -!- SIMILARITY: Belongs to the AlgK family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X99206; CAA67592.1; -; Genomic_DNA.
DR EMBL; AF039535; AAC38141.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG06931.1; -; Genomic_DNA.
DR PIR; D83202; D83202.
DR RefSeq; NP_252233.1; NC_002516.2.
DR RefSeq; WP_003112887.1; NZ_QZGE01000001.1.
DR AlphaFoldDB; P96956; -.
DR SMR; P96956; -.
DR STRING; 287.DR97_4399; -.
DR PaxDb; P96956; -.
DR EnsemblBacteria; AAG06931; AAG06931; PA3543.
DR GeneID; 878771; -.
DR KEGG; pae:PA3543; -.
DR PATRIC; fig|208964.12.peg.3707; -.
DR PseudoCAP; PA3543; -.
DR HOGENOM; CLU_595617_0_0_6; -.
DR OMA; ICYVELA; -.
DR PhylomeDB; P96956; -.
DR BioCyc; PAER208964:G1FZ6-3611-MON; -.
DR UniPathway; UPA00286; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042121; P:alginic acid biosynthetic process; IDA:PseudoCAP.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR006597; Sel1-like.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR SMART; SM00671; SEL1; 4.
PE 1: Evidence at protein level;
KW Alginate biosynthesis; Cell outer membrane; Lipoprotein; Membrane;
KW Palmitate; Reference proteome; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..475
FT /note="Alginate biosynthesis protein AlgK"
FT /id="PRO_0000020667"
FT REGION 436..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..469
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 28
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT LIPID 28
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255"
FT CONFLICT 78
FT /note="S -> R (in Ref. 1; AAC38141)"
FT /evidence="ECO:0000305"
FT CONFLICT 177
FT /note="L -> F (in Ref. 1; AAC38141)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 475 AA; 52475 MW; FBE59323A425AC62 CRC64;
MKMPILPPLP LASRHLLLAS AIALAAGCAG LPDQRLAQEA LERGDLATAQ SNYQALAAMG
YADAQVGLAD MQVASGDSAQ QAKAEKLYRE AAQTSPRARA RLGKWLAAKP GASDAEHREA
ERLLSQAFEQ GEDSALVPLI VLYLQYPQSW PEIDPQQRID QWRARGLPQA DLAQIILYRT
QGTYAQHLGE IEQVCQRWLR RMDVCWYELA TVYQMQGNAE KQKVLLEQLR AAYKAGRVPG
ERVDSVAGVL ADGELGQPDP QTAQALLEEI APSYPAAWVS LAKLLYDYPD QGDLEKMLGY
LKNAQDAAQP RAELLLGRLY YDGKWAPQDP RKAERHLLKA AASEPQANYY LGQIYRRGFL
GKVYPQKAVD HLILAARAGQ ASADMALAQL WSQGRGIQPN RVNAYVFGQL AVQQQVPQAS
DLLGQIEAQL PPAERSQAQQ LLKREQQSRG NNWQATVSLL QSQDSPINEE EPESL
