ALGK_AZOVI
ID ALGK_AZOVI Reviewed; 460 AA.
AC P94202;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 2.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=Alginate biosynthesis protein AlgK;
DE Flags: Precursor;
GN Name=algK;
OS Azotobacter vinelandii.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Azotobacter.
OX NCBI_TaxID=354;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 9046;
RX PubMed=9368366; DOI=10.1111/j.1574-6968.1997.tb12712.x;
RA Mejia-Ruiz H., Moreno S., Guzman J., Najera R., Leon R., Soberon-Chavez G.,
RA Espin G.;
RT "Isolation and characterization of an Azotobacter vinelandii algK mutant.";
RL FEMS Microbiol. Lett. 156:101-106(1997).
CC -!- FUNCTION: May be involved in the polymerization of mannuronate to
CC alginate.
CC -!- PATHWAY: Glycan biosynthesis; alginate biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000250}; Lipid-anchor
CC {ECO:0000255|PROSITE-ProRule:PRU00303}; Periplasmic side {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Cells do not encyst.
CC {ECO:0000269|PubMed:9368366}.
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; X98863; CAA67370.1; -; Genomic_DNA.
DR AlphaFoldDB; P94202; -.
DR SMR; P94202; -.
DR UniPathway; UPA00286; -.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042121; P:alginic acid biosynthetic process; IEA:UniProtKB-UniPathway.
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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Alginate biosynthesis; Cell outer membrane; Lipoprotein; Membrane;
KW Palmitate; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 18..460
FT /note="Alginate biosynthesis protein AlgK"
FT /id="PRO_0000020666"
FT LIPID 18
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 18
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ SEQUENCE 460 AA; 50987 MW; 467E5BC188E77921 CRC64;
MNLTKPLLLS ALAGLTACAN LDLPDQRLAK EALQRGDTQT AERHFRQLAD MGFTEAQLGL
ADMQLASGDP EQLRKAEQTY RMALDASPRA KARLGKLLAY KPTSSEAEKR EAAQLLSDAF
AAGEDGVLLP LAMLYLKNPQ TFPDVSLQQR IDQWRAAGHP QADIAQIVVY RTQGTYDQHL
DDIERICQQR LAEHSDCYVE LATVYLQARP EWTRTTACRA WCNSSWPLMA AHRAGGVSAQ
LVTEVAGVLS NPLLGQSNEK TAQTMLEEIA PPPGSVWRVL IYDFPGTGDT DQMLDYLAWP
CAAQPAADLL LGRLYYEGKL LPQDPFKAEE YFIKARATEN SAHYYLGQIY RRGFLGEVYP
QKAVDSLLTA ARGGQASADY ALAQLYSQGR GIRIDLANAY VFARLAVLQG RPDSEPLLQE
IKANLAPAER TRGEQMLHAE QQARYGVWQT STQLQAMQNQ