WZZB_SALTY
ID WZZB_SALTY Reviewed; 327 AA.
AC Q04866;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Chain length determinant protein;
DE AltName: Full=Polysaccharide antigen chain regulator;
GN Name=wzzB; Synonyms=cld, rol; OrderedLocusNames=STM2079;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT2;
RX PubMed=7682279; DOI=10.1111/j.1365-2958.1993.tb01163.x;
RA Bastin D.A., Stevenson G., Brown P.K., Haase A., Reeves P.R.;
RT "Repeat unit polysaccharides of bacteria: a model for polymerization
RT resembling that of ribosomes and fatty acid synthetase, with a novel
RT mechanism for determining chain length.";
RL Mol. Microbiol. 7:725-734(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT2;
RX PubMed=1379582; DOI=10.1128/jb.174.16.5228-5236.1992;
RA Batchelor R.A., Alifano P., Biffali E., Hull S.I., Hull R.A.;
RT "Nucleotide sequences of the genes regulating O-polysaccharide antigen
RT chain length (rol) from Escherichia coli and Salmonella typhimurium:
RT protein homology and functional complementation.";
RL J. Bacteriol. 174:5228-5236(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
CC -!- FUNCTION: Confers a modal distribution of chain length on the O-antigen
CC component of lipopolysaccharide (LPS). Gives rise to a reduced number
CC of short chain molecules and increases in numbers of longer molecules,
CC with a modal value of 20.
CC -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC biosynthesis.
CC -!- INTERACTION:
CC Q04866; Q04866: wzzB; NbExp=4; IntAct=EBI-15680694, EBI-15680694;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the WzzB/Cld/Rol family. {ECO:0000305}.
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DR EMBL; Z17278; CAA78946.1; -; Genomic_DNA.
DR EMBL; M89933; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AE006468; AAL20983.1; -; Genomic_DNA.
DR RefSeq; NP_461024.1; NC_003197.2.
DR RefSeq; WP_000215261.1; NC_003197.2.
DR PDB; 3B8P; X-ray; 3.10 A; A/B/C/D/E=54-294.
DR PDB; 4E29; X-ray; 1.60 A; A/B=201-293.
DR PDB; 4E2C; X-ray; 2.80 A; A/B=256-291.
DR PDBsum; 3B8P; -.
DR PDBsum; 4E29; -.
DR PDBsum; 4E2C; -.
DR AlphaFoldDB; Q04866; -.
DR SMR; Q04866; -.
DR DIP; DIP-46396N; -.
DR STRING; 99287.STM2079; -.
DR PaxDb; Q04866; -.
DR EnsemblBacteria; AAL20983; AAL20983; STM2079.
DR GeneID; 1253600; -.
DR KEGG; stm:STM2079; -.
DR PATRIC; fig|99287.12.peg.2201; -.
DR HOGENOM; CLU_060925_1_1_6; -.
DR OMA; IIAKLWR; -.
DR PhylomeDB; Q04866; -.
DR BioCyc; SENT99287:STM2079-MON; -.
DR UniPathway; UPA00030; -.
DR EvolutionaryTrace; Q04866; -.
DR PHI-base; PHI:3728; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
DR DisProt; DP02596; -.
DR InterPro; IPR003856; LPS_length_determ_N_term.
DR Pfam; PF02706; Wzz; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane;
KW Lipopolysaccharide biosynthesis; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..327
FT /note="Chain length determinant protein"
FT /id="PRO_0000065993"
FT TOPO_DOM 1..31
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 53..294
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 295..315
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 316..327
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CONFLICT 50
FT /note="M -> I (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 136
FT /note="Y -> D (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 158..159
FT /note="EV -> QL (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 164
FT /note="E -> Q (in Ref. 2)"
FT /evidence="ECO:0000305"
FT STRAND 56..63
FT /evidence="ECO:0007829|PDB:3B8P"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:3B8P"
FT HELIX 71..81
FT /evidence="ECO:0007829|PDB:3B8P"
FT HELIX 88..111
FT /evidence="ECO:0007829|PDB:3B8P"
FT STRAND 112..115
FT /evidence="ECO:0007829|PDB:3B8P"
FT STRAND 118..125
FT /evidence="ECO:0007829|PDB:3B8P"
FT STRAND 132..140
FT /evidence="ECO:0007829|PDB:3B8P"
FT HELIX 141..199
FT /evidence="ECO:0007829|PDB:3B8P"
FT HELIX 201..210
FT /evidence="ECO:0007829|PDB:4E29"
FT TURN 225..227
FT /evidence="ECO:0007829|PDB:4E29"
FT HELIX 228..231
FT /evidence="ECO:0007829|PDB:4E29"
FT HELIX 233..241
FT /evidence="ECO:0007829|PDB:4E29"
FT HELIX 243..245
FT /evidence="ECO:0007829|PDB:4E29"
FT HELIX 252..266
FT /evidence="ECO:0007829|PDB:4E29"
FT TURN 271..273
FT /evidence="ECO:0007829|PDB:3B8P"
FT STRAND 278..281
FT /evidence="ECO:0007829|PDB:4E29"
SQ SEQUENCE 327 AA; 36259 MW; 72D8BA8A3F4DF1A9 CRC64;
MTVDSNTSSG RGNDPEQIDL IELLLQLWRG KMTIIVAVII AILLAVGYLM IAKEKWTSTA
IITQPDAAQV ATYTNALNVL YGGNAPKISE VQANFISRFS SAFSALSEVL DNQKEREKLT
IEQSVKGQAL PLSVSYVSTT AEGAQRRLAE YIQQVDEEVA KELEVDLKDN ITLQTKTLQE
SLETQEVVAQ EQKDLRIKQI EEALRYADEA KITQPQIQQT QDVTQDTMFL LGSDALKSMI
QNEATRPLVF SPAYYQTKQT LLDIKNLKVT ADTVHVYRYV MKPTLPVRRD SPKTAITLVL
AVLLGGMIGA GIVLGRNALR SYKPKAL
