WZZB_ECOLI
ID WZZB_ECOLI Reviewed; 326 AA.
AC P76372; O07997; O07998; P77049;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Chain length determinant protein;
DE AltName: Full=Polysaccharide antigen chain regulator;
GN Name=wzzB; Synonyms=cld, rol, wzz; OrderedLocusNames=b2027, JW5836;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / DH5-alpha;
RA Klee S.R., Tzschaschel B.D., Timmis K.N., Guzman C.A.;
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=BL21-DE3;
RX PubMed=16079137; DOI=10.1074/jbc.m506479200;
RA Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L.,
RA von Heijne G., Daley D.O.;
RT "Protein complexes of the Escherichia coli cell envelope.";
RL J. Biol. Chem. 280:34409-34419(2005).
RN [6]
RP SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
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 -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC biosynthesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16079137}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996,
CC ECO:0000269|PubMed:16079137}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:16079137}.
CC -!- SIMILARITY: Belongs to the WzzB/Cld/Rol family. {ECO:0000305}.
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DR EMBL; Y07559; CAA68844.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75088.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA15859.1; -; Genomic_DNA.
DR RefSeq; NP_416531.4; NC_000913.3.
DR RefSeq; WP_001393575.1; NZ_LN832404.1.
DR PDB; 6RBG; EM; 3.00 A; A/B/C/D/E/F/G/H=1-326.
DR PDBsum; 6RBG; -.
DR AlphaFoldDB; P76372; -.
DR SMR; P76372; -.
DR BioGRID; 4261360; 332.
DR STRING; 511145.b2027; -.
DR jPOST; P76372; -.
DR PaxDb; P76372; -.
DR PRIDE; P76372; -.
DR EnsemblBacteria; AAC75088; AAC75088; b2027.
DR EnsemblBacteria; BAA15859; BAA15859; BAA15859.
DR GeneID; 946553; -.
DR KEGG; ecj:JW5836; -.
DR KEGG; eco:b2027; -.
DR PATRIC; fig|1411691.4.peg.225; -.
DR EchoBASE; EB3182; -.
DR eggNOG; COG3765; Bacteria.
DR HOGENOM; CLU_060925_1_1_6; -.
DR InParanoid; P76372; -.
DR OMA; IIAKLWR; -.
DR PhylomeDB; P76372; -.
DR BioCyc; EcoCyc:G7090-MON; -.
DR UniPathway; UPA00030; -.
DR PRO; PR:P76372; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; 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:0004713; F:protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
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..326
FT /note="Chain length determinant protein"
FT /id="PRO_0000065992"
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..295
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 296..316
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 317..326
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:6RBG"
FT HELIX 26..29
FT /evidence="ECO:0007829|PDB:6RBG"
FT HELIX 32..48
FT /evidence="ECO:0007829|PDB:6RBG"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:6RBG"
FT STRAND 57..63
FT /evidence="ECO:0007829|PDB:6RBG"
FT TURN 67..69
FT /evidence="ECO:0007829|PDB:6RBG"
FT HELIX 71..79
FT /evidence="ECO:0007829|PDB:6RBG"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:6RBG"
FT TURN 88..90
FT /evidence="ECO:0007829|PDB:6RBG"
FT HELIX 91..95
FT /evidence="ECO:0007829|PDB:6RBG"
FT HELIX 97..103
FT /evidence="ECO:0007829|PDB:6RBG"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:6RBG"
FT STRAND 107..110
FT /evidence="ECO:0007829|PDB:6RBG"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:6RBG"
FT STRAND 119..129
FT /evidence="ECO:0007829|PDB:6RBG"
FT STRAND 131..137
FT /evidence="ECO:0007829|PDB:6RBG"
FT STRAND 139..142
FT /evidence="ECO:0007829|PDB:6RBG"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:6RBG"
FT HELIX 146..159
FT /evidence="ECO:0007829|PDB:6RBG"
FT HELIX 161..174
FT /evidence="ECO:0007829|PDB:6RBG"
FT HELIX 176..179
FT /evidence="ECO:0007829|PDB:6RBG"
FT TURN 181..183
FT /evidence="ECO:0007829|PDB:6RBG"
FT HELIX 184..209
FT /evidence="ECO:0007829|PDB:6RBG"
FT HELIX 227..232
FT /evidence="ECO:0007829|PDB:6RBG"
FT HELIX 234..237
FT /evidence="ECO:0007829|PDB:6RBG"
FT HELIX 239..242
FT /evidence="ECO:0007829|PDB:6RBG"
FT HELIX 255..267
FT /evidence="ECO:0007829|PDB:6RBG"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:6RBG"
FT STRAND 279..282
FT /evidence="ECO:0007829|PDB:6RBG"
FT HELIX 297..323
FT /evidence="ECO:0007829|PDB:6RBG"
SQ SEQUENCE 326 AA; 36455 MW; 9D4DA2A9E5E7E8F8 CRC64;
MRVENNNVSG QNHDPEQIDL IDLLVQLWRG KMTIIISVIV AIALAIGYLA VAKEKWTSTA
IITQPDVGQI AGYNNAMNVI YGQAAPKVSD LQETLIGRFS SAFSALAETL DNQEEREKLT
IEPSVKNQQL PLTVSYVGQT AEGAQMKLAQ YIQQVDDKVN QELEKDLKDN IALGRKNLQD
SLRTQEVVAQ EQKDLRIRQI QEALQYANQA QVTKPQIQQT GEDITQDTLF LLGSEALESM
IKHEATRPLV FSPNYYQTRQ NLLDIESLKV DDLDIHAYRY VMKPMLPIRR DSPKKAITLI
LAVLLGGMVG AGIVLGRNAL RNYNAK
